Journal articles: 'STM1'

1

Ligr, Martin, Iris Velten, Eleonore Fröhlich, Frank Madeo, Matthias Ledig, Kai-Uwe Fröhlich, Dieter H. Wolf, and Wolfgang Hilt. "The Proteasomal Substrate Stm1 Participates in Apoptosis-like Cell Death in Yeast." Molecular Biology of the Cell 12, no. 8 (August 2001): 2422–32. http://dx.doi.org/10.1091/mbc.12.8.2422.

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We have identified the yeast gene STM1 in an overexpression screen for new proteasomal substrates. Stm1 is unstable in wild-type cells and stabilized in cells with defective proteasomal activity and thus a bona fide substrate of the proteasome. It is localized in the perinuclear region and is required for growth in the presence of mutagens. Overexpression in cells with impaired proteasomal degradation leads to cell death accompanied with cytological markers of apoptosis: loss of plasma membrane asymmetry, chromatin condensation, and DNA cleavage. Cells lacking Stm1 display deficiency in the apoptosis-like cell death process induced by treatment with low concentrations of H2O2. We suggest that Stm1 is involved in the control of the apoptosis-like cell death in yeast. Survival is increased when Stm1 is completely missing from the cells or when inhibition of Stm1 synthesis permits proteasomal degradation to decrease its amount in the cell. Conversely, Stm1 accumulation induces cell death. In addition we identified five other genes whose overexpression in proteasomal mutants caused similar apoptotic phenotypes.

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Barlow, Blake R., Lovreet S. Shergill, Mandy D. Bish, and Kevin W. Bradley. "Investigations of the Potential Interactions Between Pre-emergence Residual Herbicides, Variety, and Seed Treatments in Soybean." Weed Technology 32, no. 5 (September 24, 2018): 570–78. http://dx.doi.org/10.1017/wet.2018.44.

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AbstractField experiments were performed in 2016 and 2017 in Missouri to determine whether interactions exist between PRE herbicides and seed treatments in soybean. The experiments consisted of a randomized complete block design with factorial arrangements of varieties, seed treatments, and herbicides. We selected two genetically similar varieties of soybean, one with known tolerance to PPO-inhibiting herbicides and one with known sensitivity. Each variety of seed received three separate seed treatment mixtures (STMs): (1) STM1, imidacloprid plus prothioconazol+penflufen+metalaxyl plus metalaxyl plusBacillus subtilis+B. pumilis, (2) STM2,Pasteuria nishizawaeplus thiamethoxam plus prothioconazol+penflufen+metalaxyl plus metalaxyl plusB. subtilis+B. pumilis, and (3) STM3, fluopyram plus imidacloprid plus prothioconazol+penflufen+metalaxyl plus metalaxyl plusB. subtilis+B. pumilis. Chlorimuron-ethyl+flumioxazin+pyroxasulfone, chlorimuron-ethyl+flumioxazin+metribuzin, and chlorimuron-ethyl+sulfentrazone were applied PRE to each variety and seed treatment combination at 1× and 2× the labeled use rate. Chlorimuron-ethyl+sulfentrazone treatment at the 2× rate resulted in greater injury of 8% and 14% to the sensitive variety than the tolerant in 2016 and 2017, respectively; this was the highest injury observed from any herbicide treatment in either year. In 2017, chlorimuron-ethyl+sulfentrazone resulted in the greatest height reductions in both varieties, but this reduction was more evident in the sensitive (19%) than in the tolerant (6%) variety. Overall, yield differences between the two varieties were not consistent between years, and for both varieties, the sulfentrazone-containing treatments resulted in the highest yield losses. The results of this research indicate that there is a larger interaction between herbicides and varieties than there is between herbicides and seed treatments, or seed treatments and varieties.

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Bachtiar, Endang W., Kuo-Ching Sheng, Theodora Fifis, Anita Gamvrellis, Magdalena Plebanski, Peter J. Coloe, and Peter M. Smooker. "Delivery of a heterologous antigen by a registeredSalmonellavaccine (STM1)." FEMS Microbiology Letters 227, no. 2 (October 2003): 211–17. http://dx.doi.org/10.1016/s0378-1097(03)00683-9.

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4

Kumar, Chandrakesh, and Rajan Mishra. "Miniaturized Dual Band Meander Antenna For WLAN/STM1 Application." i-manager's Journal on Communication Engineering and Systems 4, no. 3 (July 15, 2015): 20–24. http://dx.doi.org/10.26634/jcs.4.3.3454.

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5

Balagopal, V., and R. Parker. "Stm1 modulates translation after 80S formation in Saccharomyces cerevisiae." RNA 17, no. 5 (April 1, 2011): 835–42. http://dx.doi.org/10.1261/rna.2677311.

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6

Balagopal, Vidya, and Roy Parker. "Stm1 Modulates mRNA Decay and Dhh1 Function in Saccharomyces cerevisiae." Genetics 181, no. 1 (November 17, 2008): 93–103. http://dx.doi.org/10.1534/genetics.108.092601.

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Hata, Hiroaki, Hisayuki Mitsui, Hong Liu, Yongli Bai, Clyde L. Denis, Yuki Shimizu, and Akira Sakai. "Dhh1p, a Putative RNA Helicase, Associates with the General Transcription Factors Pop2p and Ccr4p from Saccharomyces cerevisiae." Genetics 148, no. 2 (February 1, 1998): 571–79. http://dx.doi.org/10.1093/genetics/148.2.571.

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Abstract The POP2 (Caf1) protein in Saccharomyces cerevisiae affects a variety of transcriptional processes and is a component of the Ccr4p complex. We have isolated five multicopy suppressor genes of a pop2 deletion mutation: CCR4, DHH1 (a putative RNA helicase), PKC1, STM1, and MPT5 (multicopy suppressor of pop two). Overexpression of either the CCR4 or DHH1 genes effectively suppressed phenotypes associated with pop2 mutant cells; overexpression of PKC1, STM1, or MPT5 genes produced only partial suppression. Disruption of the CCR4 or DHH1 genes resulted in phenotypes similar to those observed for pop2 cells. In addition, overexpression of the DHH1 gene also suppressed the ccr4 mutation, suggesting a close relationship between the POP2, CCR4, and DHH1 genes. Two-hybrid analysis and coimmunoprecipitation experiments revealed that Pop2p and Dhh1p interact physically, and these and other data suggest that Dhh1p is also a component of the Ccr4p complex. Finally, we investigated the genetic interaction between factors associated with POP2 and the PKC1 pathway. The temperature-sensitive growth defect of dhh1 or mpt5 cells was suppressed by overexpression of PKC1, and the defect of mpk1 cells was suppressed by overexpression of MPT5. These results and phenotypic analysis of double mutants from the POP2 and PKC1 pathways suggested that the POP2 and the PKC1 pathways are independent but have some overlapping functions.

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8

Hayashi, Hikari, Riku Nagai, Taisho Abe, Miki Wada, Koichi Ito, and Nono Takeuchi-Tomita. "Tight interaction of eEF2 in the presence of Stm1 on ribosome." Journal of Biochemistry 163, no. 3 (October 23, 2017): 177–85. http://dx.doi.org/10.1093/jb/mvx070.

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9

Katayama, T., N. Inoue, and H. Torigoe. "Location of the triplex DNA-binding domain of Saccharomyces cerevisiae Stm1 protein." Nucleic Acids Symposium Series 51, no. 1 (November 1, 2007): 123–24. http://dx.doi.org/10.1093/nass/nrm062.

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10

Hayashi, N., and S. Murakami. "STM1, a gene which encodes a guanine quadruplex binding protein, interacts with CDC13 in Saccharomyces cerevisiae." Molecular Genetics and Genomics 267, no. 6 (August 2002): 806–13. http://dx.doi.org/10.1007/s00438-002-0712-3.

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Katayama, T., and H. Torigoe. "The interaction between the purine motif triplex and the triplex DNA-binding domain of Saccharomyces cerevisiae Stm1 protein." Nucleic Acids Symposium Series 52, no. 1 (September 1, 2008): 111–12. http://dx.doi.org/10.1093/nass/nrn057.

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12

Kawano-Kawada, Miyuki, Taisuke Ueda, Hikari Mori, Haruka Ichimura, Kaoru Takegawa, and Takayuki Sekito. "Stm1 is a vacuolar PQ-loop protein involved in the transport of basic amino acids in Schizosaccharomyces pombe." Biochimica et Biophysica Acta (BBA) - Biomembranes 1863, no. 2 (February 2021): 183507. http://dx.doi.org/10.1016/j.bbamem.2020.183507.

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13

Chung, Kyung-Sook, Misun Won, Jung-Joon Lee, Jiwon Ahn, Kwang-Lae Hoe, Dong-Uk Kim, Kyung-Bin Song, and Hyang-Sook Yoo. "Yeast-based screening to identify modulators of G-protein signaling using uncontrolled cell division cycle by overexpression of Stm1." Journal of Biotechnology 129, no. 3 (May 2007): 547–54. http://dx.doi.org/10.1016/j.jbiotec.2007.01.007.

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14

Cortina, J. M., J. Martinell, V. Artiz, J. Fraile, and G. Rábago. "Comparative clinical results with Omniscience (STM1), Medtronic-Hall, and Björk-Shiley convexo-concave (70 degrees) prostheses in mitral valve replacement." Journal of Thoracic and Cardiovascular Surgery 91, no. 2 (February 1986): 174–83. http://dx.doi.org/10.1016/s0022-5223(19)36076-3.

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15

Nguyen, Thong Ba, Vishwanath Vasudev Prabhu, Yan Hong Piao, Young Eun Oh, Rami Fatima Zahra, and Young-Chul Chung. "Effects of Stathmin 1 Gene Knockout on Behaviors and Dopaminergic Markers in Mice Exposed to Social Defeat Stress." Brain Sciences 9, no. 9 (August 26, 2019): 215. http://dx.doi.org/10.3390/brainsci9090215.

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Stathmin (STMN), a microtubule-destabilizing factor, can regulate fear, anxiety, and learning. Social defeat stress (SDS) has detrimental effects on mental health and increases the risk of various psychiatric diseases. This study investigated the effects of STMN1 gene knockout (KO) on behavioral parameters and dopaminergic markers using an SDS mouse model. The STMN1 KO mice showed anxious hyperactivity, impaired object recognition, and decreased levels of neutral and social investigating behaviors at baseline compared to wild-type (WT) mice. The impact of SDS on neutral, social investigating and dominant behaviors differed markedly between the STMN1 WT and KO mice. In addition, different levels of total DARPP-32 and pDARPP-32 Thr75 expression were observed among the control, unsusceptible, and susceptible groups of STMN1 KO mice. Our results show that STMN1 has specific roles in locomotion, object recognition, and social interactions. Moreover, SDS had differential impacts on social interactions and dopaminergic markers between STMN1 WT and KO mice.

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Yan, Kevin Kok-Phen, Ikenna Obi, and Nasim Sabouri. "The RGG domain in the C-terminus of the DEAD box helicases Dbp2 and Ded1 is necessary for G-quadruplex destabilization." Nucleic Acids Research 49, no. 14 (July 24, 2021): 8339–54. http://dx.doi.org/10.1093/nar/gkab620.

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Abstract The identification of G-quadruplex (G4) binding proteins and insights into their mechanism of action are important for understanding the regulatory functions of G4 structures. Here, we performed an unbiased affinity-purification assay coupled with mass spectrometry and identified 30 putative G4 binding proteins from the fission yeast Schizosaccharomyces pombe. Gene ontology analysis of the molecular functions enriched in this pull-down assay included mRNA binding, RNA helicase activity, and translation regulator activity. We focused this study on three of the identified proteins that possessed putative arginine-glycine-glycine (RGG) domains, namely the Stm1 homolog Oga1 and the DEAD box RNA helicases Dbp2 and Ded1. We found that Oga1, Dbp2, and Ded1 bound to both DNA and RNA G4s in vitro. Both Dbp2 and Ded1 bound to G4 structures through the RGG domain located in the C-terminal region of the helicases, and point mutations in this domain weakened the G4 binding properties of the helicases. Dbp2 and Ded1 destabilized less thermostable G4 RNA and DNA structures, and this ability was independent of ATP but dependent on the RGG domain. Our study provides the first evidence that the RGG motifs in DEAD box helicases are necessary for both G4 binding and G4 destabilization.

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17

Chung, Kyung-Sook, Misun Won, Sang-Bong Lee, Young-Joo Jang, Kwang-Lae Hoe, Dong-Uk Kim, Ji-Won Lee, Kyu-Won Kim, and Hyang-Sook Yoo. "Isolation of a novel gene fromSchizosaccharomyces pombe: stm1 +, encoding a seven-transmembrane loop protein that may couple with the heterotrimeric Gα2 protein, Gpa2." Journal of Biological Chemistry 277, no. 9 (March 2002): 7626–27. http://dx.doi.org/10.1016/s0021-9258(19)82325-6.

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18

Chung, Kyung-Sook, Misun Won, Sang-Bong Lee, Young-Joo Jang, Kwang-Lae Hoe, Dong-Uk Kim, Ji-Won Lee, Kyu-Won Kim, and Hyang-Sook Yoo. "Isolation of a Novel Gene fromSchizosaccharomyces pombe: stm1+Encoding a Seven-transmembrane Loop Protein That May Couple with the Heterotrimeric Gα2 Protein, Gpa2." Journal of Biological Chemistry 276, no. 43 (July 18, 2001): 40190–201. http://dx.doi.org/10.1074/jbc.m100341200.

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GROVE-WHITE, D. H., A. J. H. LEATHERBARROW, P. J. CRIPPS, P. J. DIGGLE, and N. P. FRENCH. "Molecular epidemiology and genetic diversity ofCampylobacter jejuniin ruminants." Epidemiology and Infection 139, no. 11 (December 7, 2010): 1661–71. http://dx.doi.org/10.1017/s0950268810002736.

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SUMMARYMulti-locus sequence typing was performed on 1003Campylobacter jejuniisolates collected in a 2-year longitudinal study of 15 dairy farms and four sheep farms in Lancashire, UK. There was considerable farm-level variation in occurrence and prevalence of clonal complexes (CC). Clonal complexes ST61, ST21, ST403 and ST45 were most prevalent in cattle while in sheep CC ST42, ST21, ST48 and ST52 were most prevalent. CC ST45, a complex previously shown to be more common in summer months in human cases, was more prevalent in summer in our ruminant samples. Gene flow analysis demonstrated a high level of genetic heterogeneity at the within-farm level. Sequence-type diversity was greater in cattle compared to sheep, in cattle at pasturevs. housed, and in isolates from farms on the Pennines compared to the Southern Fylde. Sequence-type diversity was greatest in isolates belonging to CC ST21, ST45 and ST206.

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20

Walsh, Ciara M., Michael Chvanov, Lee P. Haynes, Ole H. Petersen, Alexei V. Tepikin, and Robert D. Burgoyne. "Role of phosphoinositides in STIM1 dynamics and store-operated calcium entry." Biochemical Journal 425, no. 1 (December 14, 2009): 159–68. http://dx.doi.org/10.1042/bj20090884.

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Ca2+ entry through store-operated Ca2+ channels involves the interaction at ER–PM (endoplasmic reticulum–plasma membrane) junctions of STIM (stromal interaction molecule) and Orai. STIM proteins are sensors of the luminal ER Ca2+ concentration and, following depletion of ER Ca2+, they oligomerize and translocate to ER–PM junctions where they form STIM puncta. Direct binding to Orai proteins activates their Ca2+ channel function. It has been suggested that an additional interaction of the C-terminal polybasic domain of STIM1 with PM phosphoinositides could contribute to STIM1 puncta formation prior to binding to Orai. In the present study, we investigated the role of phosphoinositides in the formation of STIM1 puncta and SOCE (store-operated Ca2+ entry) in response to store depletion. Treatment of HeLa cells with inhibitors of PI3K (phosphatidylinositol 3-kinase) and PI4K (phosphatidylinositol 4-kinase) (wortmannin and LY294002) partially inhibited formation of STIM1 puncta. Additional rapid depletion of PtdIns(4,5)P2 resulted in more substantial inhibition of the translocation of STIM1–EYFP (enhanced yellow fluorescent protein) into puncta. The inhibition was extensive at a concentration of LY294002 (50 μM) that should primarily inhibit PI3K, consistent with a major role for PtdIns(4,5)P2 and PtdIns(3,4,5)P3 in puncta formation. Depletion of phosphoinositides also inhibited SOCE based on measurement of the rise in intracellular Ca2+ concentration after store depletion. Overexpression of Orai1 resulted in a recovery of translocation of STMI1 into puncta following phosphoinositide depletion and, under these conditions, SOCE was increased to above control levels. These observations support the idea that phosphoinositides are not essential but contribute to STIM1 accumulation at ER–PM junctions with a second translocation mechanism involving direct STIM1–Orai interactions.

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Kubo, Takashi, Masayuki Hogiri, Hiroshi Kagata, and Atsushi Nakahira. "Synthesis of Nano-Sized Barium Titanate Powder by Rotary-Hydrothermal Process." Key Engineering Materials 421-422 (December 2009): 269–72. http://dx.doi.org/10.4028/www.scientific.net/kem.421-422.269.

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Nano-sized BaTiO3 powders with narrow size distribution and the high tetragonality were attempted to synthesize by the rotary-hydrothermal process in water system, using two kinds of commercial anatase-type TiO2 (ST21/ST01) with different particle size and Ba(OH)2. The rotary-hydrothermal syntheses were done with the rotary-speed of 20 revolutions per minute at 523 K for 24 h. Highly- and mono-dispersed BaTiO3 powders were successfully synthesized by applying the rotary-hydrothermal process. For rotary-hydrothermal synthesis, it was found that the average size, tetragonality, and quality of the BaTiO3 particle strongly depended on the particle size of the starting material. In the case of using ST01 as a starting material, BaTiO3 nano-powders mainly composed of coarse-faceted particles (average particle size = ca.100 nm) with the tetragonal phase and very little lattice defects were successfully synthesized.

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Sato, Norihiro, Kiyomi Sasaki, Takuma Katayama, Yusuke Nomura, and Hidetaka Torigoe. "3B1446 Mechanism of the interaction between triplex DNA and triplex DNA-binding protein Stm1(3B Nucleic acid binding proteins,The 49th Annual Meeting of the Biophysical Society of Japan)." Seibutsu Butsuri 51, supplement (2011): S111—S112. http://dx.doi.org/10.2142/biophys.51.s111_6.

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Maloney, Jenny G., Yunah Jang, Aleksey Molokin, Nadja S. George, and Monica Santin. "Wide Genetic Diversity of Blastocystis in White-Tailed Deer (Odocoileus virginianus) from Maryland, USA." Microorganisms 9, no. 6 (June 21, 2021): 1343. http://dx.doi.org/10.3390/microorganisms9061343.

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Blastocystis is a gastrointestinal protist frequently reported in humans and animals worldwide. Wildlife populations, including deer, may serve as reservoirs of parasitic diseases for both humans and domestic animals, either through direct contact or through contamination of food or water resources. However, no studies of the occurrence and subtype distribution of Blastocystis in wildlife populations have been conducted in the United States. PCR and next generation amplicon sequencing were used to determine the occurrence and subtypes of Blastocystis in white-tailed deer (Odocoileus virginianus). Blastocystis was common, with 88.8% (71/80) of samples found to be positive. Twelve subtypes were identified, ten previously reported (ST1, ST3, ST4, ST10, ST14, ST21, and ST23–ST26) and two novel subtypes (ST30 and ST31). To confirm the validity of ST30 and ST31, MinION sequencing was used to obtain full-length SSU rRNA gene sequences, and phylogenetic and pairwise distance analyses were performed. ST10, ST14, and ST24 were the most commonly observed subtypes. Potentially zoonotic subtypes ST1, ST3, or ST4 were present in 8.5% of Blastocystis-positives. Mixed subtype infections were common (90.1% of Blastocystis-positives). This study is the first to subtype Blastocystis in white-tailed deer. White-tailed deer were found to be commonly infected/colonized with a wide diversity of subtypes, including two novel subtypes, zoonotic subtypes, and subtypes frequently reported in domestic animals. More studies in wildlife are needed to better understand their role in the transmission of Blastocystis.

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JONAS, R., S. KITTL, G. OVERESCH, and P. KUHNERT. "Genotypes and antibiotic resistance of bovineCampylobacterand their contribution to human campylobacteriosis." Epidemiology and Infection 143, no. 11 (December 16, 2014): 2373–80. http://dx.doi.org/10.1017/s0950268814003410.

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SUMMARYCampylobacter jejuniandCampylobacter coliare the most important bacterial causes of human gastroenteritis. Chicken has been recognized as a major source for human infection, whereas cattle might also contribute to a lesser extent. However, there is a paucity of information available regardingCampylobacterin Swiss cattle and their role for human campylobacteriosis. To gain more information on genotypes and antibiotic resistance of bovineC. jejuniandC. coliand on their contribution to human disease, 97 cattle isolates were analysed. Multilocus sequence typing (MLST) andflaBtyping were applied and thegyrAand 23S rRNA genes were screened for point mutations responsible for quinolone and macrolide resistance, respectively. A total of 37 sequence types (STs) and 44flaBtypes were identified, including two sequence types and fiveflaBtypes not previously described. Most common sequence types were ST21 (21%), ST61 (12%) and ST48 (11%). Only one isolate was macrolide resistant while 31% (n= 30) were quinolone resistant. Source attribution indicated chicken as the main source of human infection with cattle being second. In conclusion, cattle should not be underestimated as a potential source of human campylobacteriosis.

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Titze, Isabel, and Volker Krömker. "Antimicrobial Activity of a Phage Mixture and a Lactic Acid Bacterium against Staphylococcus aureus from Bovine Mastitis." Veterinary Sciences 7, no. 1 (March 6, 2020): 31. http://dx.doi.org/10.3390/vetsci7010031.

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The antimicrobial activity of a phage mixture and a lactic acid bacterium against Staphylococcus aureus isolates from bovine origin was investigated in vitro with regard to possible applications in the therapy of udder inflammation (mastitis) caused by bacterial infections. The S. aureus isolates used for inoculation derived from quarter foremilk samples of mastitis cases. For the examination of the antimicrobial activity, the reduction of the S. aureus germ density was determined [log10 cfu/mL]. The phage mixture consisted of the three obligatory lytic and S. aureus-specific phages STA1.ST29, EB1.ST11 and EB1.ST27 (1:1:1). The selected Lactobacillus plantarum strain with proven antimicrobial properties and the phage mixture were tested against S. aureus in milk, both alone and in combination. The application of the lactic acid bacterium showed only a low reduction ability for a 24 h incubation period. The bacteriophage mixture as well as its combination with the lactic acid bacterium showed high antimicrobial activity against S. aureus for a 24 h incubation period at 37 °C, with only the phage mixture showing significance.

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Park, Ji Hee, Seung Yeon Jeong, Jun Hee Choi, and Eun Hui Lee. "Pathological Mechanism of a Constitutively Active Form of Stromal Interaction Molecule 1 in Skeletal Muscle." Biomolecules 11, no. 8 (July 21, 2021): 1064. http://dx.doi.org/10.3390/biom11081064.

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Stromal interaction molecule 1 (STIM1) is the main protein that, along with Orai1, mediates store-operated Ca2+ entry (SOCE) in skeletal muscle. Abnormal SOCE due to mutations in STIM1 is one of the causes of human skeletal muscle diseases. STIM1-R304Q (a constitutively active form of STIM1) has been found in human patients with skeletal muscle phenotypes such as muscle weakness, myalgia, muscle stiffness, and contracture. However, the pathological mechanism(s) of STIM1-R304Q in skeletal muscle have not been well studied. To examine the pathological mechanism(s) of STIM1-R304Q in skeletal muscle, STIM1-R304Q was expressed in mouse primary skeletal myotubes, and the properties of the skeletal myotubes were examined using single-myotube Ca2+ imaging, transmission electron microscopy (TEM), and biochemical approaches. STIM1-R304Q did not interfere with the terminal differentiation of skeletal myoblasts to myotubes and retained the ability of STIM1 to attenuate dihydropyridine receptor (DHPR) activity. STIM1-R304Q induced hyper-SOCE (that exceeded the SOCE by wild-type STIM1) by affecting both the amplitude and the onset rate of SOCE. Unlike that by wild-type STIM1, hyper-SOCE by STIM1-R304Q contributed to a disturbance in Ca2+ distribution between the cytosol and the sarcoplasmic reticulum (SR) (high Ca2+ in the cytosol and low Ca2+ in the SR). Moreover, the hyper-SOCE and the high cytosolic Ca2+ level induced by STIM1-R304Q involve changes in mitochondrial shape. Therefore, a series of these cellular defects induced by STIM1-R304Q could induce deleterious skeletal muscle phenotypes in human patients carrying STIM1-R304Q.

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Titze, Isabel, Tatiana Lehnherr, Hansjörg Lehnherr, and Volker Krömker. "Efficacy of Bacteriophages Against Staphylococcus aureus Isolates from Bovine Mastitis." Pharmaceuticals 13, no. 3 (February 26, 2020): 35. http://dx.doi.org/10.3390/ph13030035.

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The lytic efficacy of bacteriophages against Staphylococcus aureus isolates from bovine milk was investigated in vitro, regarding possible applications in the therapy of udder inflammation caused by bacterial infections (mastitis). The host range of sequenced, lytic bacteriophages was determined against a collection of 92 Staphylococcus (S.) aureus isolates. The isolates originated from quarter foremilk samples of clinical and subclinical mastitis cases. A spot test and a subsequent plaque assay were used to determine the phage host range. According to their host range, propagation and storage properties, three phages, STA1.ST29, EB1.ST11, and EB1.ST27, were selected for preparing a bacteriophage mixture (1:1:1), which was examined for its lytic activity against S. aureus in pasteurized and raw milk. It was found that almost two thirds of the isolates could be lysed by at least one of the tested phages. The bacteriophage mixture was able to reduce the S. aureus germ density in pasteurized milk and its reduction ability was maintained in raw milk, with only a moderate decrease compared to the results in pasteurized milk. The significant reduction ability of the phage mixture in raw milk promotes further in vivo investigation.

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Li, Yong-jun, Lia Danelishvili, Dirk Wagner, Mary Petrofsky, and Luiz E. Bermudez. "Identification of virulence determinants of Mycobacterium avium that impact on the ability to resist host killing mechanisms." Journal of Medical Microbiology 59, no. 1 (January 1, 2010): 8–16. http://dx.doi.org/10.1099/jmm.0.012864-0.

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Mycobacterium avium is an opportunistic pathogen associated with pulmonary disease in non-AIDS patients and disseminated infection in patients with AIDS. The chief route of infection is by colonization and invasion of the mucosa of the gastrointestinal tract, but infection through the respiratory route also occurs. After crossing the mucosa, M. avium infects and replicates within tissue macrophages. To identify M. avium genes required for survival in vivo, a library of signature-tagged transposon mutants was constructed and screened for clones attenuated in mice. Thirty-two clones were found to be attenuated for their virulence, from which eleven were sequenced and tested further. All the mutants studied grew similarly in vitro to the wild-type MAC104. Ten mutants were tested individually in mice, confirming the attenuated phenotype. MAV_2450, a polyketide synthase homologue to Mycobacterium tuberculosis pks12, was identified. STM5 and STM10 genes (encoding two hypothetical proteins MAV_4292 and MAV_4012) were associated with susceptibility to oxidative products. Mutants MAV_2450, MAV_4292, MAV_0385 and MAV_4264 live in macrophage vacuoles with acidic pH (below 6.9). Mutants MAV_4292, MAV_0385 and MAV_4264 were susceptible to nitric oxide in vitro. The study of individual mutants can potentially lead to new knowledge about M. avium pathogenic mechanisms.

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Zhang, Lane, Limin Wang, Shu Li, Jingyi Xue, and Dali Luo. "Calsequestrin-1 Regulates Store-Operated Ca2+ Entry by Inhibiting STIM1 Aggregation." Cellular Physiology and Biochemistry 38, no. 6 (2016): 2183–93. http://dx.doi.org/10.1159/000445574.

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Background/Aims: Stromal interacting molecule-1 (STIM1) aggregation and redistribution to plasma membrane to interact with Orai1 constitute the core mechanism of store-operated Ca2+ entry (SOCE). Previous study has revealed that calsequestrin-1 (CSQ1) regulates SOCE in HEK293 cells through interacting with STIM1 and inhibiting STIM1/Orai1 interaction. Here, we further investigate how CSQ1/STIM1 interaction affects SOCE. Methods: Using confocal microscopy, STIM1 aggregation and co-localizations with CSQ1 or Orai1 upon Ca2+ store depletion by thapsigargin were measured and quantified by Imaris software in HeLa cells transfected with different CSQ1 mutants. The interactions of CSQ1/STIM1 and STIM1/Orai1, and internal Ca2+ changes were detected by co-immunoprecipitation and Fura2, respectively. Results: Wt-CSQ1 overexpression significantly reduced STIM1 clustering in the perimembrane and cytosolic regions, whereas over-expression of a C-terminal amino acid 362-396 deletion mutant (C35) did not. Consistently, a significant depression of SOCE, increased CSQ1 monomerization and CSQ1/STIM1 interaction, and a reduced STIM1/Orai1 association were observed in wt-CSQ1 but not in C35-transfected cells. Additionally, mutant lacking C-terminal AA 388-396 deletion exerted weaker potency in inhibiting STIM1 aggregation and association with Orai1 than wt-CSQ1. Conclusions: Our results demonstrate that CSQ1 monomers suppress SOCE by interacting with STIM1 and attenuating STIM1 aggregation via its C-terminal amino acid 362-396.

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Maus, Mate, Amit Jairaman, Peter B. Stathopulos, Martin Muik, Marc Fahrner, Carl Weidinger, Melina Benson, et al. "Missense mutation in immunodeficient patients shows the multifunctional roles of coiled-coil domain 3 (CC3) in STIM1 activation." Proceedings of the National Academy of Sciences 112, no. 19 (April 27, 2015): 6206–11. http://dx.doi.org/10.1073/pnas.1418852112.

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Store-operated Ca2+ entry (SOCE) is a universal Ca2+ influx pathway that is important for the function of many cell types. SOCE occurs upon depletion of endoplasmic reticulum (ER) Ca2+ stores and relies on a complex molecular interplay between the plasma membrane (PM) Ca2+ channel ORAI1 and the ER Ca2+ sensor stromal interaction molecule (STIM) 1. Patients with null mutations in ORAI1 or STIM1 genes present with severe combined immunodeficiency (SCID)-like disease. Here, we describe the molecular mechanisms by which a loss-of-function STIM1 mutation (R429C) in human patients abolishes SOCE. R429 is located in the third coiled-coil (CC3) domain of the cytoplasmic C terminus of STIM1. Mutation of R429 destabilizes the CC3 structure and alters the conformation of the STIM1 C terminus, thereby releasing a polybasic domain that promotes STIM1 recruitment to ER–PM junctions. However, the mutation also impairs cytoplasmic STIM1 oligomerization and abolishes STIM1–ORAI1 interactions. Thus, despite its constitutive localization at ER–PM junctions, mutant STIM1 fails to activate SOCE. Our results demonstrate multifunctional roles of the CC3 domain in regulating intra- and intermolecular STIM1 interactions that control (i) transition of STIM1 from a quiescent to an active conformational state, (ii) cytoplasmic STIM1 oligomerization, and (iii) STIM1–ORAI1 binding required for ORAI1 activation.

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Jha, Archana, Malini Ahuja, József Maléth, Claudia M. Moreno, Joseph P. Yuan, Min Seuk Kim, and Shmuel Muallem. "The STIM1 CTID domain determines access of SARAF to SOAR to regulate Orai1 channel function." Journal of Cell Biology 202, no. 1 (July 1, 2013): 71–79. http://dx.doi.org/10.1083/jcb.201301148.

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Ca2+ influx by store-operated Ca2+ channels (SOCs) mediates all Ca2+-dependent cell functions, but excess Ca2+ influx is highly toxic. The molecular components of SOC are the pore-forming Orai1 channel and the endoplasmic reticulum Ca2+ sensor STIM1. Slow Ca2+-dependent inactivation (SCDI) of Orai1 guards against cell damage, but its molecular mechanism is unknown. Here, we used homology modeling to identify a conserved STIM1(448–530) C-terminal inhibitory domain (CTID), whose deletion resulted in spontaneous clustering of STIM1 and full activation of Orai1 in the absence of store depletion. CTID regulated SCDI by determining access to and interaction of the STIM1 inhibitor SARAF with STIM1 Orai1 activation region (SOAR), the STIM1 domain that activates Orai1. CTID had two lobes, STIM1(448–490) and STIM1(490–530), with distinct roles in mediating access of SARAF to SOAR. The STIM1(448–490) lobe restricted, whereas the STIM1(490–530) lobe directed, SARAF to SOAR. The two lobes cooperated to determine the features of SCDI. These findings highlight the central role of STIM1 in SCDI and provide a molecular mechanism for SCDI of Orai1.

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Dong-Sin, HOU, WANG Lin-Ci, and SIE Cing-Cun. "STME." Industrial Robot Magazine 4, no. 1 (January 31, 2015): 1–3. http://dx.doi.org/10.32738/irm.201501.0001.

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Commelin, M. "STMI." Revue Générale Nucléaire, no. 4 (July 1990): 418–19. http://dx.doi.org/10.1051/rgn/19904418.

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Yu, Junwei, Haining Zhang, Mingshu Zhang, Yongqiang Deng, Huiyu Wang, Jingze Lu, Tao Xu, and Pingyong Xu. "An aromatic amino acid in the coiled-coil 1 domain plays a crucial role in the auto-inhibitory mechanism of STIM1." Biochemical Journal 454, no. 3 (August 29, 2013): 401–9. http://dx.doi.org/10.1042/bj20130292.

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STIM1 (stromal interaction molecule 1) is one of the key elements that mediate store-operated Ca2+ entry via CRAC (Ca2+- release-activated Ca2+) channels in immune and non-excitable cells. Under physiological conditions, the intramolecular auto-inhibitions in STIM1 C- and STIM1 N-termini play essential roles in keeping STIM1 in an inactive state. However, the auto-inhibitory mechanism of the STIM1 C-terminus is still unclear. In the present study, we first predicted a short inhibitory domain (residues 310–317) in human STIM1 that might determine the different localizations of human STIM1 from Caenorhabditis elegans STIM1 in resting cells. Next, we confirmed the prediction and further identified an aromatic amino acid residue, Tyr316, that played a crucial role in maintaining STIM1 in a closed conformation in quiescent cells. Full-length STIM1-Y316A formed constitutive clusters near the plasma membrane and activated the CRAC channel in the resting state when co-expressed with Orai1. The introduction of a Y316A mutation caused the higher-order oligomerization of the in vitro purified STIM1 fragment containing both the auto-inhibitory domain and CAD (CRAC-activating domain). We propose that the Tyr316 residue may be involved in the auto-inhibitory mechanism of the STIM1 C-terminus in the quiescent state. This inhibition could be achieved either by interacting with the CAD using hydrogen and/or hydrophobic bonds, or by an intermolecular interaction using repulsive forces, which maintained a dimeric STIM1.

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Nomura, Atsuo, Shunichi Yokoe, Kiichiro Tomoda, Takatoshi Nakagawa, Francisco Javier Martin-Romero, and Michio Asahi. "Fluctuation in O-GlcNAcylation inactivates STIM1 to reduce store-operated calcium ion entry via down-regulation of Ser621 phosphorylation." Journal of Biological Chemistry 295, no. 50 (October 6, 2020): 17071–82. http://dx.doi.org/10.1074/jbc.ra120.014271.

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Stromal interaction molecule 1 (STIM1) plays a pivotal role in store-operated Ca2+ entry (SOCE), an essential mechanism in cellular calcium signaling and in maintaining cellular calcium balance. Because O-GlcNAcylation plays pivotal roles in various cellular function, we examined the effect of fluctuation in STIM1 O-GlcNAcylation on SOCE activity. We found that both increase and decrease in STIM1 O-GlcNAcylation impaired SOCE activity. To determine the molecular basis, we established STIM1-knockout HEK293 (STIM1-KO-HEK) cells using the CRISPR/Cas9 system and transfected STIM1 WT (STIM1-KO-WT-HEK), S621A (STIM1-KO-S621A-HEK), or T626A (STIM1-KO-T626A-HEK) cells. Using these cells, we examined the possible O-GlcNAcylation sites of STIM1 to determine whether the sites were O-GlcNAcylated. Co-immunoprecipitation analysis revealed that Ser621 and Thr626 were O-GlcNAcylated and that Thr626 was O-GlcNAcylated in the steady state but Ser621 was not. The SOCE activity in STIM1-KO-S621A-HEK and STIM1-KO-T626A-HEK cells was lower than that in STIM1-KO-WT-HEK cells because of reduced phosphorylation at Ser621. Treatment with the O-GlcNAcase inhibitor Thiamet G or O-GlcNAc transferase (OGT) transfection, which increases O-GlcNAcylation, reduced SOCE activity, whereas treatment with the OGT inhibitor ST045849 or siOGT transfection, which decreases O-GlcNAcylation, also reduced SOCE activity. Decrease in SOCE activity due to increase and decrease in O-GlcNAcylation was attributable to reduced phosphorylation at Ser621. These data suggest that both decrease in O-GlcNAcylation at Thr626 and increase in O-GlcNAcylation at Ser621 in STIM1 lead to impairment of SOCE activity through decrease in Ser621 phosphorylation. Targeting STIM1 O-GlcNAcylation could provide a promising treatment option for the related diseases, such as neurodegenerative diseases.

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Rao, Jaladanki N., Navneeta Rathor, Tongtong Zou, Lan Liu, Lan Xiao, Ting-Xi Yu, Yu-Hong Cui, and Jian-Ying Wang. "STIM1 translocation to the plasma membrane enhances intestinal epithelial restitution by inducing TRPC1-mediated Ca2+ signaling after wounding." American Journal of Physiology-Cell Physiology 299, no. 3 (September 2010): C579—C588. http://dx.doi.org/10.1152/ajpcell.00066.2010.

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Early epithelial restitution is an important repair modality in the gut mucosa and occurs as a consequence of epithelial cell migration. Canonical transient receptor potential-1 (TRPC1) functions as a store-operated Ca2+ channel (SOCs) in intestinal epithelial cells (IECs) and regulates intestinal restitution, but the exact upstream signals initiating TRPC1 activation after mucosal injury remain elusive. Stromal interaction molecule 1 (STIM1) is a single membrane-spanning protein and is recently identified as essential components of SOC activation. The current study was performed to determine whether STIM1 plays a role in the regulation of intestinal epithelial restitution by activating TRPC1 channels. STIM1 translocation to the plasma membrane increased after wounding, which was followed by an increase in IEC migration to reseal wounds. Increased STIM1 levels at the plasma membrane by overexpressing EF-hand mutant STIM1 enhanced Ca2+ influx through SOCs and stimulated IEC migration after wounding. STIM1 interacted with TRPC1 and formed STIM1/TRPC1 complex, whereas inactivation of STIM1 by STIM1 silencing decreased SOC-mediated Ca2+ influx and inhibited epithelial restitution. In cells overexpressing EF-hand mutant STIM1, TRPC1 silencing also decreased STIM1/TRPC1 complex, reduced SOC-mediated Ca2+ influx, and repressed cell migration after wounding. Our findings demonstrate that induced STIM1 translocation to the plasma membrane promotes IEC migration after wounding by enhancing TRPC1-mediated Ca2+ signaling and provide new insight into the mechanism of intestinal epithelial restitution.

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Pascual-Caro, Carlos, Maria Berrocal, Aida M. Lopez-Guerrero, Alberto Alvarez-Barrientos, Eulalia Pozo-Guisado, Carlos Gutierrez-Merino, Ana M. Mata, and Francisco Javier Martin-Romero. "STIM1 deficiency is linked to Alzheimer’s disease and triggers cell death in SH-SY5Y cells by upregulation of L-type voltage-operated Ca2+ entry." Journal of Molecular Medicine 96, no. 10 (August 7, 2018): 1061–79. http://dx.doi.org/10.1007/s00109-018-1677-y.

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Abstract STIM1 is an endoplasmic reticulum protein with a role in Ca2+ mobilization and signaling. As a sensor of intraluminal Ca2+ levels, STIM1 modulates plasma membrane Ca2+ channels to regulate Ca2+ entry. In neuroblastoma SH-SY5Y cells and in familial Alzheimer’s disease patient skin fibroblasts, STIM1 is cleaved at the transmembrane domain by the presenilin-1-associated γ-secretase, leading to dysregulation of Ca2+ homeostasis. In this report, we investigated expression levels of STIM1 in brain tissues (medium frontal gyrus) of pathologically confirmed Alzheimer’s disease patients, and observed that STIM1 protein expression level decreased with the progression of neurodegeneration. To study the role of STIM1 in neurodegeneration, a strategy was designed to knock-out the expression of STIM1 gene in the SH-SY5Y neuroblastoma cell line by CRISPR/Cas9-mediated genome editing, as an in vitro model to examine the phenotype of STIM1-deficient neuronal cells. It was proved that, while STIM1 is not required for the differentiation of SH-SY5Y cells, it is absolutely essential for cell survival in differentiating cells. Differentiated STIM1-KO cells showed a significant decrease of mitochondrial respiratory chain complex I activity, mitochondrial inner membrane depolarization, reduced mitochondrial free Ca2+ concentration, and higher levels of senescence as compared with wild-type cells. In parallel, STIM1-KO cells showed a potentiated Ca2+ entry in response to depolarization, which was sensitive to nifedipine, pointing to L-type voltage-operated Ca2+ channels as mediators of the upregulated Ca2+ entry. The stable knocking-down of CACNA1C transcripts restored mitochondrial function, increased mitochondrial Ca2+ levels, and dropped senescence to basal levels, demonstrating the essential role of the upregulation of voltage-operated Ca2+ entry through Cav1.2 channels in STIM1-deficient SH-SY5Y cell death. Key messages STIM1 protein expression decreases with the progression of neurodegeneration in Alzheimer’s disease. STIM1 is essential for cell viability in differentiated SH-SY5Y cells. STIM1 deficiency triggers voltage-regulated Ca2+ entry-dependent cell death. Mitochondrial dysfunction and senescence are features of STIM1-deficient differentiated cells.

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Gu, J., A. Y. S. Law, B. H. Y. Yeung, and Chris K. C. Wong. "Characterization of stanniocalcin 1 binding and signaling in gill cells of Japanese eels." Journal of Molecular Endocrinology 54, no. 3 (June 2015): 305–14. http://dx.doi.org/10.1530/jme-14-0320.

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Stanniocalcin 1 (STC1) is a hypocalcemic hormone that is known to play an important role in calcium metabolism in teleost fish. An increase in blood Ca2+ levels stimulates its synthesis and release. The biological action of STC1 inhibits gill Ca2+ transport (GCAT), but we as yet have no clear understanding of how STC1 inhibits GCAT. In the present study, we characterized the binding, signaling, and action of STC1 on gill cells. Treatment of gill cell cultures with the extracts of corpuscles of Stannius or recombinant STC1 proteins (STC1–V5) led to an increase in cytosolic cAMP levels. Using in situ ligand-binding assays, we demonstrated that STC1–V5 binds to both lamellar and inter-lamellar regions of gill sections. The binding sites were significantly increased in gill sections obtained from fish adapted to high-Ca2+ (2 mM) freshwater (FW) as compared with those from fish adapted to low-Ca2+ (0.2 mM) FW. Receptor-binding assays illustrated specific binding of STC1-alkaline phosphatase to plasma membrane (Kd of 0.36 nM), mitochondria (Kd of 0.41 nM), and nuclear (Kd of 0.71 nM) preparations from gill cells. STC1 binding capacity was significantly greater in the plasma membrane preparations of gills obtained from fish adapted to high-Ca2+ FW. Using isolated pavement cells and mitochondria-rich cells in cAMP assays, we obtained results indicating that both cell types responded to STC1. To illustrate the biological action of STC1, we conducted Ca2+ imaging experiments to demonstrate the effects of STC1 on thapsigargin-induced elevation of cytosolic Ca2+. Our results indicated that STC1 exerted its inhibitory action via a cAMP pathway to lower intracellular Ca2+ levels. Intriguingly, we were able to block the action of STC1 using an inhibitor, NS-398, of cyclooxygenase-2 (COX-2), which is known to stimulate the activity of sarcoplasmic and endoplasmic reticulum Ca2+-ATPase (SERCA). A follow-up experiment in which gill cells were incubated with STC1 revealed a downregulation of the epithelial Ca2+ channel (ecacl) but an upregulation of cox-2 expression. The ECaCl is a gatekeeper for Ca2+ entry, whereas COX-2 mediates an activation of SERCA. Taking these results together, the present study is, to our knowledge, the first to provide evidence of STC1 binding and signaling as well as the first to decipher the mechanism of the effect of STC1 on fish gills.

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Covington, Elizabeth D., Minnie M. Wu, and Richard S. Lewis. "Essential Role for the CRAC Activation Domain in Store-dependent Oligomerization of STIM1." Molecular Biology of the Cell 21, no. 11 (June 2010): 1897–907. http://dx.doi.org/10.1091/mbc.e10-02-0145.

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Oligomerization of the ER Ca2+ sensor STIM1 is an essential step in store-operated Ca2+ entry. The lumenal EF-hand and SAM domains of STIM1 are believed to initiate oligomerization after Ca2+ store depletion, but the contributions of STIM1 cytosolic domains (coiled-coil 1, CC1; coiled-coil 2, CC2; CRAC activation domain, CAD) to this process are not well understood. By applying coimmunoprecipitation and fluorescence photobleaching and energy transfer techniques to truncated and mutant STIM1 proteins, we find that STIM1 cytosolic domains play distinct roles in forming both “resting” oligomers in cells with replete Ca2+ stores and higher-order oligomers in store-depleted cells. CC1 supports the formation of resting STIM1 oligomers and appears to interact with cytosolic components to slow STIM1 diffusion. On store depletion, STIM1 lacking all cytosolic domains (STIM1-ΔC) oligomerizes through EF-SAM interactions alone, but these oligomers are unstable. Addition of CC1 + CAD, but not CC1 alone, enables the formation of stable store-dependent oligomers. Within the CAD, both CC2 and C-terminal residues contribute to oligomer formation. Our results reveal a new function for the CAD: in addition to binding and activating Orai1, it is directly involved in STIM1 oligomerization, the initial event triggering store-operated Ca2+ entry.

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Yang, Yanfang, Zhansheng Jiang, Ning Ma, Bin Wang, Jun Liu, Lina Zhang, and Lin Gu. "MicroRNA-223 Targeting STIM1 Inhibits the Biological Behavior of Breast Cancer." Cellular Physiology and Biochemistry 45, no. 2 (2018): 856–66. http://dx.doi.org/10.1159/000487180.

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Background/Aims: To investigate the cellular effects and clinical significance of microRNA-223 (miR-223) in breast cancer by targeting stromal interaction molecule1 (STIM1). Methods: Breast cancer cell lines (T47D, MCF-7, SKB-R3, MDA-MB-231 and MDA-MB-435) and a normal breast epithelial cell line (MCF-10A) were prepared for this study. MiR-223 mimics, anti-miR-223 and pcDNA 3.1-STIM1 were transiently transfected into cancer cells independently or together, and then RT-qPCR was performed to detect the expressions of miR-223 and STIM1 mRNA, dual-luciferase reporter assay was conducted to examine the effects of miR-223 on STIM1, Western blotting was used to measure the expressions of the STIM1 proteins, MTT and Trans-well assays were performed to detect cell proliferation and invasion. Finally, the correlation of miR-223 and STIM1 was investigated by detecting with ISH and IHC in breast cancer specimens or the corresponding adjacent normal tissues. Results: Compared with normal cells and tissues, breast cancer tissues and cells exhibited significantly lower expression of miR-223, but higher expression of STIM1. MiR-223 could inhibit the proliferation and invasiveness of breast cancer cells by negatively regulating the expressions of STIM1. Reimplantation with STIM1 partially rescued the miRNA-223-induced inhibition of breast cancer cells. Clinical data revealed that high expression of STIM1 and miR-223 was respectively detrimental and beneficial factor impacting patient’s disease-free survival (DFS) rather than overall survival (OS). Moreover, Pearson correlation analysis also confirmed that STIM1 was inversely correlated with miR-223. Conclusion: MiR-223 inhibits the proliferation and invasion of breast cancer by targeting STIM1. The miR-223/STIM1 axis could possibly be a potential therapeutic target for treating breast cancer patients.

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Jiang, WQ, AC Chang, M. Satoh, Y. Furuichi, PP Tam, and RR Reddel. "The distribution of stanniocalcin 1 protein in fetal mouse tissues suggests a role in bone and muscle development." Journal of Endocrinology 165, no. 2 (May 1, 2000): 457–66. http://dx.doi.org/10.1677/joe.0.1650457.

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We previously isolated a mammalian gene STC1 that encodes a glycoprotein related to stanniocalcin (STC), a fish hormone that plays a major role in calcium homeostasis. However, the mammalian STC1 gene is expressed in a variety of adult tissues in contrast to fish where STC is expressed only in one unique gland, the corpuscles of Stannius. This suggested that STC1 may have wider autocrine/paracrine functions in mammals. In the present study, using immunocytochemistry, we showed that STC1 protein is localized in the developing bone and muscle of the mouse fetus. During endochondral bone formation, STC1 is found principally in prechondrocytes and prehypertrophic chondrocytes. During intramembranous bone formation STC1 is present in the mesenchyme that is about to undergo ossification. STC1 is also found in the myocardiocytes of the developing heart and at all stages of differentiation from myoblasts to myotube formation in developing skeletal muscle. The specific localization of STC1 to chondrocytes and muscle cells suggests a role for this protein in chondrogenic and myogenic differentiation.

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Chang, Chi-Lun, Yu-Ju Chen, Carlo Giovanni Quintanilla, Ting-Sung Hsieh, and Jen Liou. "EB1 binding restricts STIM1 translocation to ER–PM junctions and regulates store-operated Ca2+ entry." Journal of Cell Biology 217, no. 6 (March 21, 2018): 2047–58. http://dx.doi.org/10.1083/jcb.201711151.

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The endoplasmic reticulum (ER) Ca2+ sensor STIM1 forms oligomers and translocates to ER–plasma membrane (PM) junctions to activate store-operated Ca2+ entry (SOCE) after ER Ca2+ depletion. STIM1 also interacts with EB1 and dynamically tracks microtubule (MT) plus ends. Nevertheless, the role of STIM1–EB1 interaction in regulating SOCE remains unresolved. Using live-cell imaging combined with a synthetic construct approach, we found that EB1 binding constitutes a trapping mechanism restricting STIM1 targeting to ER–PM junctions. We further showed that STIM1 oligomers retain EB1 binding ability in ER Ca2+-depleted cells. By trapping STIM1 molecules at dynamic contacts between the ER and MT plus ends, EB1 binding delayed STIM1 translocation to ER–PM junctions during ER Ca2+ depletion and prevented excess SOCE and ER Ca2+ overload. Our study suggests that STIM1–EB1 interaction shapes the kinetics and amplitude of local SOCE in cellular regions with growing MTs and contributes to spatiotemporal regulation of Ca2+ signaling crucial for cellular functions and homeostasis.

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Pascual-Caro, Carlos, Yolanda Orantos-Aguilera, Irene Sanchez-Lopez, Jaime de Juan-Sanz, Jan B. Parys, Estela Area-Gomez, Eulalia Pozo-Guisado, and Francisco Javier Martin-Romero. "STIM1 Deficiency Leads to Specific Down-Regulation of ITPR3 in SH-SY5Y Cells." International Journal of Molecular Sciences 21, no. 18 (September 9, 2020): 6598. http://dx.doi.org/10.3390/ijms21186598.

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STIM1 is an endoplasmic reticulum (ER) protein that modulates the activity of a number of Ca2+ transport systems. By direct physical interaction with ORAI1, a plasma membrane Ca2+ channel, STIM1 activates the ICRAC current, whereas the binding with the voltage-operated Ca2+ channel CaV1.2 inhibits the current through this latter channel. In this way, STIM1 is a key regulator of Ca2+ signaling in excitable and non-excitable cells, and altered STIM1 levels have been reported to underlie several pathologies, including immunodeficiency, neurodegenerative diseases, and cancer. In both sporadic and familial Alzheimer’s disease, a decrease of STIM1 protein levels accounts for the alteration of Ca2+ handling that compromises neuronal cell viability. Using SH-SY5Y cells edited by CRISPR/Cas9 to knockout STIM1 gene expression, this work evaluated the molecular mechanisms underlying the cell death triggered by the deficiency of STIM1, demonstrating that STIM1 is a positive regulator of ITPR3 gene expression. ITPR3 (or IP3R3) is a Ca2+ channel enriched at ER-mitochondria contact sites where it provides Ca2+ for transport into the mitochondria. Thus, STIM1 deficiency leads to a strong reduction of ITPR3 transcript and ITPR3 protein levels, a consequent decrease of the mitochondria free Ca2+ concentration ([Ca2+]mit), reduction of mitochondrial oxygen consumption rate, and decrease in ATP synthesis rate. All these values were normalized by ectopic expression of ITPR3 in STIM1-KO cells, providing strong evidence for a new mode of regulation of [Ca2+]mit mediated by the STIM1-ITPR3 axis.

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Chang, Andy C. M., Jeon Cha, Frank Koentgen, and Roger R. Reddel. "The Murine Stanniocalcin 1 Gene Is Not Essential for Growth and Development." Molecular and Cellular Biology 25, no. 23 (December 1, 2005): 10604–10. http://dx.doi.org/10.1128/mcb.25.23.10604-10610.2005.

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ABSTRACT The stanniocalcin 1 (STC1) gene is expressed in a wide variety of tissues, including the kidney, prostate, thyroid, bone, and ovary. STC1 protein is considered to have roles in many physiological processes, including bone development, reproduction, wound healing, angiogenesis, and modulation of inflammatory response. In fish, STC1 is a hormone that is secreted by the corpuscles of Stannius and is involved in calcium and phosphate homeostasis. To determine the role of STC1 in mammals, we generated Stc1-null mice by gene targeting. The number of Stc1 − / − mice obtained was in accordance with Mendelian ratios, and both males and females produced offspring normally. No anatomical or histological abnormalities were detected in any tissues. Our results demonstrated that Stc1 function is not essential for growth or reproduction in the mouse.

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Laurent, B. C., X. Yang, and M. Carlson. "An essential Saccharomyces cerevisiae gene homologous to SNF2 encodes a helicase-related protein in a new family." Molecular and Cellular Biology 12, no. 4 (April 1992): 1893–902. http://dx.doi.org/10.1128/mcb.12.4.1893.

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The Saccharomyces cerevisiae SNF2 gene affects the expression of many diversely regulated genes and has been implicated in transcriptional activation. We report here the cloning and characterization of STH1, a gene that is homologous to SNF2. STH1 is essential for mitotic growth and is functionally distinct from SNF2. A bifunctional STH1-beta-galactosidase protein is located in the nucleus. The predicted 155,914-Da STH1 protein is 72% identical to SNF2 over 661 amino acids and 46% identical over another stretch of 66 amino acids. Both STH1 and SNF2 contain a putative nucleoside triphosphate-binding site and sequences resembling the consensus helicase motifs. The large region of homology shared by STH1 and SNF2 is conserved among other eukaryotic proteins, and STH1 and SNF2 appear to define a novel family of proteins related to helicases.

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Laurent, B. C., X. Yang, and M. Carlson. "An essential Saccharomyces cerevisiae gene homologous to SNF2 encodes a helicase-related protein in a new family." Molecular and Cellular Biology 12, no. 4 (April 1992): 1893–902. http://dx.doi.org/10.1128/mcb.12.4.1893-1902.1992.

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The Saccharomyces cerevisiae SNF2 gene affects the expression of many diversely regulated genes and has been implicated in transcriptional activation. We report here the cloning and characterization of STH1, a gene that is homologous to SNF2. STH1 is essential for mitotic growth and is functionally distinct from SNF2. A bifunctional STH1-beta-galactosidase protein is located in the nucleus. The predicted 155,914-Da STH1 protein is 72% identical to SNF2 over 661 amino acids and 46% identical over another stretch of 66 amino acids. Both STH1 and SNF2 contain a putative nucleoside triphosphate-binding site and sequences resembling the consensus helicase motifs. The large region of homology shared by STH1 and SNF2 is conserved among other eukaryotic proteins, and STH1 and SNF2 appear to define a novel family of proteins related to helicases.

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Albarrán, Letizia, José J. López, Luis J. Gómez, Ginés M. Salido, and Juan A. Rosado. "SARAF modulates TRPC1, but not TRPC6, channel function in a STIM1-independent manner." Biochemical Journal 473, no. 20 (October 11, 2016): 3581–95. http://dx.doi.org/10.1042/bcj20160348.

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Canonical transient receptor potential-1 (TRPC1) is an almost ubiquitously expressed channel that plays a relevant role in cell function. As other TRPC members, TRPC1 forms receptor-operated cation channels that exhibit both STIM1-dependent and store-independent behaviour. The STIM1 inhibitor SARAF (for store-operated Ca2+ entry (SOCE)-associated regulatory factor) modulates SOCE by interaction with the STIM1 region responsible for Orai1 activation (SOAR). Furthermore, SARAF modulates Ca2+ entry through the arachidonate-regulated Ca2+ (ARC) channels, consisting of Orai1 and Orai3 heteropentamers and plasma membrane-resident STIM1. While a role for STIM1–Orai1-mediated signals has been demonstrated, the possible role of SARAF in TRPC1 function remains unknown. Here, we provide evidence for the interaction of SARAF with TRPC1, independently of STIM1 both in STIM1-deficient NG115-401L cells and SH-SY5Y cells endogenously expressing STIM1. Silencing of SARAF expression in STIM1-deficient cells demonstrated that SARAF plays a negative regulatory role in TRPC1-mediated Ca2+ entry. The interaction of SARAF with TRPC1 in STIM1-deficient cells, as well as with the TRPC1 pool not associated with STIM1 in STIM1-expressing cells was enhanced by stimulation with the physiological agonist ATP. In contrast with TRPC1, we found that the interaction between SARAF and TRPC6 was constitutive rather than inducible by agonist stimulation. Furthermore, we found that SARAF expression silencing was without effect on Ca2+ entry evoked by agonists in TRPC6 overexpressing cells, as well as in Ca2+ influx evoked by the TRPC6 activator Hyp9. These findings provide evidence for a new regulator of TRPC1 channel function and highlight the relevance of SARAF in intracellular Ca2+ homeostasis.

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Lee, Keon Jin, Jin Seok Woo, Ji-Hye Hwang, Changdo Hyun, Chung-Hyun Cho, Do Han Kim, and Eun Hui Lee. "STIM1 negatively regulates Ca2+ release from the sarcoplasmic reticulum in skeletal myotubes." Biochemical Journal 453, no. 2 (June 28, 2013): 187–200. http://dx.doi.org/10.1042/bj20130178.

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STIM1 (stromal interaction molecule 1) mediates SOCE (store-operated Ca2+ entry) in skeletal muscle. However, the direct role(s) of STIM1 in skeletal muscle, such as Ca2+ release from the SR (sarcoplasmic reticulum) for muscle contraction, have not been identified. The times required for the maximal expression of endogenous STIM1 or Orai1, or for the appearance of puncta during the differentiation of mouse primary skeletal myoblasts to myotubes, were all different, and the formation of puncta was detected with no stimulus during differentiation, suggesting that, in skeletal muscle, the formation of puncta is a part of the differentiation. Wild-type STIM1 and two STIM1 mutants (Triple mutant, missing Ca2+-sensing residues but possessing the intact C-terminus; and E136X, missing the C-terminus) were overexpressed in the myotubes. The wild-type STIM1 increased SOCE, whereas neither mutant had an effect on SOCE. It was interesting that increases in the formation of puncta were observed in the Triple mutant as well as in wild-type STIM1, suggesting that SOCE-irrelevant puncta could exist in skeletal muscle. On the other hand, overexpression of wild-type or Triple mutant, but not E136X, attenuated Ca2+ releases from the SR in response to KCl [evoking ECC (excitation–contraction coupling) via activating DHPR (dihydropyridine receptor)] in a dominant-negative manner. The attenuation was removed by STIM1 knockdown, and STIM1 was co-immunoprecipitated with DHRP in a Ca2+-independent manner. These results suggest that STIM1 negatively regulates Ca2+ release from the SR through the direct interaction of the STIM1 C-terminus with DHPR, and that STIM1 is involved in both ECC and SOCE in skeletal muscle.

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Wang, Yanxia, Sarika Chaudhari, Yuezhong Ren, and Rong Ma. "Impairment of hepatic nuclear factor-4α binding to the Stim1 promoter contributes to high glucose-induced upregulation of STIM1 expression in glomerular mesangial cells." American Journal of Physiology-Renal Physiology 308, no. 10 (May 15, 2015): F1135—F1145. http://dx.doi.org/10.1152/ajprenal.00563.2014.

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The present study was carried out to investigate if hepatic nuclear factor (HNF)4α contributed to the high glucose-induced increase in stromal interacting molecule (STIM)1 protein abundance in glomerular mesangial cells (MCs). Western blot and immunofluorescence experiments showed HNF4α expression in MCs. Knockdown of HNF4α using a small interfering RNA approach significantly increased mRNA expression levels of both STIM1 and Orai1 and protein expression levels of STIM1 in cultured human MCs. Consistently, overexpression of HNF4α reduced expressed STIM1 protein expression in human embryonic kidney-293 cells. Furthermore, high glucose treatment did not significantly change the abundance of HNF4α protein in MCs but significantly attenuated HNF4α binding activity to the Stim1 promoter. Moreover, knockdown of HNF4α significantly augmented store-operated Ca2+ entry, which is known to be gated by STIM1 and has recently been found to be antifibrotic in MCs. In agreement with those results, knockdown of HNF4α significantly attenuated the fibrotic response of high glucose. These results suggest that HNF4α negatively regulates STIM1 transcription in MCs. High glucose increases STIM1 expression levels by impairing HNF4α binding activity to the Stim1 promoter, which subsequently releases Stim1 transcription from HNF4α repression. Since the STIM1-gated store-operated Ca2+ entry pathway in MCs has an antifibrotic effect, inhibition of HNF4α in MCs might be a potential therapeutic option for diabetic kidney disease.

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Chang, H. C., D. F. Nathan, and S. Lindquist. "In vivo analysis of the Hsp90 cochaperone Sti1 (p60)." Molecular and Cellular Biology 17, no. 1 (January 1997): 318–25. http://dx.doi.org/10.1128/mcb.17.1.318.

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Hsp90 interacts with Sti1 (p60) in lysates of yeast and vertebrate cells. Here we provide the first analysis of their interaction in vivo. Saccharomyces cerevisiae mutations that eliminate Sti1 or reduce intracellular concentrations of Hsp90 individually have little or no effect on growth at normal temperatures. However, when combined, the mutations greatly reduce or eliminate growth. Furthermore, overexpression of Sti1 has allele-specific effects on cells carrying various hsp90ts point mutations. These genetic interactions provide strong evidence that Hsp90 and Sti1 interact in vivo and that their functions are closely allied. Indeed, deletion of STI1 reduces the in vivo activity of the Hsp90 target protein, glucocorticoid receptor (GR). Mutations in GR that eliminate interaction with Hsp90 also eliminate the effects of the sti1 deletion. Examination of GR protein complexes in the sti1 deletion mutant reveals a selective increase in the concentration of GR-Ydj1 complexes, supporting previous hypotheses that Ydj1 functions at an early step in the maturation of GR and that Sti1 acts at an intermediate step. Deletion of STI1 also reduces the in vivo activity of another, unrelated Hsp90 target protein, v-Src. Our data indicate that Sti1 is a general factor in the maturation of Hsp90 target proteins and support earlier suggestions that Hsp90 matures even very different target proteins by a similar mechanism.

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Journal articles on the topic 'STM1'

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