Academic literature on the topic 'Scd6 C-terminal'
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Journal articles on the topic "Scd6 C-terminal"
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Chang, Eric, Geoffrey Bartholomeusz, Ruth Pimental, Jing Chen, Hong Lai, Li-hua L. Wang, Peirong Yang, and Stevan Marcus. "Direct Binding and In Vivo Regulation of the Fission Yeast p21-Activated Kinase Shk1 by the SH3 Domain Protein Scd2." Molecular and Cellular Biology 19, no. 12 (December 1, 1999): 8066–74. http://dx.doi.org/10.1128/mcb.19.12.8066.
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ABSTRACT The Ste20/p21-activated kinase homolog Shk1 is essential for viability and required for normal morphology, mating, and cell cycle control in the fission yeast Schizosaccharomyces pombe. Shk1 is regulated by the p21 G protein Cdc42, which has been shown to form a complex with the SH3 domain protein Scd2 (also called Ral3). In this study, we investigated whether Scd2 plays a role in regulating Shk1 function. We found that recombinant Scd2 and Shk1 interact directly in vitro and that they interact in vivo, as determined by the two-hybrid assay and genetic analyses in fission yeast. The second of two N-terminal SH3 domains of Scd2 is both necessary and sufficient for interaction with Shk1. While full-length Scd2 interacted with only the R1 N-terminal regulatory subdomain of Shk1, a C-terminal deletion mutant of Scd2 interacted with both the R1 and R3 subdomains of Shk1, suggesting that the non-SH3 C-terminal domain of Scd2 may be involved in defining specificity in SH3 binding domain recognition. Overexpression of Scd2 stimulated the autophosphorylation activity of wild-type Shk1 in fission yeast but, consistent with results of genetic analyses, did not stimulate the activity of a Shk1 protein lacking the R1 subdomain. Results of additional two-hybrid experiments suggest that Scd2 may stimulate Shk1 catalytic function, at least in part, by positively modulating protein-protein interaction between Cdc42 and Shk1. We propose that Scd2 functions as an organizing center, or scaffold, for the Cdc42 complex in fission yeast and that it acts in concert with Cdc42 to positively regulate Shk1 function.
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Nelson, K. K., M. Holmer, and S. K. Lemmon. "SCD5, a suppressor of clathrin deficiency, encodes a novel protein with a late secretory function in yeast." Molecular Biology of the Cell 7, no. 2 (February 1996): 245–60. http://dx.doi.org/10.1091/mbc.7.2.245.
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Clathrin and its associated proteins constitute a major class of coat proteins involved in vesicle budding during membrane transport. An interesting characteristic of the yeast clathrin heavy chain gene (CHC1) is that in some strains a CHC1 deletion is lethal, while in others it is not. Recently, our laboratory developed a screen that identified five multicopy suppressors that can rescue lethal strains of clathrin heavy chain-deficient yeast (Chc - scd1-i) to viability. One of these suppressors, SCD5, encodes a novel protein of 872 amino acids containing two regions of repeated motifs of unknown function. Deletion of SCD5 has shown that it is essential for cell growth at 30 degrees C. scd5-delta strains carrying low copy plasmids encoding C-terminal truncations of Scd5p are temperature sensitive for growth at 37 degrees C. At the nonpermissive temperature, cells expressing a 338-amino acid deletion (Scd5P-delta 338) accumulate an internal pool of fully glycosylated invertase and mature alpha-factor, while processing and sorting of the vacuolar hydrolase carboxypeptidase Y is normal. The truncation mutant also accumulates 80- to 100-nm vesicles similar to many late sec mutants. Moreover, at 34 degrees C, overexpression of Scd5p suppresses the temperature sensitivity of a sec2 mutant, which is blocked at a post-Golgi step of the secretory pathway. Biochemical analyses indicate that approximately 50% of Scd5p sediments with a 100,000 x g membrane fraction and is associated as a peripheral membrane protein. Overall, these results indicate that Scd5p is involved in vesicular transport at a late stage of the secretory pathway. Furthermore, this suggests that the lethality of clathrin-deficient yeast can be rescued by modulation of vesicular transport at this late secretory step.
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Christiansen, Dale, Patricia Devaux, Brigitte Réveil, Alexey Evlashev, Branka Horvat, Josette Lamy, Chantal Rabourdin-Combe, Jacques H. M. Cohen, and Denis Gerlier. "Octamerization Enables Soluble CD46 Receptor To Neutralize Measles Virus In Vitro and In Vivo." Journal of Virology 74, no. 10 (May 15, 2000): 4672–78. http://dx.doi.org/10.1128/jvi.74.10.4672-4678.2000.
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ABSTRACT A chimeric fusion protein encompassing the CD46 ectodomain linked to the C-terminal part of the C4b binding protein (C4bp) α chain (sCD46-C4bpα) was produced in eukaryotic cells. This protein, secreted as a disulfide-linked homo-octamer, was recognized by a panel of anti-CD46 antibodies with varying avidities. Unlike monomeric sCD46, the octameric sCD46-C4bpα protein was devoid of complement regulatory activity. However, sCD46-C4bpα was able to bind to the measles virus hemagglutinin protein expressed on murine cells with a higher avidity than soluble monomeric sCD46. Moreover, the octameric sCD46-C4bpα protein was significantly more efficient than monomeric sCD46 in inhibiting virus binding to CD46, in blocking virus induced cell-cell fusion, and in neutralizing measles virus in vitro. In addition, the octameric sCD46-C4bpα protein, but not the monomeric sCD46, fully protected CD46 transgenic mice against a lethal intracranial measles virus challenge.
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Zhao, Xiaoyang, Min Wang, Jingjing Liu, and Xiong Su. "Stearoyl CoA Desaturase 1 and Inositol-Requiring Protein 1α Determine the Efficiency of Oleic Acid in Alleviating Silica Nanoparticle-Induced Insulin Resistance." Journal of Biomedical Nanotechnology 17, no. 7 (July 1, 2021): 1349–63. http://dx.doi.org/10.1166/jbn.2021.3109.
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Despite the widespread use of silica nanoparticles (SiNPs), their metabolic impact and mechanisms of action have not been well studied. Exposure to SiNPs induces insulin resistance (IR) in hepatocytes by endoplasmic reticulum (ER) stress via inositol-requiring protein 1α (IRE1α) activation of c-Jun N-terminal kinases (JNK). It has been well established that stearoyl CoA desaturase (SCD1) and its major product oleic acid elicited beneficial effects in restoring ER homeostasis. However, the potential coordination of SCD1 and IRE1α in determining SiNP regulation of insulin signaling is unclear. Herein, we investigated the effects of SCD1 and oleic acid on IR induced by SiNPs or thapsigargin in hepatocytes. SCD1 overexpression or oleic acid efficiently reversed SiNP-induced ER stress and IR, whereas the effects of thapsigargin treatment could not be restored. Thapsigargin diminished SCD1 protein levels, leading to the accumulation of IRE1α and sustained activation of the IRE1α/JNK pathway. Moreover, knockdown of activating transcription factor 4 (ATF4) upstream of SCD1 suppressed SiNP-induced SCD1 expression, rescued the activated IRE1α, and inhibited insulin signaling but was not able to restore the effects of thapsigargin. Collectively, downregulation of SCD1 and excess accumulation of IRE1α protein prevented the beneficial effects of exogenous oleic acid on IR induced by ER stress. Our results provide valuable mechanistic insights into the synergic regulation of IR by SiNPs and ER stress and suggest a combinational strategy to restore ER homeostasis by targeting SCD1 and IRE1α proteins, as well as supplementation of unsaturated fatty acids.
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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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Henry, Kenneth R., Kathleen D'Hondt, JiSuk Chang, Thomas Newpher, Kristen Huang, R. Tod Hudson, Howard Riezman, and Sandra K. Lemmon. "Scd5p and Clathrin Function Are Important for Cortical Actin Organization, Endocytosis, and Localization of Sla2p in Yeast." Molecular Biology of the Cell 13, no. 8 (August 2002): 2607–25. http://dx.doi.org/10.1091/mbc.e02-01-0012.
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SCD5 was identified as a multicopy suppressor of clathrin HC-deficient yeast. SCD5 is essential, but anscd5-Δ338 mutant, expressing Scd5p with a C-terminal truncation of 338 amino acids, is temperature sensitive for growth. Further studies here demonstrate that scd5-Δ338affects receptor-mediated and fluid-phase endocytosis and normal actin organization. The scd5-Δ338 mutant contains larger and depolarized cortical actin patches and a prevalence of G-actin bars.scd5-Δ338 also displays synthetic negative genetic interactions with mutations in several other proteins important for cortical actin organization and endocytosis. Moreover, Scd5p colocalizes with cortical actin. Analysis has revealed that clathrin-deficient yeast also have a major defect in cortical actin organization and accumulate G-actin. Overexpression ofSCD5 partially suppresses the actin defect of clathrin mutants, whereas combining scd5-Δ338 with a clathrin mutation exacerbates the actin and endocytic phenotypes. Both Scd5p and yeast clathrin physically associate with Sla2p, a homologue of the mammalian huntingtin interacting protein HIP1 and the related HIP1R. Furthermore, Sla2p localization at the cell cortex is dependent on Scd5p and clathrin function. Therefore, Scd5p and clathrin are important for actin organization and endocytosis, and Sla2p may provide a critical link between clathrin and the actin cytoskeleton in yeast, similar to HIP1(R) in animal cells.
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Papadaki, Piyi, Véronique Pizon, Brian Onken, and Eric C. Chang. "Two Ras Pathways in Fission Yeast Are Differentially Regulated by Two Ras Guanine Nucleotide Exchange Factors." Molecular and Cellular Biology 22, no. 13 (July 1, 2002): 4598–606. http://dx.doi.org/10.1128/mcb.22.13.4598-4606.2002.
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ABSTRACT How a given Ras prreotein coordinates multiple signaling inputs and outputs is a fundamental issue of signaling specificity. Schizosaccharomyces pombe contains one Ras, Ras1, that has two distinct outputs. Ras1 activates Scd1, a presumptive guanine nucleotide exchange factor (GEF) for Cdc42, to control morphogenesis and chromosome segregation, and Byr2, a component of a mitogen-activated protein kinase cascade, to control mating. So far there is only one established Ras1 GEF, Ste6. Paradoxically, ste6 null (ste6Δ) mutants are sterile but normal in cell morphology. This suggests that Ste6 specifically activates the Ras1-Byr2 pathway and that there is another GEF capable of activating the Scd1 pathway. We thereby characterized a potential GEF, Efc25. Genetic data place Efc25 upstream of the Ras1-Scd1, but not the Ras1-Byr2, pathway. Like ras1Δ and scd1Δ, efc25Δ is synthetically lethal with a deletion in tea1, a critical element for cell polarity control. Using truncated proteins, we showed that the C-terminal GEF domain of Efc25 is essential for function and regulated by the N terminus. We conclude that Efc25 acts as a Ras1 GEF specific for the Scd1 pathway. While ste6 expression is induced during mating, efc25 expression is constitutive. Moreover, Efc25 overexpression renders cells hyperelongated and sterile; the latter can be rescued by activated Ras1. This suggests that Efc25 can recruit Ras1 to selectively activate Scd1 at the expense of Byr2. Reciprocally, Ste6 overexpression can block Scd1 activation. We propose that external signals can partly segregate two Ras1 pathways by modulating GEF expression and that GEFs can influence how Ras is coupled to specific effectors.
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Zhuang, Zhen-Jie, Chao-Wen Shan, Bo Li, Min-Xia Pang, Han Wang, Yan Luo, Yin-lan Liu, et al. "Linarin Enriched Extract Attenuates Liver Injury and Inflammation Induced by High-Fat High-Cholesterol Diet in Rats." Evidence-Based Complementary and Alternative Medicine 2017 (2017): 1–9. http://dx.doi.org/10.1155/2017/4701570.
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The aim of this study was to explore the potential beneficial effects of linarin enriched Flos Chrysanthemi extract (Lin-extract) on nonalcoholic steatohepatitis (NASH) induced by high-fat high-cholesterol (HFHC) diet in rats. SD rats received normal diet, HFHC diet, or HFHC diet plus different doses of Lin-extract. The liver content of triglyceride and total cholesterol markedly increased in HFHC diet-fed model rats while middle and high dose of Lin-extract lowered liver cholesterol significantly. The expression of stearoyl-CoA desaturase (SCD1) was upregulated by HFHC diet and further elevated by high dose Lin-extract. High dose of Lin-extract also markedly lowered the serum alanine aminotransferase (ALT) and aspartate aminotransferase (AST) and inhibited the activation of c-Jun N-terminal kinase (JNK) induced by HFHC in livers. The HFHC-increased mRNA levels of hepatic inflammation cytokines, including monocyte chemotactic protein-1 (MCP-1), tumor necrosis factor-α(TNF-α), and chemokine (C-X-C motif) ligand 1 (CXCL1), were suppressed by Lin-extract dose-dependently. Furthermore, pathology evaluation showed that high dose Lin-extract greatly improved lobular inflammation. Our results suggest that Lin-extract could attenuate liver injury and inflammation induced by HFHC diet in rats. Its modulatory effect on lipid metabolism may partially contribute to this protective effect.
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Yu, Wenjie, Cheng-Zhen Chen, Yanxia Peng, Ze Li, Yan Gao, Shuang Liang, Bao Yuan, Nam-Hyung Kim, Hao Jiang, and Jia-Bao Zhang. "KRAS Affects Adipogenic Differentiation by Regulating Autophagy and MAPK Activation in 3T3-L1 and C2C12 Cells." International Journal of Molecular Sciences 22, no. 24 (December 20, 2021): 13630. http://dx.doi.org/10.3390/ijms222413630.
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Kirsten rat sarcoma 2 viral oncogene homolog (Kras) is a proto-oncogene that encodes the small GTPase transductor protein KRAS, which has previously been found to promote cytokine secretion, cell survival, and chemotaxis. However, its effects on preadipocyte differentiation and lipid accumulation are unclear. In this study, the effects of KRAS inhibition on proliferation, autophagy, and adipogenic differentiation as well as its potential mechanisms were analyzed in the 3T3-L1 and C2C12 cell lines. The results showed that KRAS was localized mainly in the nuclei of 3T3-L1 and C2C12 cells. Inhibition of KRAS altered mammalian target of rapamycin (Mtor), proliferating cell nuclear antigen (Pcna), Myc, peroxisome proliferator-activated receptor γ (PPARγ), CCAAT/enhancer binding protein beta (C/ebp-β), diacylglycerol O-acyltransferase 1 (Dgat1), and stearoyl-coenzyme A desaturase 1 (Scd1) expression, thereby reducing cell proliferation capacity while inducing autophagy, enhancing differentiation of 3T3-L1 and C2C12 cells into mature adipocytes, and increasing adipogenesis and the capacity to store lipids. Moreover, during differentiation, KRAS inhibition reduced the levels of extracellular regulated protein kinases (ERK), c-Jun N-terminal kinase (JNK), p38, and phosphatidylinositol 3 kinase (PI3K) activation. These results show that KRAS has unique regulatory effects on cell proliferation, autophagy, adipogenic differentiation, and lipid accumulation.
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Jung, Tae Woo, Sun-Young Kim, Da-Som Kim, Eui-Cheol Shin, Yong Bae Park, and Kyoung-Tae Lee. "Euodia daniellii Hemsl. (Bee-Bee Tree) Oil Attenuates Palmitate-Induced Lipid Accumulation and Apoptosis in Hepatocytes." Pharmacology 101, no. 5-6 (2018): 298–308. http://dx.doi.org/10.1159/000487892.
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Hepatic lipid accumulation and apoptosis is elevated in patients with non-alcoholic steatohepatitis and is closely associated with severity. Saturated fatty acid palmitate stimulates lipid accumulation and apoptosis in hepatocytes. In the present study, we examined bee-bee tree oil (BO)-mediated protective effects on palmitate-induced lipid accumulation and apoptosis in mouse primary hepatocytes. Cells were cultured in a control media or the same media containing 150 or 300 µmol/L of albumin-bound palmitate for 24 h. BO concentrations used were 0, 0.1, 0.2, or 0.5%. Palmitate induced lipid accumulation and mRNA expression of lipogenic genes such as SREBP1c and SCD1. However, BO prevented these changes. Furthermore, palmitate stimulated caspase-3 activity and decreased cell viability in the absence of BO. BO reduced palmitate-induced activation of caspase-3 and cell death in a dose-dependent manner. AMP-activated protein kinase inhibitors abolished the effects of BO. Furthermore, BO suppressed palmitate-induced c-Jun N-terminal kinase (JNK) phosphorylation through the 5' adenosine monophosphate-activated protein kinase (AMPK)-dependent pathway. In conclusion, BO attenuated palmitate-induced hepatic steatosis and apoptosis through AMPK-mediated suppression of JNK signaling. These data suggest that BO is an important determinant of saturated fatty acid-induced lipid accumulation and apoptosis, and may be an effective therapeutic strategy for treatment of obesity-mediated liver diseases.
Dissertations / Theses on the topic "Scd6 C-terminal"
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Tsou, Wei-Ling, and 鄒瑋玲. "Analyzing C-terminal alternative splicing of Cav2.1and developing the Splice-Isoform-Specific RNAi as apotential therapeutic strategy for SCA6." Thesis, 2011. http://ndltd.ncl.edu.tw/handle/67428207508990682896.
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博士國立陽明大學
神經科學研究所
99
Spinocerebellar ataxia type 6 (SCA6) is an inherited neurodegenerative disorder characterized by the preferential degeneration of cerebellar Purkinje cells. SCA6 is caused by a polyglutamine (polyQ)-coding CAG repeat expansion in the 3’ end of the CACNA1A gene, which encodes the P/Q-type voltage-gated calcium channel alpha1A subunit Cav2.1. Purkinje cells express two major Cav2.1 mRNA splice isoforms (protein variants). The “long” variant (V2) contains the pathogenic polyglutamine expansion in the C-terminal tail, whereas the “short” variant (V1) lacks the polyglutamine tract. No effective treatments are currently available to combat this relentlessly progressive disorder; therefore, there is a pressing need to develop safe and efficacious therapies for preventing the neurodegeneration associated with SCA6. RNA interference is a promising therapeutic approach for neurodegenerative diseases, including various autosomal dominant spinocerebellar ataxias. Taking advantage of alternative splicing near the 3’ end of Cav2.1 transcripts, we designed splice isoform-specific (SIS)-RNAi molecules to selectively suppress expression of the polyQ-coding variant (V2). Embedding anti-SCA6 siRNAs within the context of a modified, brain-specific human miR-124 led to improved splice-specific target suppression compared to first generation shRNA platforms. We identified 3’ end base pair modifications in fully processed anti-SCA6 guide strands, supporting the proper recognition of these novel artificial miR124-based constructs by the cellular RNAi machinery. In the Cav2.1 mini-gene reporter system, CAG expansions were also found to enhance splicing activity at the 3’ end of Cav2.1, leading to a selective increase in the levels of polyQ-containing Cav2.1 variants, which may contribute to SCA6 disease pathogenesis. We cloned U6-miR124 expression cassettes into a recombinant adeno-associated viral (rAAV) vector for in vivo testing. Laser capture microdissection (LCM) of mouse Purkinje cells for Cav2.1 mRNA quantification revealed that the injection of mice with a low dose of rAAV-miR124 significantly reduced endogenous Cav2.1 expression. Unexpectedly, injection of high levels of rAAV induced significant neurotoxicity in mouse Purkinje neurons. Our results support the preclinical development of SIS-RNAi as a novel therapeutic approach for the treatment of SCA6; however, improper levels of rAAV-mediated delivery could be a potential concern. The long-term safety and efficacy of rAAV-mediated miRNA delivery should be further investigated in mouse models.