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Journal articles on the topic 'Mucolipin'

Author: Grafiati

Published: 9 March 2023

Last updated: 10 March 2023

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1

Puertollano, Rosa, and Kirill Kiselyov. "TRPMLs: in sickness and in health." American Journal of Physiology-Renal Physiology 296, no. 6 (June 2009): F1245—F1254. http://dx.doi.org/10.1152/ajprenal.90522.2008.

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TRPML1, TRPML2 and TRPML3 belong to the mucolipin family of the TRP superfamily of ion channels. The founding member of this family, TRPML1, was cloned during the search for the genetic determinants of the lysosomal storage disease mucolipidosis type IV (MLIV). Mucolipins are predominantly expressed within the endocytic pathway, where they appear to regulate membrane traffic and/or degradation. The physiology of mucolipins raises some of the most interesting questions of modern cell biology. Their traffic and localization is a multistep process involving a system of adaptor proteins, while their ion channel activity possibly exemplifies the rare cases of regulation of endocytic traffic and hydrolysis by ion channels. Finally, dysregulation of mucolipins results in cell death leading to neurodegenerative phenotypes of MLIV and of the varitint-waddler mouse model of familial deafness. The present review discusses current knowledge and questions regarding this novel family of disease-relevant ion channels with a specific focus on mucolipin regulation and their role in membrane traffic and cell death. Since mucolipins are ubiquitously expressed, this review may be useful for a wide audience of basic biologists and clinicians.

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2

Vergarajauregui, Silvia, Ross Oberdick, Kirill Kiselyov, and Rosa Puertollano. "Mucolipin 1 channel activity is regulated by protein kinase A-mediated phosphorylation." Biochemical Journal 410, no. 2 (February 12, 2008): 417–25. http://dx.doi.org/10.1042/bj20070713.

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Mucolipins constitute a family of cation channels with homology with the transient receptor potential family. Mutations in MCOLN1 (mucolipin 1) have been linked to mucolipidosis type IV, a recessive lysosomal storage disease characterized by severe neurological and ophthalmologic abnormalities. At present, little is known about the mechanisms that regulate MCOLN1 activity. In the present paper, we addressed whether MCOLN1 activity is regulated by phosphorylation. We identified two PKA (protein kinase A) consensus motifs in the C-terminal tail of MCOLN1, containing Ser557 and Ser559. Ser557 was the principal phosphorylation site, as mutation of this residue to alanine caused a greater than 75% reduction in the total levels of phosphorylated MCOLN1 C-terminal tail. Activation of PKA with forskolin promoted MCOLN1 phosphorylation, both in vitro and in vivo. In contrast, addition of the PKA inhibitor H89 abolished MCOLN1 phosphorylation. We also found that PKA-mediated phosphorylation regulates MCOLN1 channel activity. Forskolin treatment decreased MCOLN1 channel activity, whereas treatment with H89 increased MCOLN1 channel activity. The stimulatory effect of H89 on MCOLN1 function was not observed when Ser557 and Ser559 were mutated to alanine residues, indicating that these two residues are essential for PKA-mediated negative regulation of MCOLN1. This paper presents the first example of regulation of a member of the mucolipin family by phosphorylation.

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3

Lima, W. C., F. Leuba, T. Soldati, and P. Cosson. "Mucolipin controls lysosome exocytosis in Dictyostelium." Journal of Cell Science 125, no. 9 (February 22, 2012): 2315–22. http://dx.doi.org/10.1242/jcs.100362.

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4

Curcio-Morelli, Cyntia, Peng Zhang, Bhuvarahamurthy Venugopal, Florie A. Charles, Marsha F. Browning, Horacio F. Cantiello, and Susan A. Slaugenhaupt. "Functional multimerization of mucolipin channel proteins." Journal of Cellular Physiology 222, no. 2 (February 2010): 328–35. http://dx.doi.org/10.1002/jcp.21956.

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5

Zufferey, Madeleine, and Cedric Blanc. "The RA11 and RA12 antibodies recognize a peptide of the D. discoideum Mucolipin protein by western blot." Antibody Reports 3, no. 1 (February 6, 2020): e127. http://dx.doi.org/10.24450/journals/abrep.2020.e127.

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6

Bach, Gideon. "Mucolipin 1: endocytosis and cation channel—a review." Pflügers Archiv - European Journal of Physiology 451, no. 1 (November 27, 2004): 313–17. http://dx.doi.org/10.1007/s00424-004-1361-7.

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7

Al-Alawi, Badriya, Beena Harikrishna, Khalid Al-Thihli, Sana Al Zuhabi, Anuradha Ganesh, Zainab Al Hashami, Zeyana Al Dhamhmani, Razan Zadjali, Nafila B. Al Riyami, and Fahad Zadjali. "Mucolipidosis Type IV in Omani Families with a Novel MCOLN1 Mutation: Search for Evidence of Founder Effect." Genes 13, no. 2 (January 28, 2022): 248. http://dx.doi.org/10.3390/genes13020248.

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Mucolipidosis Type IV (MLIV) is caused by a deficiency of the mucolipin cation channel encoded by Mucolipin TRP Cation Channel 1 gene (MCOLN1). It is a slowly progressive neurodevelopmental and neurodegenerative disorder causing severe psychomotor developmental delay and progressive visual impairment, which is often misdiagnosed as cerebral palsy. We describe six patients with MLIV from two Omani families with a novel c.237+5G>A mutation in the MCOLN1 gene predicted to affect mRNA splicing. Mutation screening with a high-resolution melting (HRM) assay in a large population sample did not detect this mutation in control subjects. This report highlights the importance of considering MLIV in the differential diagnosis of patients in a pediatric age group with cerebral palsy-like presentation. Although the same rare mutation was seen in two apparently unrelated families, this was not seen in the sample screened from the general population. The HRM assay provides a cost-effective assay for population screening for the c.237+5G>A mutation.

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8

Thompson, Eric G., Lara Schaheen, Hope Dang, and Hanna Fares. "Lysosomal trafficking functions of mucolipin-1 in murine macrophages." BMC Cell Biology 8, no. 1 (2007): 54. http://dx.doi.org/10.1186/1471-2121-8-54.

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9

Curcio-Morelli, Cyntia, Florie A. Charles, Matthew C. Micsenyi, Yi Cao, Bhuvarahamurthy Venugopal, Marsha F. Browning, Kostantin Dobrenis, Susan L. Cotman, Steven U. Walkley, and Susan A. Slaugenhaupt. "Macroautophagy is defective in mucolipin-1-deficient mouse neurons." Neurobiology of Disease 40, no. 2 (November 2010): 370–77. http://dx.doi.org/10.1016/j.nbd.2010.06.010.

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10

Bach, Gideon, David A. Zeevi, Ayala Frumkin, and Aviram Kogot-Levin. "Mucolipidosis type IV and the mucolipins." Biochemical Society Transactions 38, no. 6 (November 24, 2010): 1432–35. http://dx.doi.org/10.1042/bst0381432.

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MLIV (mucolipidosis type IV) is a neurodegenerative lysosomal storage disorder caused by mutations in MCOLN1, a gene that encodes TRPML1 (mucolipin-1), a member of the TRPML (transient receptor potential mucolipin) cation channels. Two additional homologues are TRPML2 and TRPML3 comprising the TRPML subgroup in the TRP superfamily. The three proteins play apparently key roles along the endocytosis process, and thus their cellular localization varies among the different group members. Thus TRPML1 is localized exclusively to late endosomes and lysosomes, TRPML2 is primarily located in the recycling clathrin-independent GPI (glycosylphosphatidylinositol)-anchored proteins and early endosomes, and TRPML3 is primarily located in early endosomes. Apparently, all three proteins' main physiological function underlies Ca2+ channelling, regulating the endocytosis process. Recent findings also indicate that the three TRPML proteins form heteromeric complexes at least in some of their cellular content. The physiological role of these complexes in lysosomal function remains to be elucidated, as well as their effect on the pathophysiology of MLIV. Another open question is whether any one of the TRPMLs bears additional function in channel activity

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11

Yang, Yiming, Xingjian Zhai, and Yassine El Hiani. "TRPML1—Emerging Roles in Cancer." Cells 9, no. 12 (December 13, 2020): 2682. http://dx.doi.org/10.3390/cells9122682.

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The mucolipin-1 (TRPML1) channel maintains lysosomal ionic homeostasis and regulates autophagic flux. Defects of TRPML1 lead to lysosomal storage diseases and neurodegeneration. In this report, we discuss emerging evidence pertaining to differential regulation of TRPML1 signaling pathways in cancer progression with the goal of leveraging the oncogenic potential of TRPML1 to inspire therapeutic interventions.

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12

Zhang, Xiaoli, Wei Chen, Qiong Gao, Junsheng Yang, Xueni Yan, Han Zhao, Lin Su, et al. "Rapamycin directly activates lysosomal mucolipin TRP channels independent of mTOR." PLOS Biology 17, no. 5 (May 21, 2019): e3000252. http://dx.doi.org/10.1371/journal.pbio.3000252.

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13

Curcio-Morelli, Cyntia, Florie A. Charles, Matthew C. Micsenyi, Yi Cao, Bhuvarahamurthy Venugopal, Marsha F. Browning, Kostantin Dobrenis, Susan L. Cotman, Steven U. Walkley, and Susan A. Slaugenhaupt. "34. Macroautophagy is defective in mucolipin 1-deficient mouse neurons." Molecular Genetics and Metabolism 99, no. 2 (February 2010): S15. http://dx.doi.org/10.1016/j.ymgme.2009.10.051.

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14

Cantiello, Horacio F., Nicolás Montalbetti, Wolfgang H. Goldmann, Malay K. Raychowdhury, Silvia González-Perrett, Gustavo A. Timpanaro, and Bernard Chasan. "Cation channel activity of mucolipin-1: the effect of calcium." Pflügers Archiv - European Journal of Physiology 451, no. 1 (August 23, 2005): 304–12. http://dx.doi.org/10.1007/s00424-005-1448-9.

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15

Valadez, Jessica A., and Math P. Cuajungco. "PAX5 is the transcriptional activator of mucolipin-2 (MCOLN2) gene." Gene 555, no. 2 (January 2015): 194–202. http://dx.doi.org/10.1016/j.gene.2014.11.003.

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16

Chenik, Mehdi, Feriel Douagi, Yosser Ben Achour, Noureddine Ben Khalef, Meriem Ouakad, Hechmi Louzir, and Koussay Dellagi. "Characterization of two different mucolipin-like genes from Leishmania major." Parasitology Research 98, no. 1 (October 21, 2005): 5–13. http://dx.doi.org/10.1007/s00436-005-0012-z.

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17

Weinstock, Laura D., Amanda M. Furness, Shawn S. Herron, Sierra S. Smith, Sitara B. Sankar, Samantha G. DeRosa, Dadi Gao, et al. "Fingolimod phosphate inhibits astrocyte inflammatory activity in mucolipidosis IV." Human Molecular Genetics 27, no. 15 (May 16, 2018): 2725–38. http://dx.doi.org/10.1093/hmg/ddy182.

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Abstract Mucolipidosis IV (MLIV) is an orphan neurodevelopmental disease that causes severe neurologic dysfunction and loss of vision. Currently there is no therapy for MLIV. It is caused by loss of function of the lysosomal channel mucolipin-1, also known as TRPML1. Knockout of the Mcoln1 gene in a mouse model mirrors clinical and neuropathologic signs in humans. Using this model, we previously observed robust activation of microglia and astrocytes in early symptomatic stages of disease. Here we investigate the consequence of mucolipin-1 loss on astrocyte inflammatory activation in vivo and in vitro and apply a pharmacologic approach to restore Mcoln1−/− astrocyte homeostasis using a clinically approved immunomodulator, fingolimod. We found that Mcoln1−/− mice over-express numerous pro-inflammatory cytokines, some of which were also over-expressed in astrocyte cultures. Changes in the cytokine profile in Mcoln1−/− astrocytes are concomitant with changes in phospho-protein signaling, including activation of PI3K/Akt and MAPK pathways. Fingolimod promotes cytokine homeostasis, down-regulates signaling within the PI3K/Akt and MAPK pathways and restores the lysosomal compartment in Mcoln1−/− astrocytes. These data suggest that fingolimod is a promising candidate for preclinical evaluation in our MLIV mouse model, which, in case of success, can be rapidly translated into clinical trial.

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18

Goldin, Ehud, Rafael C. Caruso, William Benko, Christine R. Kaneski, Stephanie Stahl, and Raphael Schiffmann. "Isolated Ocular Disease Is Associated with Decreased Mucolipin-1 Channel Conductance." Investigative Opthalmology & Visual Science 49, no. 7 (July 1, 2008): 3134. http://dx.doi.org/10.1167/iovs.07-1649.

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19

Miedel, Mark T., Kelly M. Weixel, Jennifer R. Bruns, Linton M. Traub, and Ora A. Weisz. "Posttranslational Cleavage and Adaptor Protein Complex-dependent Trafficking of Mucolipin-1." Journal of Biological Chemistry 281, no. 18 (March 3, 2006): 12751–59. http://dx.doi.org/10.1074/jbc.m511104200.

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20

Vergarajauregui, Silvia, and Rosa Puertollano. "Two Di-Leucine Motifs Regulate Trafficking of Mucolipin-1 to Lysosomes." Traffic 7, no. 3 (January 9, 2006): 337–53. http://dx.doi.org/10.1111/j.1600-0854.2006.00387.x.

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21

Morelli, Maria Beatrice, Consuelo Amantini, Daniele Tomassoni, Massimo Nabissi, Antonella Arcella, and Giorgio Santoni. "Transient Receptor Potential Mucolipin-1 Channels in Glioblastoma: Role in Patient’s Survival." Cancers 11, no. 4 (April 12, 2019): 525. http://dx.doi.org/10.3390/cancers11040525.

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A link between mucolipin channels and tumors has been recently suggested. Herein, we aim to investigate the transient receptor potential mucolipin (TRPML)-1 relevance in glioblastoma. The expression of this channel was evaluated via qRT-PCR and immunohistochemistry in biopsies from 66 glioblastoma patients and two human glioblastoma cell lines and compared to normal human brain, astrocytes, and epileptic tissues. The subcellular distribution of TRPML-1 was examined via confocal microscopy in the glioma cell lines. Then, to assess the role of TRPML-1, cell viability assays have been conducted in T98 and U251 cell lines treated with the specific TRPML-1 agonist, MK6-83. We found that MK6-83 reduced cell viability and induced caspase-3-dependent apoptosis. Indeed, the TRPML-1 silencing or the blockage of TRPML-1 dependent [Ca2+]i release abrogated these effects. In addition, exposure of glioma cells to the reactive oxygen species (ROS) inducer, carbonyl cyanide m-chlorophenylhydrazone (CCCP), stimulated a TRPML-1-dependent autophagic cell death, as demonstrated by the ability of the autophagic inhibitor bafilomycin A, the TRPML-1 inhibitor sphingomyelin, and the TRPML-1 silencing to completely inhibit the CCCP-mediated effects. To test a possible correlation with patient’s survival, Kaplan–Meier, univariate, and multivariate analysis have been performed. Data showed that the loss/reduction of TRPML-1 mRNA expression strongly correlates with short survival in glioblastoma (GBM) patients, suggesting that the reduction of TRPML-1 expression represents a negative prognostic factor in GBM patients.

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22

Zambon, Alberto A., Alexandra Lemaigre, Rahul Phadke, Stephanie Grunewald, Caroline Sewry, Anna Sarkozy, Emma Clement, and Francesco Muntoni. "Persistently elevated CK and lysosomal storage myopathy associated with mucolipin 1 defects." Neuromuscular Disorders 31, no. 3 (March 2021): 212–17. http://dx.doi.org/10.1016/j.nmd.2020.12.009.

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23

Pryor, Paul R., Frank Reimann, Fiona M. Gribble, and J. Paul Luzio. "Mucolipin-1 Is a Lysosomal Membrane Protein Required for Intracellular Lactosylceramide Traffic." Traffic 7, no. 10 (September 13, 2006): 1388–98. http://dx.doi.org/10.1111/j.1600-0854.2006.00475.x.

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24

Fares, Hanna, and Iva Greenwald. "Regulation of endocytosis by CUP-5, the Caenorhabditis elegans mucolipin-1 homolog." Nature Genetics 28, no. 1 (May 2001): 64–68. http://dx.doi.org/10.1038/ng0501-64.

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25

Santoni, Giorgio, Federica Maggi, Consuelo Amantini, Antonietta Arcella, Oliviero Marinelli, Massimo Nabissi, Matteo Santoni, and Maria Beatrice Morelli. "Coexpression of TRPML1 and TRPML2 Mucolipin Channels Affects the Survival of Glioblastoma Patients." International Journal of Molecular Sciences 23, no. 14 (July 13, 2022): 7741. http://dx.doi.org/10.3390/ijms23147741.

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Among brain cancers, glioblastoma (GBM) is the most malignant glioma with an extremely poor prognosis. It is characterized by high cell heterogeneity, which can be linked to its high malignancy. We have previously demonstrated that TRPML1 channels affect the OS of GBM patients. Herein, by RT-PCR, FACS and Western blot, we demonstrated that TRPML1 and TRPML2 channels are differently expressed in GBM patients and cell lines. Moreover, these channels partially colocalized in ER and lysosomal compartments in GBM cell lines, as evaluated by confocal analysis. Interestingly, the silencing of TRPML1 or TRPML2 by RNA interference results in the decrease in the other receptor at protein level. Moreover, the double knockdown of TRPML1 and TRPML2 leads to increased GBM cell survival with respect to single-channel-silenced cells, and improves migration and invasion ability of U251 cells. Finally, the Kaplan–Meier survival analysis demonstrated that patients with high TRPML2 expression in absence of TRPML1 expression strongly correlates with short OS, whereas high TRPML1 associated with low TRPML2 mRNA expression correlates with longer OS in GBM patients. The worst OS in GBM patients is associated with the loss of both TRPML1 and TRPML2 channels.

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26

Lelouvier, Benjamin, and Rosa Puertollano. "Mucolipin-3 Regulates Luminal Calcium, Acidification, and Membrane Fusion in the Endosomal Pathway." Journal of Biological Chemistry 286, no. 11 (January 18, 2011): 9826–32. http://dx.doi.org/10.1074/jbc.m110.169185.

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27

LaPlante, Janice M., C. P. Ye, Stephen J. Quinn, Ehud Goldin, Edward M. Brown, Susan A. Slaugenhaupt, and Peter M. Vassilev. "Functional links between mucolipin-1 and Ca2+-dependent membrane trafficking in mucolipidosis IV." Biochemical and Biophysical Research Communications 322, no. 4 (October 2004): 1384–91. http://dx.doi.org/10.1016/j.bbrc.2004.08.045.

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28

Sharma, Deep, Rekha Rana, and Kiran Thakur. "A REVIEW ON ROLE OF TRPV CATION CHANNELS." Journal of Biomedical and Pharmaceutical Research 10, no. 2 (March 30, 2021): 32–51. http://dx.doi.org/10.32553/jbpr.v10i2.857.

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The mammalian branch of the Transient Receptor Potential (TRP) superfamily of cation channels consists of 28 members. They can be subdivided in six main subfamilies: the TRPC (‘Canonical’), TRPV (‘Vanilloid’), TRPM (‘Melastatin’), TRPP (‘Polycystin’), TRPML (‘Mucolipin’) and the TRPA (‘Ankyrin’) group. The TRPV subfamily comprises channels that are critically involved in nociception and thermo-sensing (TRPV1, TRPV2, TRPV3, TRPV4) as well as highly Ca2+ selective channels involved in Ca2+ absorption/ reabsorption in mammals (TRPV5, TRPV6). In this review we summarize fundamental physiological properties of all TRPV members in the light of various cellular functions of these channels and their significance in the various diseases.

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29

Wang, Haitao, Yan Dong, Baijie Wan, Yinghua Ji, and Qiufang Xu. "Identification and Characterization Analysis of Transient Receptor Potential Mucolipin Protein of Laodelphax striatellus Fallén." Insects 12, no. 12 (December 12, 2021): 1107. http://dx.doi.org/10.3390/insects12121107.

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Transient receptor potential mucolipin (TRPML) protein in flies plays a pivotal role in Ca2+ ions release, resulting in membrane trafficking, autophagy and ion homeostasis. However, to date, the characterization of TRPML in agricultural pests remains unknown. Here, we firstly reported the TRPML of a destructive pest of gramineous crops, Laodelphax striatellus. The L. striatellus TRPML (Ls-TRPML) has a 1818 bp open reading frame, encoding 605 amino acid. TRPML in agricultural pests is evolutionarily conserved, and the expression of Ls-TRPML is predominately higher in the ovary than in other organs of L. striatellus at the transcript and protein level. The Bac–Bac system showed that Ls-TRPML localized in the plasma membrane, nuclear membrane and nucleus and co-localized with lysosome in Spodoptera frugiperda cells. The immunofluorescence microscopy analysis showed that Ls-TRPML localized in the cytoplasm and around the nuclei of the intestine cells or ovary follicular cells of L. striatellus. The results from the lipid-binding assay revealed that Ls-TRPML strongly bound to phosphatidylinositol-3,5-bisphosphate, as compared with other phosphoinositides. Overall, our results helped is identify and characterize the TRPML protein of L. striatellus, shedding light on the function of TRPML in multiple cellular processes in agricultural pests.

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30

Kilpatrick, Bethan S., Elizabeth Yates, Christian Grimm, Anthony H. Schapira, and Sandip Patel. "Endo-lysosomal TRP mucolipin-1 channels trigger global ER Ca2+release and Ca2+influx." Journal of Cell Science 129, no. 20 (August 30, 2016): 3859–67. http://dx.doi.org/10.1242/jcs.190322.

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31

Karacsonyi, Claudia, Anitza San Miguel, and Rosa Puertollano. "Mucolipin-2 Localizes to the Arf6-Associated Pathway and Regulates Recycling of GPI-APs." Traffic 8, no. 10 (July 5, 2007): 1404–14. http://dx.doi.org/10.1111/j.1600-0854.2007.00619.x.

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32

Kiselyov, Kirill. "The mucolipin-1 TRPML1 ion channel transmembrane-163 TMEM163 protein and lysosomal zinc handling." Frontiers in Bioscience 22, no. 8 (2017): 1330–43. http://dx.doi.org/10.2741/4546.

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33

Raychowdhury, M. K. "Molecular pathophysiology of mucolipidosis type IV: pH dysregulation of the mucolipin-1 cation channel." Human Molecular Genetics 13, no. 6 (January 20, 2004): 617–27. http://dx.doi.org/10.1093/hmg/ddh067.

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34

Xiong, Jian, Xinghua Feng, and Michael X. Zhu. "Targeting Sequence and Function-Dependence of Subcellular Localization of Transient Receptor Potential Mucolipin Channels." Biophysical Journal 110, no. 3 (February 2016): 613a—614a. http://dx.doi.org/10.1016/j.bpj.2015.11.3275.

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35

Li, Xiaobing, Shin-ichiroh Saitoh, Takuma Shibata, Natsuko Tanimura, Ryutaro Fukui, and Kensuke Miyake. "Mucolipin 1 positively regulates TLR7 responses in dendritic cells by facilitating RNA transportation to lysosomes." International Immunology 27, no. 2 (September 19, 2014): 83–94. http://dx.doi.org/10.1093/intimm/dxu086.

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36

Treusch, S., S. Knuth, S. A. Slaugenhaupt, E. Goldin, B. D. Grant, and H. Fares. "Caenorhabditis elegans functional orthologue of human protein h-mucolipin-1 is required for lysosome biogenesis." Proceedings of the National Academy of Sciences 101, no. 13 (March 15, 2004): 4483–88. http://dx.doi.org/10.1073/pnas.0400709101.

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37

Martina, Jose A., Benjamin Lelouvier, and Rosa Puertollano. "The Calcium Channel Mucolipin-3 is a Novel Regulator of Trafficking Along the Endosomal Pathway." Traffic 10, no. 8 (August 2009): 1143–56. http://dx.doi.org/10.1111/j.1600-0854.2009.00935.x.

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38

Cuajungco, Math P., Joshua Silva, Ania Habibi, and Jessica A. Valadez. "The mucolipin-2 (TRPML2) ion channel: a tissue-specific protein crucial to normal cell function." Pflügers Archiv - European Journal of Physiology 468, no. 2 (September 4, 2015): 177–92. http://dx.doi.org/10.1007/s00424-015-1732-2.

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39

Bishnoi, Mahendra, and Louis S. Premkumar. "Changes in TRP Channels Expression in Painful Conditions." Open Pain Journal 6, no. 1 (March 8, 2013): 10–22. http://dx.doi.org/10.2174/1876386301306010010.

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Over the last fifteen years after the successful cloning of the first nociceptive Transient Receptor Potential (TRP) channel, TRP Vanilloid 1, other members of the TRP channel family have been cloned, characterized and implicated in different modalities of pain. Tremendous progress has been made with regard to the specific role of these TRP channels in nociception using electrophysiological and molecular methods, along with behavioral models combined with gene disruption techniques. This review summarizes the evidence supporting the role of TRP channels (TRP Vanilloid 1, TRP Vanilloid 2, TRP Vanilloid 3, TRP Vanilloid 4, TRP Ankyrin 1, TRP Melastatin 2, TRP Melastatin 3, TRP Melastatin 8, TRP Mucolipin 3 and TRP Canonical 1, 6) involved in nociception. The review also highlights the current status and future avenues for developing TRP channel modulators as analgesic agents.

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40

Wheeler, Simon, Ralf Schmid, and Dan J. Sillence. "Lipid–Protein Interactions in Niemann–Pick Type C Disease: Insights from Molecular Modeling." International Journal of Molecular Sciences 20, no. 3 (February 7, 2019): 717. http://dx.doi.org/10.3390/ijms20030717.

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The accumulation of lipids in the late endosomes and lysosomes of Niemann–Pick type C disease (NPCD) cells is a consequence of the dysfunction of one protein (usually NPC1) but induces dysfunction in many proteins. We used molecular docking to propose (a) that NPC1 exports not just cholesterol, but also sphingosine, (b) that the cholesterol sensitivity of big potassium channel (BK) can be traced to a previously unappreciated site on the channel’s voltage sensor, (c) that transient receptor potential mucolipin 1 (TRPML1) inhibition by sphingomyelin is likely an indirect effect, and (d) that phosphoinositides are responsible for both the mislocalization of annexin A2 (AnxA2) and a soluble NSF (N-ethylmaleimide Sensitive Fusion) protein attachment receptor (SNARE) recycling defect. These results are set in the context of existing knowledge of NPCD to sketch an account of the endolysosomal pathology key to this disease.

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41

Vergarajauregui, S., J. A. Martina, and R. Puertollano. "LAPTMs regulate lysosomal function and interact with mucolipin 1: new clues for understanding mucolipidosis type IV." Journal of Cell Science 124, no. 3 (January 11, 2011): 459–68. http://dx.doi.org/10.1242/jcs.076240.

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42

Yamaguchi, Soichiro, Archana Jha, Qin Li, Abigail A. Soyombo, George D. Dickinson, Dev Churamani, Eugen Brailoiu, Sandip Patel, and Shmuel Muallem. "Transient Receptor Potential Mucolipin 1 (TRPML1) and Two-pore Channels Are Functionally Independent Organellar Ion Channels." Journal of Biological Chemistry 286, no. 26 (May 3, 2011): 22934–42. http://dx.doi.org/10.1074/jbc.m110.210930.

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Takumida, Masaya, and Matti Anniko. "Expression of transient receptor potential channel mucolipin (TRPML) and polycystine (TRPP) in the mouse inner ear." Acta Oto-Laryngologica 130, no. 2 (January 18, 2010): 196–203. http://dx.doi.org/10.3109/00016480903013593.

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Vassort, Guy, and Julio Alvarez. "Transient receptor potential: a large family of new channels of which several are involved in cardiac arrhythmiaThis article is one of a selection of papers from the NATO Advanced Research Workshop on Translational Knowledge for Heart Health (published in part 1 of a 2-part Special Issue)." Canadian Journal of Physiology and Pharmacology 87, no. 2 (February 2009): 100–107. http://dx.doi.org/10.1139/y08-112.

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Abstract:

The transient receptor potential (TRP) family of ion channels comprises more than 50 cation-permeable channels expressed throughout the animal kingdom. TRPs can be grouped into 7 main subfamilies according to structural homology: the TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPP (polycystin), TRPML (mucolipin), TRPA (ankyrin), and TRPN (NO mechanopotential). During the past 20 years, the cloning and characterization after reexpression of most members of these cation channels have led to a plethora of data and more recently to some understanding of their roles in various cells and tissues. Specifically in the heart, TRPs are known to be involved in various diseases, including hypertrophy, heart failure, and arrhythmia. The later part of this review focuses on the potential contribution of TRPs to cardiac rhythm and their potential proarrhythmic effects. Furthermore, several neurotransmitters that activate the formation of diacylglycerol could modulate cardiac rhythm or, like ATP, induce arrhythmia.

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Yu, Lu, Xiaoli Zhang, Yexin Yang, Dan Li, Kaiyuan Tang, Zifan Zhao, Wanwan He, et al. "Small-molecule activation of lysosomal TRP channels ameliorates Duchenne muscular dystrophy in mouse models." Science Advances 6, no. 6 (February 2020): eaaz2736. http://dx.doi.org/10.1126/sciadv.aaz2736.

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Abstract:

Duchenne muscular dystrophy (DMD) is a devastating disease caused by mutations in dystrophin that compromise sarcolemma integrity. Currently, there is no treatment for DMD. Mutations in transient receptor potential mucolipin 1 (ML1), a lysosomal Ca2+ channel required for lysosomal exocytosis, produce a DMD-like phenotype. Here, we show that transgenic overexpression or pharmacological activation of ML1 in vivo facilitates sarcolemma repair and alleviates the dystrophic phenotypes in both skeletal and cardiac muscles of mdx mice (a mouse model of DMD). Hallmark dystrophic features of DMD, including myofiber necrosis, central nucleation, fibrosis, elevated serum creatine kinase levels, reduced muscle force, impaired motor ability, and dilated cardiomyopathies, were all ameliorated by increasing ML1 activity. ML1-dependent activation of transcription factor EB (TFEB) corrects lysosomal insufficiency to diminish muscle damage. Hence, targeting lysosomal Ca2+ channels may represent a promising approach to treat DMD and related muscle diseases.

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Jezela-Stanek, Aleksandra, Elżbieta Ciara, and Karolina M. Stepien. "Neuropathophysiology, Genetic Profile, and Clinical Manifestation of Mucolipidosis IV—A Review and Case Series." International Journal of Molecular Sciences 21, no. 12 (June 26, 2020): 4564. http://dx.doi.org/10.3390/ijms21124564.

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Mucolipidosis type IV (MLIV) is an ultra-rare lysosomal storage disorder caused by biallelic mutations in MCOLN1 gene encoding the transient receptor potential channel mucolipin-1. So far, 35 pathogenic or likely pathogenic MLIV-related variants have been described. Clinical manifestations include severe intellectual disability, speech deficit, progressive visual impairment leading to blindness, and myopathy. The severity of the condition may vary, including less severe psychomotor delay and/or ocular findings. As no striking recognizable facial dysmorphism, skeletal anomalies, organomegaly, or lysosomal enzyme abnormalities in serum are common features of MLIV, the clinical diagnosis may be significantly improved because of characteristic ophthalmological anomalies. This review aims to outline the pathophysiology and genetic defects of this condition with a focus on the genotype–phenotype correlation amongst cases published in the literature. The authors will present their own clinical observations and long-term outcomes in adult MLIV cases.

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Morelli, Maria Beatrice, Massimo Nabissi, Consuelo Amantini, Daniele Tomassoni, Francesco Rossi, Claudio Cardinali, Matteo Santoni, et al. "Overexpression of transient receptor potential mucolipin-2 ion channels in gliomas: role in tumor growth and progression." Oncotarget 7, no. 28 (May 27, 2016): 43654–68. http://dx.doi.org/10.18632/oncotarget.9661.

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Vergarajauregui, Silvia, Jose A. Martina, and Rosa Puertollano. "Identification of the Penta-EF-hand Protein ALG-2 as a Ca2+-dependent Interactor of Mucolipin-1." Journal of Biological Chemistry 284, no. 52 (October 28, 2009): 36357–66. http://dx.doi.org/10.1074/jbc.m109.047241.

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Remis, Natalie N., Teerawat Wiwatpanit, Andrew J. Castiglioni, Emma N. Flores, Jorge A. Cantú, and Jaime García-Añoveros. "Mucolipin Co-deficiency Causes Accelerated Endolysosomal Vacuolation of Enterocytes and Failure-to-Thrive from Birth to Weaning." PLoS Genetics 10, no. 12 (December 18, 2014): e1004833. http://dx.doi.org/10.1371/journal.pgen.1004833.

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Wang, Xiang, Xianping Dong, Dongbiao Shen, Taylor Dawson, Xinran Li, Qi Zhang, Xiping Cheng, et al. "PI(3,5)P2 Controls Membrane Trafficking by Direct Activation of Mucolipin Ca2+ Release Channels in the Endolysosome." Biophysical Journal 100, no. 3 (February 2011): 109a. http://dx.doi.org/10.1016/j.bpj.2010.12.804.

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