NDLI: Co-chaperone Specificity in Gating of the Polypeptide Conducting Channel in the Membrane of the Human Endoplasmic Reticulum

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Co-chaperone Specificity in Gating of the Polypeptide Conducting Channel in the Membrane of the Human Endoplasmic Reticulum

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Co-chaperone Specificity in Gating of the Polypeptide Conducting Channel in the Membrane of the Human Endoplasmic Reticulum

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Lampel, Pavel Urban, Sabine Katharina Hemmis, Birgit Cavalié, Adolfo Bochen, Florian Wagner, Richard Klein, Marie-christine Schäuble, Nico Jung, Martin Dudek, Johanna Hassdenteufel, Sarah Zimmermann, Richard Melnyk, Armin Chen, Xing-zhen Wang, Qian Greiner, Markus Gamayun, Igor Schorr, Stefan
Description	Author Affiliation: Schorr S ( From the Departments of Medical Biochemistry and Molecular Biology and.); Klein MC ( From the Departments of Medical Biochemistry and Molecular Biology and.); Gamayun I ( Experimental and Clinical Pharmacology and Toxicology, Saarland University, 66421 Homburg, Germany.); Melnyk A ( From the Departments of Medical Biochemistry and Molecular Biology and.); Jung M ( From the Departments of Medical Biochemistry and Molecular Biology and.); Schäuble N ( From the Departments of Medical Biochemistry and Molecular Biology and.); Wang Q ( the Department of Physiology, University of Alberta, Edmonton T6G 2H7, Canada, and.); Hemmis B ( the Division of Biophysics, Universität Osnabrück, FB Biologie/Chemie, 49076 Osnabrück, Germany.); Bochen F ( From the Departments of Medical Biochemistry and Molecular Biology and.); Greiner M ( From the Departments of Medical Biochemistry and Molecular Biology and.); Lampel P ( From the Departments of Medical Biochemistry and Molecular Biology and.); Urban SK ( From the Departments of Medical Biochemistry and Molecular Biology and.); Hassdenteufel S ( From the Departments of Medical Biochemistry and Molecular Biology and.); Dudek J ( From the Departments of Medical Biochemistry and Molecular Biology and.); Chen XZ ( the Department of Physiology, University of Alberta, Edmonton T6G 2H7, Canada, and.); Wagner R ( the Division of Biophysics, Universität Osnabrück, FB Biologie/Chemie, 49076 Osnabrück, Germany.); Cavalié A ( Experimental and Clinical Pharmacology and Toxicology, Saarland University, 66421 Homburg, Germany.); Zimmermann R ( From the Departments of Medical Biochemistry and Molecular Biology and richard.zimmermann@uks.eu.)
Abstract	In mammalian cells, signal peptide-dependent protein transport into the endoplasmic reticulum (ER) is mediated by a dynamic polypeptide-conducting channel, the heterotrimeric Sec61 complex. Previous work has characterized the Sec61 complex as a potential ER Ca(2+) leak channel in HeLa cells and identified ER lumenal molecular chaperone immunoglobulin heavy-chain-binding protein (BiP) as limiting Ca(2+) leakage via the open Sec61 channel by facilitating channel closing. This BiP activity involves binding of BiP to the ER lumenal loop 7 of Sec61 in the vicinity of tyrosine 344. Of note, the Y344H mutation destroys the BiP binding site and causes pancreatic ß-cell apoptosis and diabetes in mice. Here, we systematically depleted HeLa cells of the BiP co-chaperones by siRNA-mediated gene silencing and used live cell Ca(2+) imaging to monitor the effects on ER Ca(2+) leakage. Depletion of either one of the ER lumenal BiP co-chaperones, ERj3 and ERj6, but not the ER membrane-resident co-chaperones (such as Sec63 protein, which assists BiP in Sec61 channel opening) led to increased Ca(2+) leakage via Sec6 complex, thereby phenocopying the effect of BiP depletion. Thus, BiP facilitates Sec61 channel closure (i.e. limits ER Ca(2+) leakage) via the Sec61 channel with the help of ERj3 and ERj6. Interestingly, deletion of ERj6 causes pancreatic ß-cell failure and diabetes in mice and humans. We suggest that co-chaperone-controlled gating of the Sec61 channel by BiP is particularly important for cells, which are highly active in protein secretion, and that breakdown of this regulatory mechanism can cause apoptosis and disease.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	30
Volume Number	290
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2015-07-24
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Diabetes Mellitus Genetics Endoplasmic Reticulum Metabolism HSP40 Heat-Shock Proteins Heat-Shock Proteins Membrane Proteins Animals Binding Sites Calcium Calcium Signaling Pathology Gene Silencing HeLa Cells Insulin-Secreting Cells Mice Protein Binding Protein Transport Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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