دورية أكاديمية
أعرض في EDS

Yeast derlin Dfm1 employs a chaperone-like function to resolve misfolded membrane protein stress.

التفاصيل البيبلوغرافية
العنوان: Yeast derlin Dfm1 employs a chaperone-like function to resolve misfolded membrane protein stress.
المؤلفون: Kandel R; Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, California, United States of America., Jung J; Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, California, United States of America., Syau D; Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, California, United States of America., Kuo T; Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, California, United States of America., Songster L; Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, California, United States of America., Horn C; Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, California, United States of America., Chapman C; Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, California, United States of America., Aguayo A; Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, California, United States of America., Duttke S; School of Molecular Biosciences, College of Veterinary Medicine, Washington State University, Pullman, Washington, United States of America., Benner C; Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, California, United States of America., Neal SE; Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, California, United States of America.
المصدر: PLoS biology [PLoS Biol] 2023 Jan 23; Vol. 21 (1), pp. e3001950. Date of Electronic Publication: 2023 Jan 23 (Print Publication: 2023).
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
اللغة: English
بيانات الدورية: Publisher: Public Library of Science Country of Publication: United States NLM ID: 101183755 Publication Model: eCollection Cited Medium: Internet ISSN: 1545-7885 (Electronic) Linking ISSN: 15449173 NLM ISO Abbreviation: PLoS Biol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: San Francisco, CA : Public Library of Science, [2003]-
مواضيع طبية MeSH: Membrane Proteins*/metabolism , Protein Folding* , Saccharomyces cerevisiae*/metabolism , Saccharomyces cerevisiae Proteins*/metabolism, Molecular Chaperones/metabolism
مستخلص: Protein aggregates are a common feature of diseased and aged cells. Membrane proteins comprise a quarter of the proteome, and yet, it is not well understood how aggregation of membrane proteins is regulated and what effects these aggregates can have on cellular health. We have determined in yeast that the derlin Dfm1 has a chaperone-like activity that influences misfolded membrane protein aggregation. We establish that this function of Dfm1 does not require recruitment of the ATPase Cdc48 and it is distinct from Dfm1's previously identified function in dislocating misfolded membrane proteins from the endoplasmic reticulum (ER) to the cytosol for degradation. Additionally, we assess the cellular impacts of misfolded membrane proteins in the absence of Dfm1 and determine that misfolded membrane proteins are toxic to cells in the absence of Dfm1 and cause disruptions to proteasomal and ubiquitin homeostasis.
Competing Interests: The authors have declared no competing interests exist.
(Copyright: © 2023 Kandel et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.)
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معلومات مُعتمدة: T32 GM133351 United States GM NIGMS NIH HHS; R35 GM133565 United States GM NIGMS NIH HHS; R25 HL145817 United States HL NHLBI NIH HHS; T32 HL007444 United States HL NHLBI NIH HHS; R00 GM135515 United States GM NIGMS NIH HHS
المشرفين على المادة: 0 (Dfm1 protein, S cerevisiae)
0 (Membrane Proteins)
0 (Molecular Chaperones)
0 (Saccharomyces cerevisiae Proteins)
تواريخ الأحداث: Date Created: 20230123 Date Completed: 20230213 Latest Revision: 20240608
رمز التحديث: 20240608
مُعرف محوري في PubMed: PMC9894555
DOI: 10.1371/journal.pbio.3001950
PMID: 36689475
قاعدة البيانات: MEDLINE
الوصف
تدمد:1545-7885
DOI:10.1371/journal.pbio.3001950