Hsp40/70/110 chaperones adapt nuclear protein quality control to serve cytosolic clients
نویسندگان
چکیده
منابع مشابه
Molecular chaperones in protein quality control.
Proteins must fold into their correct three-dimensional conformation in order to attain their biological function. Conversely, protein aggregation and misfolding are primary contributors to many devastating human diseases, such as prion-mediated infections, Alzheimer's disease, type II diabetes and cystic fibrosis. While the native conformation of a polypeptide is encoded within its primary ami...
متن کاملMolecular chaperones and protein quality control.
In living cells, both newly made and preexisting polypeptide chains are at constant risk for misfolding and aggregation. In accordance with the wide diversity of misfolded forms, elaborate quality-control strategies have evolved to counter these inevitable mishaps. Recent reports describe the removal of aggregates from the cytosol; reveal mechanisms for protein quality control in the endoplasmi...
متن کاملMolecular Chaperones and Protein Quality Control
Bernd Bukau,1 Jonathan Weissman,2 and Arthur Horwich3,4,* 1Zentrum fur Molekulare Biologie, Universität Heidelberg, 69120 Heidelberg, Germany 2Department of Cellular and Molecular Pharmacology and Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94143, USA 3Department of Genetics and Howard Hughes Medical Institute, Yale University School of Medicine, ...
متن کاملProtein Quality Control by Molecular Chaperones in Neurodegeneration
Protein homeostasis (proteostasis) requires the timely degradation of misfolded proteins and their aggregates by protein quality control (PQC), of which molecular chaperones are an essential component. Compared with other cell types, PQC in neurons is particularly challenging because they have a unique cellular structure with long extensions. Making it worse, neurons are postmitotic, i.e., cann...
متن کاملProtein quality control: triage by chaperones and proteases.
Proteases and chaperones together serve to maintain quahty control of cellular proteins. Both types of en zymes have as their substrates the variety of misfolded and partially folded proteins that arise from slow rates of folding or assembly, chemical or thermal stress, intrinsic structural instability, and biosynthetic errors. The pri mary function of classical chaperones, such as the Esch ...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2018
ISSN: 0021-9525,1540-8140
DOI: 10.1083/jcb.201706091