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Maintenance of organellar protein homeostasis by ER-associated degradation and related mechanisms
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SYSNO ASEP 0543461 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Maintenance of organellar protein homeostasis by ER-associated degradation and related mechanisms Author(s) Lemberg, M. K. (DE)
Stříšovský, Kvido (UOCHB-X) RID, ORCIDSource Title Molecular Cell. - : Cell Press - ISSN 1097-2765
Roč. 81, č. 12 (2021), s. 2507-2519Number of pages 13 s. Language eng - English Country US - United States Keywords reticulum-associated degradation ; signal peptide peptidase ; class I molecules OECD category Biochemistry and molecular biology R&D Projects GA18-09556S GA ČR - Czech Science Foundation (CSF) GA20-25331S GA ČR - Czech Science Foundation (CSF) EF16_019/0000729 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Limited access Institutional support UOCHB-X - RVO:61388963 UT WOS 000674490700005 EID SCOPUS 85107984069 DOI https://doi.org/10.1016/j.molcel.2021.05.004 Annotation Protein homeostasis mechanisms are fundamentally important to match cellular needs and to counteract stress conditions. A fundamental challenge is to understand how defective proteins are recognized and extracted from cellular organelles to be degraded in the cytoplasm. The endoplasmic reticulum (ER)-associated degradation (ERAD) pathway is the best-understood organellar protein quality control system. Here, we review new insights into the mechanism of recognition and retrotranslocation of client proteins in ERAD. In addition to the membrane-integral ERAD E3 ubiquitin ligases, we highlight one protein family that is remarkably often involved in various aspects of membrane protein quality control and protein dislocation: the rhomboid superfamily, which includes derlins and intramembrane serine proteases. Rhomboid-like proteins have been found to control protein homeostasis in the ER, but also in other eukaryotic organelles and in bacteria, pointing toward conserved principles of membrane protein quality control across organelles and evolution. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Year of Publishing 2022 Electronic address https://doi.org/10.1016/j.molcel.2021.05.004
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