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Maintenance of organellar protein homeostasis by ER-associated degradation and related mechanisms

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, ORCID}
Source Title	Molecular Cell. - : Cell Press - ISSN 1097-2765 Roč. 81, č. 12 (2021), s. 2507-2519
Number 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	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 ; Viktorie Chládková, Tel.: 232 002 434
Year of Publishing	2022
Electronic address	https://doi.org/10.1016/j.molcel.2021.05.004

Number of the records: 1