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

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    SYSNO ASEP0543461
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleMaintenance of organellar protein homeostasis by ER-associated degradation and related mechanisms
    Author(s) Lemberg, M. K. (DE)
    Stříšovský, Kvido (UOCHB-X) RID, ORCID
    Source TitleMolecular Cell. - : Elsevier - ISSN 1097-2765
    Roč. 81, č. 12 (2021), s. 2507-2519
    Number of pages13 s.
    Languageeng - English
    CountryUS - United States
    Keywordsreticulum-associated degradation ; signal peptide peptidase ; class I molecules
    OECD categoryBiochemistry and molecular biology
    R&D ProjectsGA18-09556S GA ČR - Czech Science Foundation (CSF)
    GA20-25331S GA ČR - Czech Science Foundation (CSF)
    EF16_019/0000729 GA MŠk - Ministry of Education, Youth and Sports (MEYS)
    Method of publishingLimited access
    Institutional supportUOCHB-X - RVO:61388963
    UT WOS000674490700005
    EID SCOPUS85107984069
    DOI10.1016/j.molcel.2021.05.004
    AnnotationProtein 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.
    WorkplaceInstitute of Organic Chemistry and Biochemistry
    ContactMarie Odehnalová,marie.odehnalova@uochb.cas.cz Tel.: 220 183 418 ; Viktorie Chládková, viktorie.chladkova@uochb.cas.cz, Tel.: 232 002 434
    Year of Publishing2022
    Electronic addresshttps://doi.org/10.1016/j.molcel.2021.05.004
Number of the records: 1