Počet záznamů: 1  

A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins

  1. 1.
    SYSNO ASEP0506443
    Druh ASEPJ - Článek v odborném periodiku
    Zařazení RIVJ - Článek v odborném periodiku
    Poddruh JČlánek ve WOS
    NázevA prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins
    Tvůrce(i) Groušl, Tomáš (MBU-M) RID, ORCID
    Ungelenk, S. (DE)
    Miller, S. (DE)
    Ho, CT. (DE)
    Khokhrina, M. (DE)
    Mayer, M.P. (DE)
    Bukau, B. (DE)
    Mogk, A. (DE)
    Zdroj.dok.Journal of Cell Biology. - : Rockefeller University Press - ISSN 0021-9525
    Roč. 217, č. 4 (2018), s. 1269-1285
    Poč.str.17 s.
    Jazyk dok.eng - angličtina
    Země vyd.US - Spojené státy americké
    Klíč. slovaheat-shock proteins ; saccharomyces-cerevisiae ; molecular chaperones
    Vědní obor RIVEE - Mikrobiologie, virologie
    Obor OECDMicrobiology
    Způsob publikováníOpen access
    Institucionální podporaMBU-M - RVO:61388971
    UT WOS000428997800013
    EID SCOPUS85044752009
    DOI10.1083/jcb.201708116
    AnotaceChaperones with aggregase activity promote and organize the aggregation of misfolded proteins and their deposition at specific intracellular sites. This activity represents a novel cytoprotective strategy of protein quality control systems, however, little is known about its mechanism. In yeast, the small heat shock protein Hsp42 orchestrates the stress-induced sequestration of misfolded proteins into cytosolic aggregates (CytoQ). In this study, we show that Hsp42 harbors a prion-like domain (PrLD) and a canonical intrinsically disordered domain (IDD) that act coordinately to promote and control protein aggregation. Hsp42 PrLD is essential for CytoQ formation and is bifunctional, mediating self-association as well as binding to misfolded proteins. Hsp42 IDD confines chaperone and aggregase activity and affects CytoQ numbers and stability in vivo. Hsp42 PrLD and IDD are both crucial for cellular fitness during heat stress, demonstrating the need for sequestering misfolded proteins in a regulated manner.
    PracovištěMikrobiologický ústav
    KontaktEliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
    Rok sběru2020
    Elektronická adresahttps://rupress.org/jcb/article/217/4/1269/39199/A-prionlike-domain-in-Hsp42-drives
Počet záznamů: 1  

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