Počet záznamů: 1
A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins
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SYSNO ASEP 0506443 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název A 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. 1269-1285Poč.str. 17 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova heat-shock proteins ; saccharomyces-cerevisiae ; molecular chaperones Vědní obor RIV EE - Mikrobiologie, virologie Obor OECD Microbiology Způsob publikování Open access Institucionální podpora MBU-M - RVO:61388971 UT WOS 000428997800013 EID SCOPUS 85044752009 DOI 10.1083/jcb.201708116 Anotace Chaperones 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. Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2020 Elektronická adresa https://rupress.org/jcb/article/217/4/1269/39199/A-prionlike-domain-in-Hsp42-drives
Počet záznamů: 1