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Verfasst von:Ruger-Herreros, Carmen [VerfasserIn]   i
 Svoboda, Lucia [VerfasserIn]   i
 Mogk, Axel [VerfasserIn]   i
 Bukau, Bernd [VerfasserIn]   i
Titel:Role of j-domain proteins in yeast physiology and protein quality control
Verf.angabe:Carmen Ruger-Herreros, Lucia Svoboda, Axel Mogk and Bernd Bukau
E-Jahr:2024
Jahr:15 July 2024
Umfang:15 S.
Illustrationen:Illustrationen
Fussnoten:Online verfügbar 7 February 2024, Version des Artikels 25 June 2024 ; Gesehen am 03.02.2025
Titel Quelle:Enthalten in: Journal of molecular biology
Ort Quelle:Amsterdam [u.a.] : Elsevier, 1959
Jahr Quelle:2024
Band/Heft Quelle:436(2024), 14 vom: Juli, Artikel-ID 168484, Seite 1-15
ISSN Quelle:1089-8638
Abstract:The Hsp70 chaperone system is a central component of cellular protein quality control (PQC) by acting in a multitude of protein folding processes ranging from the folding of newly synthesized proteins to the disassembly and refolding of protein aggregates. This multifunctionality of Hsp70 is governed by J-domain proteins (JDPs), which act as indispensable co-chaperones that target specific substrates to Hsp70. The number of distinct JDPs present in a species always outnumbers Hsp70, documenting JDP function in functional diversification of Hsp70. In this review, we describe the physiological roles of JDPs in the Saccharomyces cerevisiae PQC system, with a focus on the abundant JDP generalists, Zuo1, Ydj1 and Sis1, which function in fundamental cellular processes. Ribosome-bound Zuo1 cooperates with the Hsp70 chaperones Ssb1/2 in folding and assembly of nascent polypeptides. Ydj1 and Sis1 cooperate with the Hsp70 members Ssa1 to Ssa4 to exert overlapping functions in protein folding and targeting of newly synthesized proteins to organelles including mitochondria and facilitating the degradation of aberrant proteins by E3 ligases. Furthermore, they act in protein disaggregation reactions, though Ydj1 and Sis1 differ in their modes of Hsp70 cooperation and substrate specificities. This results in functional specialization as seen in prion propagation and the underlying dominant role of Sis1 in targeting Hsp70 for shearing of prion amyloid fibrils.
DOI:doi:10.1016/j.jmb.2024.168484
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

kostenfrei: Volltext: https://doi.org/10.1016/j.jmb.2024.168484
 kostenfrei: Volltext: https://www.sciencedirect.com/science/article/pii/S0022283624000561
 DOI: https://doi.org/10.1016/j.jmb.2024.168484
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Chaperone
 Hsp70
 prion
 protein degradation
 protein disaggregation
 protein folding
K10plus-PPN:1916156010
Verknüpfungen:→ Zeitschrift

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