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Hop/Sti1 phosphorylation inhibits its co-chaperone function.
EMBO Rep. 16, 240-249 (2014)
In eukaryotes, the molecular chaperones Hsp90 and Hsp70 are connected via the co-chaperone Sti1/Hop, which allows transfer of clients. Here, we show that the basic functions of yeast Sti1 and human Hop are conserved. These include the simultaneous binding of Hsp90 and Hsp70, the inhibition of the ATPase activity of Hsp90, and the ability to support client activation in vivo. Importantly, we reveal that both Hop and Sti1 are subject to inhibitory phosphorylation, although the sites modified and the influence of regulatory phosphorylation is species specific. Phospho-mimetic variants have a reduced ability to activate clients in vivo and different affinity for Hsp70. Hop is more tightly regulated, as phosphorylation affects also the interaction with Hsp90 and induces structural rearrangements in the core part of the protein.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Saxs ; Sti1/hop ; Co‐chaperone ; Phosphorylation ; Regulation; Cancer-cell-lines; Heat-shock; Molecular-mechanism; Atpase Cycle; Hsp90 Atpase; Tyrosine Phosphorylation; Saccharomyces-cerevisiae; Nuclear Translocation; Protein Msti1; In-vivo
Language
english
Publication Year
2014
HGF-reported in Year
2015
ISSN (print) / ISBN
1469-221X
e-ISSN
1469-3178
Journal
EMBO Reports
Quellenangaben
Volume: 16,
Issue: 2,
Pages: 240-249
Publisher
EMBO Press
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)
POF-Topic(s)
30505 - New Technologies for Biomedical Discoveries
Research field(s)
Enabling and Novel Technologies
PSP Element(s)
G-552800-001
PubMed ID
25504578
Scopus ID
84922254182
Scopus ID
84920383669
WOS ID
WOS:000350695600015
Erfassungsdatum
2015-01-05