OpenSSL SSL_connect: Connection reset by peer in connection to v2.sherpa.ac.uk:443 PuSH - Publication Server of Helmholtz Zentrum München: Hop/Sti1 phosphorylation inhibits its co-chaperone function.

PuSH - Publication Server of Helmholtz Zentrum München

Röhl, A.* ; Tippel, F.* ; Bender, E.* ; Schmid, A.B.* ; Richter, K.* ; Madl, T. ; Buchner, J.*

Hop/Sti1 phosphorylation inhibits its co-chaperone function.

EMBO Rep. 16, 240-249 (2014)
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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
Corresponding Author
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
ISSN (print) / ISBN 1469-221X
e-ISSN 1469-3178
Journal EMBO Reports
Quellenangaben Volume: 16, Issue: 2, Pages: 240-249 Article Number: , Supplement: ,
Publisher EMBO Press
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)