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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)
Verlagsversion DOI PMC
Free by publisher
Creative Commons Lizenzvertrag
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter 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
Zeitschrift EMBO Reports
Quellenangaben Band: 16, Heft: 2, Seiten: 240-249 Artikelnummer: , Supplement: ,
Verlag EMBO Press
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)