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Gewählte Publikation:

SHR Neuro Krebs Kardio Lipid

Röhl, A; Tippel, F; Bender, E; Schmid, AB; Richter, K; Madl, T; Buchner, J.
Hop/Sti1 phosphorylation inhibits its co-chaperone function.
EMBO Rep. 2015; 16(2):240-249 [OPEN ACCESS]
Web of Science PubMed PUBMED Central FullText FullText_MUG


Autor/innen der Med Uni Graz:
Madl Tobias

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Plum Analytics:
Number of Figures: 5
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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. © 2014 The Authors. Published under the terms of the CC BY NC ND 4.0 license.
Find related publications in this database (using NLM MeSH Indexing)
HSP70 Heat-Shock Proteins - metabolism
HSP90 Heat-Shock Proteins - metabolism
Heat-Shock Proteins - chemistry
Heat-Shock Proteins - metabolism
Humans -
Molecular Chaperones - chemistry
Molecular Chaperones - metabolism
Phosphorylation -
Protein Binding -

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