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Selected Publication:
SHR Neuro Cancer Cardio Lipid Metab Microb
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
Doi: 10.15252/embr.201439198
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- Co-authors Med Uni Graz
- Madl Tobias
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- Abstract:
- 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 -
- Find related publications in this database (Keywords)
- co-chaperone
- phosphorylation
- regulation
- SAXS
- Sti1/Hop