C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F12%3A00390477" target="_blank" >RIV/61388971:_____/12:00390477 - isvavai.cz</a>
Alternative codes found
RIV/00209805:_____/13:#0000417
Result on the web
<a href="http://www.readcube.com/articles/10.1038/onc.2012.314" target="_blank" >http://www.readcube.com/articles/10.1038/onc.2012.314</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/onc.2012.314" target="_blank" >10.1038/onc.2012.314</a>
Alternative languages
Result language
angličtina
Original language name
C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances
Original language description
Heat shock proteins Hsp90 and Hsp70 facilitate protein folding but can also direct proteins for ubiquitin-mediated degradation. The mechanisms regulating these opposite activities involve Hsp binding to co-chaperones including CHIP and HOP at their C-termini. We demonstrated that the extreme C-termini of Hsp70 and Hsp90 contain phosphorylation sites targeted by kinases including CK1, CK2 and GSK3-b in vitro. The phosphorylation of Hsp90 and Hsp70 prevents binding to CHIP and thus enhances binding to HOP. Highly proliferative cells contain phosphorylated chaperones in complex with HOP and phospho-mimetic and non-phosphorylable Hsp mutant proteins show that phosphorylation is directly associated with increased proliferation rate. We also demonstrate thatprimary human cancers contain high levels of phosphorylated chaperones and show increased levels of HOP protein and mRNA
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Oncogene
ISSN
0950-9232
e-ISSN
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Volume of the periodical
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Issue of the periodical within the volume
June 2012
Country of publishing house
GB - UNITED KINGDOM
Number of pages
10
Pages from-to
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UT code for WoS article
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EID of the result in the Scopus database
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