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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

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

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

  • Volume of the periodical

  • Issue of the periodical within the volume

    June 2012

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    10

  • Pages from-to

  • UT code for WoS article

  • EID of the result in the Scopus database