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Docking dependent ubiquitination of the interferon regulatory factor-1 tumour suppressor protein by the ubiquitin ligase CHIP

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00209805%3A_____%2F11%3A%230000144" target="_blank" >RIV/00209805:_____/11:#0000144 - isvavai.cz</a>

  • Result on the web

    <a href="http://www.jbc.org/content/286/1/607.long" target="_blank" >http://www.jbc.org/content/286/1/607.long</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1074/jbc.M110.153122" target="_blank" >10.1074/jbc.M110.153122</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Docking dependent ubiquitination of the interferon regulatory factor-1 tumour suppressor protein by the ubiquitin ligase CHIP

  • Original language description

    The IRF-1 tumor suppressor turns over rapidly with a half-life of between 20?40 min. This allows IRF-1 to reach new steady state protein levels swiftly in response to changing environmental conditions. Whereas CHIP (C terminus of Hsc70-interacting protein), appears to chaperone IRF-1 in unstressed cells, formation of a stable IRF-1CHIP complex is seen under specific stress conditions. Complex formation, in heat- or heavy metaltreated cells, is accompanied by a decrease in IRF-1 steady state levels and an increase in IRF-1 ubiquitination. CHIP binds directly to an intrinsically disordered domain in the central region of IRF-1, and this site is sufficient to form a stable complex with CHIP in cells and to compete in trans with full-length IRF-1, leadingto a reduction in its ubiquitination. The study reveals a complex relationship between CHIP and IRF-1 and highlights the role that direct binding or ?docking? of CHIP to its substrate(s) can play in its mechanism of action as an E3 ligase

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    EB - Genetics and molecular biology

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2011

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    The Journal of biological chemistry

  • ISSN

    0021-9258

  • e-ISSN

  • Volume of the periodical

    286

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    13

  • Pages from-to

    607-619

  • UT code for WoS article

    000285782800063

  • EID of the result in the Scopus database