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
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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
EB - Genetics and molecular biology
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
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
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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
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