Docking dependent ubiquitination of the interferon regulatory factor-1 tumour suppressor protein by the ubiquitin ligase CHIP
Identifikátory výsledku
Kód výsledku v 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>
Výsledek na webu
<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>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Docking dependent ubiquitination of the interferon regulatory factor-1 tumour suppressor protein by the ubiquitin ligase CHIP
Popis výsledku v původním jazyce
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
Název v anglickém jazyce
Docking dependent ubiquitination of the interferon regulatory factor-1 tumour suppressor protein by the ubiquitin ligase CHIP
Popis výsledku anglicky
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
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
EB - Genetika a molekulární biologie
OECD FORD obor
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Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2011
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
The Journal of biological chemistry
ISSN
0021-9258
e-ISSN
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Svazek periodika
286
Číslo periodika v rámci svazku
1
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
13
Strana od-do
607-619
Kód UT WoS článku
000285782800063
EID výsledku v databázi Scopus
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