USP7 counteracts SCF TrCP - but not APC Cdh1 -mediated proteolysis of Claspin

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15110%2F09%3A00010975" target="_blank" >RIV/61989592:15110/09:00010975 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
USP7 counteracts SCF TrCP - but not APC Cdh1 -mediated proteolysis of Claspin
Original language description
Claspin is an adaptor protein that facilitates the ataxia telangiectasia and Rad3-related (ATR)- mediated phosphorylation and activation of Chk1, a key effector kinase in the DNA damage response. Effi cient termination of Chk1 signaling in mitosis and during checkpoint recovery requires SCF TrCP - dependent destruction of Claspin. Here, we identify the deubiquitylating enzyme ubiquitin-specifi c protease 7 (USP7) as a novel reg ulator of Claspin stability. Claspin and USP7 interact in vivo, and USP7 isrequired to maintain steady-state levels of Claspin. Furthermore, USP7-mediated deubiquitylation markedly prolongs the half-life of Claspin, which in turn increases the magnitude and duration of Chk1 phosphorylation in response to genotoxic stress. Finally, we fi nd that in addition to the M phase ? specifi c, SCF TrCP -mediated degradation, Claspin is destabilized by the anaphase-promoting complex (APC) and thus remains unstable in G1. Importantly, we demonstrate that USP7 specifi cally
Czech name
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Czech description
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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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Publication year
2009
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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