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Matches in SemOpenAlex for { <https://semopenalex.org/work/W1970267023> ?p ?o ?g. }

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• W1970267023 startingPage "13074" @default.
• W1970267023 abstract "CLASPIN is an essential mediator in the DNA replication checkpoint, responsible for ATR (ataxia telangiectasia and Rad3-related protein)-dependent activation of CHK1 (checkpoint kinase 1). Here we found a dynamic signaling pathway that regulates CLASPIN turn over. Under unperturbed conditions, the E3 ubiquitin ligase HERC2 regulates the stability of the deubiquitinating enzyme USP20 by promoting ubiquitination-mediated proteasomal degradation. Under replication stress, ATR-mediated phosphorylation of USP20 results in the disassociation of HERC2 from USP20. USP20 in turn deubiquitinates K48-linked-polyubiquitinated CLASPIN, stabilizing CLASPIN and ultimately promoting CHK1 phosphorylation and CHK1-directed checkpoint activation. Inhibition of USP20 expression promotes chromosome instability and xenograft tumor growth. Taken together, our findings demonstrated a novel function of HERC2/USP20 in coordinating CHK1 activation by modulating CLASPIN stability, which ultimately promotes genome stability and suppresses tumor growth." @default.
• W1970267023 created "2016-06-24" @default.
• W1970267023 creator A5001932154 @default.
• W1970267023 creator A5061081892 @default.
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• W1970267023 creator A5076234252 @default.
• W1970267023 date "2014-10-17" @default.
• W1970267023 modified "2023-10-16" @default.
• W1970267023 title "HERC2/USP20 coordinates CHK1 activation by modulating CLASPIN stability" @default.
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• W1970267023 doi "https://doi.org/10.1093/nar/gku978" @default.
• W1970267023 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4245974" @default.
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