IndraLab

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USP28 deubiquitinates CLSPN. 7 / 8
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"USP28 also modulates the DNA damage response (DDR) in cancer cells by deubiquitinating and stabilising the checkpoint kinase 2 (CHK2), the TP53-binding protein 1 (TP53BP1) and Claspin (CLSPN) [6, 7], thereby preventing apoptosis but establishing cell cycle arrest to facilitate DNA repair [8]."
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"De-ubiquitinase USP28 inhibits ubiquitination of Claspin protein and its proteasomal degradation [XREF_BIBR]."
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"Thus, USP28 deubiquitinates Claspin to enable the activation of a CHK1-dependent G -checkpoint , and protects checkpoint-mediators to facilitate apoptosis ."
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"Claspin is a bona fide USP28 substrate, as Claspin deubiquitination by USP28 could also be reconstituted in vitro."
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"However, it must be noted that USP28 can also deubiquitinate and stabilise other substrates not known to be associated with Fbw7, including Claspin [92] , Chk2 [93] , and LSD1 [94] , which could also [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In addition, Claspin, which was discovered as a protein required for the activation of checkpoint kinase 1 (Chk1), can be deubiquitinated by USP28 through reversing the effect of ubiquitin ligase APC/C [67, 68]."
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"Thus, deubiquitination of Claspin caused by USP28 contributes to cell cycle arrest, which maintains ovarian clear cell carcinoma cell viability in response to a genotoxic stress [68]."
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