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USP11 deubiquitinates CDKN1A. 8 / 8
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"Deubiquitylation and stabilization of p21 by USP11 is critical for cell-cycle progression and DNA damage responses."
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"In the nucleus, <span class="match term0">USP11</span> binds to <span class="match term1">p21</span>, catalyzes the removal of polyubiquitin chains conjugated onto <span class="match term1">p21</span>, and stabilizes <span class="match term1">p21</span> protein"
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"Recent studies have revealed that USP11 deubiquitinates and stabilizes p21 protein under physiological conditions, as well as in response to DNA damage [17]."
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"We further presumed that RanBPM might promote the interaction between USP11 and p21, and regulate USP11-dependent deubiquitination of p21."
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"Notably, USP11 plays a key role in DNA damage repair depending on its catalytic activity, for example, Xia Ting et al. [20] found that USP11 acts as a histone deubiquitinase in chromatin reorganization during DNA repair, Palak Shah et al. [21] found that USP11 regulates UV-induced DNA damage repair by deubiquitinating XPC, and Tanggang Deng et al. [32] identified that the deubiquitylation and stabilization of p21 by USP11 is essential for cell cycle progression and DNA damage responses."
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"USP11 may stimulate tumorigenesis by deubiquitinating cIAP2, NONO, NF90, E2F1, or cytoplasmic p21; however, it may also inhibit tumorigenesis through stabilizing PML, Mgl-1, PTEN, ARID1A, or nuclear p21 (29, 30)."
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"For instance, USP11 can reverse the ubiquitination and degradation of p21, a cyclin-dependent kinase inhibitor, and hence mediate the DNA damage response and apoptosis."
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"As a result, USP11 reverses p21 polyubiquitylation and degradation mediated by SCF SKP2, CRL4 CDT2, and APC/C CDC20 in a cell-cycle-independent manner."
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