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VCPIP1 deubiquitinates SPRTN. 21 / 21
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"VCPIP1, in turn, deubiquitinates SPRTN and promotes its chromatin relocalization."
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"Deubiquitination of SPRTN by VCPIP1 is important for DPC repair."
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"We hypothesized that VCPIP1 deubiquitinates SPRTN and promotes SPRTN-mediated DPC repair."
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"We found that VCPIP1-WT, but not VCPIP1-CA, restored SPRTN deubiquitination upon DPC induction (Figure 2C)."
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"We found that recombinant VCPIP1-WT, but not VCPIP1-CA, deubiquitinated SPRTN in vitro (Figure 2D)."
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"A previous study showed that VCPIP1 deubiquitinates SPRTN, promoting SPRTN localization to chromatin."
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"These results suggest that VCPIP1 deubiquitinates SPRTN both in vitro and in cells."
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"Neither VCPIP1 nor USP11 induce SPRTN deubiquitylation when overexpressed, while USP7 does (XREF_SUPPLEMENTARY)."
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"Of note, while this study was under consideration, it was proposed that SPRTN is deubiquitylated by VCPIP1."
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"VCIP135 was reported to function as a deubiquitinating enzyme without the assistance of p97; that is, in the activation of SPRTN, a specialized DNA-dependent metalloprotease, VCIP135 deubiquitinated SPRTN in the absence of p97 (12)."
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"Upon DPC induction, ATM and ATR kinase activates VCPIP1 and VCIP135 deubiquitinase, which in turn deubiquitinates SPRTN, regulating its chromatin localization."
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"These observations show that depletion of USP11 and VCPIP1 inhibits SPRTN deubiquitination, but in contrast to previous reports, monoubiquitination does not restrict SPRTN access to chromatin."
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"Previously, <span class="match term0">VCPIP1</span> and USP7 deubiquitinases have been shown to regulate <span class="match term1">SPRTN</span>"
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"Taken together, our data indicate that VCPIP1 regulates SPRTN via its Ub protease activity and deubiquitination of SPRTN by VCPIP1 is important for its chromatin retention in response to DPC lesions."
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"Our results so far suggest that VCPIP1 deubiquitinates SPRTN, thereby triggering association of SPRTN with chromatin following DPC damage."
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"The DUB VCPIP1/VCIP135 also deubiquitinates SPRTN after being phosphorylated and activated by ATM/ATR."
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"We observed reduced SPRTN auto-cleavage upon DPC induction in USP11 and USP7 single and double-knockdown cells, suggesting that in the absence of USP11 and USP7, SPRTN could be deubiquitinated by VCPIP1, which is recruited to chromatin upon DPC induction."
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"Huang et al. showed that in addition to SPRTN deubiquitination, VCPIP1 promoted SPRTN interaction with the acetyltransferases PCAF/GCN5."
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"However, we observe that lack of SPRTN deubiquitination by USP11 and VCPIP1 did not affect recruitment on chromatin."
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"Upon formaldehyde treatment and other yet to be identified signals, SPRTN is deubiquitinated by USP11 (this study), USP7, and VCPIP1."
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"We found that knockdown of VCPIP1 decreased acetylation of SPRTN upon DPC induction (Figure 4I), suggesting that SPRTN acetylation requires SPRTN deubiquitination."
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