IndraLab

Statements


VCPIP1 affects SPRTN
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VCPIP1 deubiquitinates SPRTN. 10 / 17
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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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"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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"VCPIP1, in turn, deubiquitinates SPRTN and promotes its chromatin relocalization."

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"These results suggest that VCPIP1 deubiquitinates SPRTN both in vitro and in cells."

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"We hypothesized that VCPIP1 deubiquitinates SPRTN and promotes SPRTN-mediated DPC repair."

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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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"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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"We found that recombinant VCPIP1-WT, but not VCPIP1-CA, deubiquitinated SPRTN in vitro (Figure 2D)."

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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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"Of note, while this study was under consideration, it was proposed that SPRTN is deubiquitylated by VCPIP1."
VCPIP1 affects SNTG2
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VCPIP1 deubiquitinates SNTG2. 9 / 9
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"One possible explanation, as described in our model (XREF_FIG), is that monoubiquitination of Syn5 occurs only transiently in early mitosis and is quickly reversed by the deubiquitinase VCIP135 in late mitosis."

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"In late mitosis, the DUB VCIP135, which associates with p97 via its UBX-L (UBX like) domain, deubiquitinates Syn5, which permits interaction between the SNAREs, membrane fusion and finally the formation of Golgi cisternae [XREF_BIBR]."

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"Therefore, we determined whether Syn5 is deubiquitinated by VCIP135."

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"Taken together, these results demonstrate that Syn5 is deubiquitinated by VCIP135 in late mitosis.Syn5 contains 17 lysines that are conserved between rat and human."

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"One possible explanation, as described in our model, is that monoubiquitination of Syn5 occurs only transiently in early mitosis and is quickly reversed by the deubiquitinase VCIP135 in late mitosis."

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"Syn5 is monoubiquitinated by the ubiquitin ligase HACE1 in early mitosis and deubiquitinated by the deubiquitinase VCIP135 in late mitosis."

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"These results suggest that Syn5 is deubiquitinated by VCIP135."

"Syn5 is monoubiquitinated by the ubiquitin ligase HACE1 in early mitosis and deubiquitinated by the deubiquitinase VCIP135 in late mitosis."

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"Taken together, these results demonstrate that Syn5 is deubiquitinated by VCIP135 in late mitosis."
VCPIP1 affects STX5
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VCPIP1 deubiquitinates STX5. 2 / 2
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"Syntaxin 5 is monoubiquitinated by HACE1 in early mitosis and deubiquitinated by the de-ubiquitinase VCIP135 in late mitosis (Wang et al. 2004)."

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"Syntaxin 5 is monoubiquitinated by HACE1 in early mitosis and deubiquitinated by the de-ubiquitinase VCIP135 in late mitosis."
VCPIP1 affects p97-p47
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VCPIP1 deubiquitinates p97-p47. 1 / 1
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"The intimate interaction of the three factors, however, suggests a mechanism that is dependent on the recognition and processing of a ubiquitin conjugate by p97-p47 and subsequent deubiquitination by VCIP135."