IndraLab

Statements


VCPIP1 is dephosphorylated. 7 / 7
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sparser
"During late mitosis, VCIP135 becomes dephosphorylated and associates with the p97–p47–Syn5 complex."

sparser
"In mitosis, VCIP135 is phosphorylated at S130 by Cdk1 and thus is inactivated, allowing syntaxin 5 to be ubiquitinated by HACE1; in telophase, VCIP135 is dephosphorylated and reactivated, removing ubiquitin from syntaxin 5 to allow p97-mediated membrane fusion ( xref ; xref )."

sparser
"In mitosis, VCIP135 is phosphorylated at S130 by Cdk1 and thus is inactivated, allowing syntaxin 5 to be ubiquitinated by HACE1; in telophase, VCIP135 is dephosphorylated and reactivated, removing ubiquitin from syntaxin 5 to allow p97-mediated membrane fusion (Huang and Wang 2017; Wang 2008)."

sparser
"Dephosphorylation of VCIP135 at S130 in telophase activates its deubiquitinase activity for Golgi reassembly."

sparser
"In mitosis, VCIP135 is phosphorylated at S130 by Cdk1 and thus is inactivated, allowing syntaxin 5 to be ubiquitinated by HACE1; in telophase, VCIP135 is dephosphorylated and reactivated, removing ubiquitin from syntaxin 5 to allow p97-mediated membrane fusion Wang 2008) ."

sparser
"Conversely, at the end of mitosis, VCIP135 is dephosphorylated (on Ser130), and this is associated with recovery of its deubiquitinase activity and with post-mitotic Golgi reassembly (Zhang and Wang, xref )."

sparser
"Dephosphorylation of S130 on VCIP135 upon staurosporine or roscovitine but not U0126 treatment also significantly increased the DUB activity of endogenous VCIP135 ( xref ), consistent with the hypothesis that phosphorylation at S130 inactivates VCIP135."