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CDK1 phosphorylates VCPIP1. 19 / 19
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"During mitosis, Cdk1 phosphorylates p47, p37 and VCIP135, and blocks p97 controlled membrane-fusion processes so that the Golgi membranes remain disassembled."
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"VCIP135 phosphorylated by Cdc2 generated almost the same amount of mono ubiquitin after the reaction as non phosphorylated VCIP135."
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"VCIP135 phosphorylated by Cdc2 generated almost the same amount of mono ubiquitin after the reaction as non-phosphorylated VCIP135 ( Fig. 3 C, top panel, lane 2)."
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"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)."
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"All these results indicate that phosphorylation of Threonine 760 and Serine 767 in VCIP135 inhibits its binding to p97.We next tested the binding of phosphorylated VCIP135 to WAC, as presented in Fig.[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"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) ."
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"To confirm this, we investigated whether the purified Cdc2 complex phosphorylated VCIP135 in the absence of mitotic cytosol."
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"These results suggest that VCIP135 is phosphorylated on S130 by the mitotic kinase Cdk1."
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"To confirm this, we investigated whether the purified Cdc2 complex phosphorylated VCIP135 in the absence of mitotic cytosol."
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"As shown in Fig. 1 C, Cdc2 indeed phosphorylated VCIP135 (right lane)."
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"To determine whether Cdk1 directly phosphorylates VCIP135 on S130, we performed an in vitro phosphorylation assay with streptavidin-binding peptide (SBP)-tagged VCIP135 recombinant proteins."
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"We next tested the binding of phosphorylated VCIP135 to WAC, as presented in Fig. 3 A. Cdc2-phosphorylated VCIP135 still bound to GST-WAC (upper panel, lane 2), suggesting that the phosphorylation of[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Cdk1 phosphorylates VCIP135 at S130."
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"As shown in Fig. 1 C, Cdc2 indeed phosphorylated VCIP135 (right lane)."
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"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 )."
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"We show that, in early mitosis, phosphorylation of VCIP135 by Cdk1 at a single residue, S130, is sufficient to inactivate the enzyme and inhibit p97/p47-mediated Golgi membrane fusion."
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"Therefore Cdk1 directly phosphorylates VCIP135 on S130 in mitosis."
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"Phosphorylation of VCIP135 on S130 by the mitotic kinase Cdk1 in early mitosis abolishes its deubiquitinase activity and attenuates p97/p47-mediated Golgi membrane fusion."
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"During mitosis, Cdk1 phosphorylates p47, p37 and VCIP135, and blocks p97-controlled membrane-fusion processes so that the Golgi membranes remain disassembled (Uchiyama et al., xref ; Kaneko et al., xref ; Totsukawa et al., xref )."
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