IndraLab

Statements

CDK1 phosphorylates USP16. 12 / 12
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rlimsp
"Because Usp16 is phosphorylated by CDK1 (Cai et al., 1999; Xu et al., 2013), we speculated that CDK1 might serve as a priming kinase regulating Plk1–Usp16 interaction in a way similar to other cases (Liu and Maller, 2005; Zhang et al., 2009)."
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rlimsp
"To investigate this, we first set out to identify CDK1 phosphorylation sites on Usp16."
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sparser
"Cdk1 phosphorylates Usp16 and enhances its binding to Plk1."
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rlimsp
"Cdk1 phosphorylates Usp16 and enhances its binding to Plk1."
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sparser
"Because Usp16 is phosphorylated by CDK1 ( xref ; xref ), we speculated that CDK1 might serve as a priming kinase regulating Plk1–Usp16 interaction in a way similar to other cases ( xref ; xref )."
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reach
"Cdk1 phosphorylates Usp16 and enhances its binding to Plk1."
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reach
"Because Usp16 is phosphorylated by CDK1, we speculated that CDK1 might serve as a priming kinase regulating Plk1-Usp16 interaction in a way similar to other cases."
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rlimsp
"Usp16 is phosphorylated by CDK1 and Plk1."
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reach
"During the cell cycle, Ubp-M is sequentially phosphorylated and dephosphorylated, potentially by the cdc-2/cyclin B complex, which phosphorylates Ubp-M in vitro ( Cai et al., 1999 )."
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rlimsp
"The diagram shows that in early mitosis, cytosolic and possibly kinetochore-localized Usp16 is phosphorylated by CDK1 to generate a binding motif for PBD."
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sparser
"Furthermore, Usp16 promotes chromosome alignment by regulating kinetochore localization of PLK1 through phosphorylation of the Cdk1 site of USP16 [ xref ]."
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sparser
"CDK1 and Plk1 sequentially phosphorylate and activate Usp16, which in turn deubiquitinates Plk1 to maintain the kinase’s kinetochore localization and promote proper chromosome alignment in mitosis."
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