IndraLab

Statements


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sparser
"Next, we treated HeLa cells with CDK1 inhibitor RO3306 and observed a significant reduction in Plk1Usp16 interaction ( xref )."

sparser
"Because Usp16 interacts with Plk1, we suspected that it might deubiquitinate Plk1."

sparser
"Collectively, our results strongly suggest that CDK1 promotes the interaction between Plk1 and Usp16 and enhances the phosphorylation of Usp16 by Plk1."

reach
"Collectively, our results strongly suggest that CDK1 promotes the interaction between Plk1 and Usp16 and enhances the phosphorylation of Usp16 by Plk1."

sparser
"These data strongly suggest that the phosphorylation of S552 by CDK1 promotes Plk1Usp16 interaction."

No evidence text available

reach
"Recently, CDK1 dependent phosphorylation of Usp16 on S552 was shown to promote an interaction between Usp16 and Plk1."

No evidence text available

sparser
"Because Usp16 is phosphorylated by CDK1 ( xref ; xref ), we speculated that CDK1 might serve as a priming kinase regulating Plk1Usp16 interaction in a way similar to other cases ( xref ; xref )."

reach
"To identify any deubiquitylases that may deubiquitinate Plk1 in early mitosis, we performed reciprocal coimmunoprecipitation (coIP) assays and found that Usp16 specifically interacted with Plk1 in nocodazole arrested prometaphase HeLa cells (XREF_FIG)."

sparser
"To identify any deubiquitylases that may deubiquitinate Plk1 in early mitosis, we performed reciprocal coimmunoprecipitation (coIP) assays and found that Usp16 specifically interacted with Plk1 in nocodazole-arrested prometaphase HeLa cells ( xref )."

reach
"Usp16 interacts with and deubiquitinates Plk1."

reach
"Because Usp16 interacts with Plk1, we suspected that it might deubiquitinate Plk1."

reach
"Examination of the GST pull-down complexes showed that Usp16 specifically interacted with the wild-type (WT) PBD but not the PBD2A mutant (XREF_FIG), indicating that the interaction between Plk1 and Usp16 is PBD dependent."

No evidence text available

No evidence text available

sparser
"Examination of the GST pull-down complexes showed that Usp16 specifically interacted with the wild-type (WT) PBD but not the PBD2A mutant ( xref ), indicating that the interaction between Plk1 and Usp16 is PBD dependent."