IndraLab

Statements

PLK1 activates USP16. 11 / 15
4 | 2 5
signor
"Plk1 phosphorylates and activates Usp16. In vitro phosphorylation of Usp16 with single (S330A, S386A, or S486A) or collective 3A (S330A/S386A/S486A) mutation showed that Plk1 phosphorylated Usp16 at all three sites (Fig. S2 D)."
26323689
signor
"In this study, we show that ubiquitin-specific peptidase 16 (Usp16) is a novel substrate for Plk1, and sequential phosphorylation by CDK1 and Plk1 activates Usp16, which, in turn, deubiquitinates Plk1 and promotes the recruitment of Plk1 to, and its retention on, the kinetochores for proper chromosome alignment.|In vitro phosphorylation of Usp16 with single (S330A, S386A, or S486A) or collective 3A (S330A/S386A/S486A) mutation showed that Plk1 phosphorylated Usp16 at all three sites (Fig."
26323689
sparser
"These results strongly suggest that Plk1 phosphorylates and activates Usp16, but the exact molecular mechanism of the activation is not clear at the moment."
26323689
reach
"Because Usp16 deubiquitinates Plk1, we wondered whether Plk1 mediated Usp16 activation would also enhance the deubiquitination of Plk1 itself."
26323689
reach
"These results suggest that Plk1 activates Usp16, which, in turn, deubiquitinates Plk1 itself."
26323689
sparser
"Plk1 phosphorylates and activates Usp16."
26323689
sparser
"We found that the level of ubiquitinated histone H2A (ubH2A) was high in interphase and low in mitotic HeLa cells (Fig. S3, C–E), suggesting that Plk1 phosphorylates and activates Usp16."
26323689
signor
"Plk1 phosphorylates and activates Usp16. In vitro phosphorylation of Usp16 with single (S330A, S386A, or S486A) or collective 3A (S330A/S386A/S486A) mutation showed that Plk1 phosphorylated Usp16 at all three sites (Fig. S2 D)."
26323689
signor
"Plk1 phosphorylates and activates Usp16. In vitro phosphorylation of Usp16 with single (S330A, S386A, or S486A) or collective 3A (S330A/S386A/S486A) mutation showed that Plk1 phosphorylated Usp16 at all three sites (Fig. S2 D)."
26323689
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."
26323689
sparser
"These results suggest that Plk1 activates Usp16, which, in turn, deubiquitinates Plk1 itself."
26323689