IndraLab

Statements

PLK1 activates USP16. 7 / 11
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"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."
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"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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"Because Usp16 deubiquitinates Plk1, we wondered whether Plk1 mediated Usp16 activation would also enhance the deubiquitination of Plk1 itself."
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"These results suggest that Plk1 activates Usp16, which, in turn, deubiquitinates Plk1 itself."
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"Plk1 phosphorylates and activates Usp16."
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"These results suggest that Plk1 activates Usp16, which, in turn, deubiquitinates Plk1 itself."
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"These results strongly suggest that Plk1 phosphorylates and activates Usp16, but the exact molecular mechanism of the activation is not clear at the moment."
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