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USP16 deubiquitinates PLK1. 8 / 8
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"ubiquitinspecific peptidase 16 (Usp16) was identified as a PLK1 interacting protein in a co-immunoprecipitation (co-IP) assay in a PBD-dependent manner"
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"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."
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"Collectively, these results suggest that Plk1 is ubiquitinated by CUL3 based ubiquitin ligase in vivo, and the ubiquitination of Plk1 could be reversed by Usp16, which interacts with Plk1 in a PBD dependent manner in early mitosis."
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"Usp16 interacts with and deubiquitinates Plk1."
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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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"When Usp16 was knocked down by siRNA, we found that the ladder pattern bands above the main Plk1 band were enhanced, confirming our previous speculation that Usp16 might deubiquitinate Plk1 (XREF_FIG)."
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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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"Usp16 deubiquitinates Plk1, resulting in an enhanced interaction with kinetochore localized proteins such as BubR1, and thereby retains Plk1 on the kinetochores to promote proper chromosome alignment in early mitosis."
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