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PLK1 phosphorylates OTUD3. 5 / 5
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"We found that PLK1 mediates OTUD3 phosphorylation to enhance its binding abilities, resulting in YY1 stability.In this study, OTUD3 was identified to be an effective DUB for de-polyubiquitination of YY1."
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"In vitro kinase assays showed that OTUD3 protein was phosphorylated by Myc-PLK1 protein that were purified from HEK-293T cells (Fig. xref )."
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"Additional experiments showed that PLK1 failed to phosphorylate OTUD3 with Ser-326A mutations (Fig. 5J)."
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"Identification of OTUD3 phosphorylation by PLK1 adds a new layer of complexity to regulation of this signaling pathway and highlights the importance of phosphorylation in regulation of DUBs (Fig. xref )."
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"Identification of OTUD3 phosphorylation by PLK1 adds a new layer of complexity to regulation of this signaling pathway and highlights the importance of phosphorylation in regulation of DUBs (Fig. 6I)."
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