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Dual specificity protein phosphatase CDC14B (CDC14B) is an enzyme encoded by the CDC14B gene in humans. It belongs to the dual specificity protein tyrosine phosphatase family, with both tyrosine and serine/threonine phosphatase activity. CDC14B is highly homologous to yeast Cdc14 and regulates cell cycle progression, particularly the G2 DNA damage checkpoint and mitotic exit. It acts by dephosphorylating targets such as FZR1/CDH1, enabling activation of the anaphase promoting complex (APC/C), and regulates microtubule organization by stabilizing and bundling microtubules. CDC14B also modulates tumor suppressor protein p53 via site-specific dephosphorylation, affecting its stability and function, and can alter SIRT2 phosphorylation during early anaphase. Disruptions of CDC14B function can lead to cell cycle abnormalities, genomic instability, premature aging, and potentially contribute to disease processes including cancer.
Drugs would theoretically act through modulation of phosphatase activity—specifically, inhibition or activation of CDC14B’s dephosphorylation of key substrates such as p53, FZR1/CDH1, SIRT2, and those involved in G2/M checkpoint regulation
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