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Cell division cycle 14A is a human dual-specificity protein tyrosine phosphatase that regulates cell division, cell cycle exit, and the initiation of DNA replication, and is highly homologous to yeast Cdc14. Unlike its yeast orthologs, CDC14A in humans is not essential for cell viability or mitotic exit, but instead plays a crucial role in the regulation of cell migration, adhesion, and actin cytoskeleton dynamics, as well as in tumor suppression through dephosphorylation and stabilization of p53. CDC14A expression is frequently down-regulated in cancer tissues, and loss of function is associated with enhanced cell motility, reduced adhesion, and increased tumor aggressiveness, contributing to poor prognosis. It may directly modulate proteins such as KIBRA (a Hippo pathway component) and interact with cell-cycle regulatory pathways. Alternative splicing results in multiple isoforms. Mutations in CDC14A have been linked to hereditary deafness. No approved therapeutic agents directly target this phosphatase, but it remains a potential target for cancer therapy and other conditions involving disrupted cell division and migration.
Hypothetical mechanisms (no drugs validated) would include inhibition or modulation of phosphatase activity, potentially influencing cell migration, adhesion, or cell cycle progression. In cancer, loss of CDC14A activity promotes metastasis, so restoration or potentiation of its function could be therapeutically relevant. Inherited mutations cause deafness syndromes, but no mechanism is identified for approved therapies.
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