Human phosphatase CDC14A regulates actin organization through dephosphorylation of epithelial protein lost in neoplasm.

ABSTRACT: CDC14 is an essential dual-specificity phosphatase that counteracts CDK1 activity during anaphase to promote mitotic exit in Saccharomyces cerevisiae Surprisingly, human CDC14A is not essential for cell cycle progression. Instead, it regulates cell migration and cell adhesion. Little is known about the substrates of hCDC14A and the counteracting kinases. Here, we combine phospho-proteome profiling and proximity-dependent biotin identification to identify hCDC14A substrates. Among these targets were actin regulators, including the tumor suppressor eplin. hCDC14A counteracts EGF-induced rearrangements of actin cytoskeleton by dephosphorylating eplin at two known extracellular signal-regulated kinase sites, serine 362 and 604. hCDC14A^PD and eplin knockout cell lines exhibite

SUBMITTER: Chen NP 

PROVIDER: S-EPMC5441781 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature