Phospho-regulation of the Cdc14/Clp1 phosphatase delays late mitotic events in S. pombe.

Wolfe BA, McDonald WH, Yates JR, Gould KL
Dev Cell. 2006 11 (3): 423-30

PMID: 16950131 · DOI:10.1016/j.devcel.2006.07.016

In eukaryotes, exit from mitosis occurs through the inactivation of the Cdk1-cyclin B kinase complex and the reversal of its phosphorylation events. These late mitotic events are tightly regulated to occur only after the onset of anaphase and prior to cytokinesis. Central to this regulation is the conserved Cdc14 family of protein phosphatases, whose activity reverses Cdk-dependent phosphorylation events. S. cerevisiae Cdc14 activity is restrained from dephosphorylating Cdk substrates and inactivating Cdk1 through its nucleolar sequestration prior to anaphase. Here, we describe a unique mode of Cdc14 regulation that operates prior to anaphase in fission yeast. Cdk1 phosphorylates and inhibits the catalytic activity of the Cdc14 family member, Clp1/Flp1. As Cdk1 activity declines during anaphase progression, Clp1/Flp1 autocatalytically reverses these phosphorylation events to stimulate its own activity. These findings point to a simple regulatory circuit that couples Cdk1 activation with its inactivation mediated through phosphorylation-dependent regulation of Clp1/Flp1 phosphatase activity.

MeSH Terms (13)

CDC2 Protein Kinase Cell Cycle Cell Cycle Proteins Chromosome Segregation Enzyme Activation Gene Expression Regulation, Fungal Mitosis Models, Biological Phosphoprotein Phosphatases Phosphorylation Protein Tyrosine Phosphatases Schizosaccharomyces Schizosaccharomyces pombe Proteins

Connections (2)

This publication is referenced by other Labnodes entities: