Abstract：
:The Schizosaccaromyces pombe protein Flp1p belongs to a conserved family of serine-threonine-phosphatases. The founding member of this family, Saccharomyces cerevisiae Cdc14p, is required for inactivation of mitotic CDKs and reversal of CDK mediated phosphorylation at the end of mitosis, thereby bringing about the M-G1 transition. Initial studies of Flp1p suggest that it may play a different role to Cdc14p. Here we show that Flp1p is required for rapid degradation of the mitotic inducer Cdc25p at the end of mitosis, and that Cdc25p is a substrate of Flp1p in vitro. Down-regulation of Cdc25p activity by Flp1p may ensure a prompt inactivation of mitotic CDK complexes to trigger cell division. Our results suggest a regulatory mechanism, and a universal role, for Cdc14p like proteins in coordination of cytokinesis with other cell cycle events.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Esteban V,Blanco M,Cueille N,Simanis V,Moreno S,Bueno Adoi
10.1242/jcs.01107keywords:
subject
Has Abstractpub_date
2004-05-15 00:00:00pages
2461-8issue
Pt 12eissn
0021-9533issn
1477-9137pii
jcs.01107journal_volume
117pub_type
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