Loss of T73T75 phosphorylation on PP2A-B56Par1 advances mitotic entry and reduces S. pombe cell size
Halova, L.; Hagan, I. M.; Petersen, J.; Smith, D. L.; Connolly, Y.
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Mitosis is triggered when the rising activity of CDK1-Cyclin B, amplified by the CDK1/Cdc25/Wee1 feedback loop, overcomes inhibitory signalling from Wee1 and counteracting phosphatases. CDK-opposing phosphatases PP1, PP2A-B55 and PP2A-B56 are regulators of mitosis. A screen for differentially phosphorylated sites in a{Delta} PP1dis2 genetic background in Schizosaccharomyces pombe identified phosphorylation of T73 or T75 in the regulatory B56Par1 subunit. The B56Par1.T73T75 phosphorylation is directly mediated by CDK1-Cyclin B, and a phospho-mimetic mutation increased PP2A-B56Par1 phosphatase activity. Blocking B56Par1.T73T75 phosphorylation reduced cell length in unperturbed divisions from 14 to 12 {micro}m, with no other detectable phenotypes. Therefore, blocking phosphorylation at T73T75 alone prematurely unlocked amplification of the CDK1/Cdc25/Wee1 feedback loop, advancing cells into mitosis. Signalling from T73T75 reveals for the first time that timely mitotic commitment in unperturbed cycles is mediated by PP2A-B56.
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