PP2ACdc55 dephosphorylates Pds1 and inhibits spindle elongation.

PP2ACdc55 regulates cell cycle progression by reversing cyclin-dependent kinase (CDK) and polo-like kinase (Cdc5) dependent phosphorylation events. In S. cerevisiae, Cdk1 phosphorylates securin (Pds1), which facilitates Pds1 binding and inhibiting separase (Esp1). During anaphase, Esp1 cleaves the cohesin subunit Scc1 and promotes spindle elongation. Here, we show that PP2ACdc55 directly dephosphorylates Pds1 both in vivo and in vitro. Pds1 hyperphosphorylation in a cdc55 deletion mutant enhanced the Pds1-Esp1 interaction, which played a positive role in Pds1 nuclear accumulation and in spindle elongation. We also show that nuclear PP2ACdc55 played a role during replication stress to inhibit spindle elongation. This pathway acted independently of the known Mec1, Swe1 or Spindle Assembly Checkpoint (SAC) checkpoint pathways. We propose a model where Pds1 dephosphorylation by PP2ACdc55 disrupts the Pds1-Esp1 protein interaction and inhibits Pds1 nuclear accumulation, which prevents spindle elongation, a process that is elevated during replication stress. © 2020. Published by The Company of Biologists Ltd.

Citation

Shoily Khondker, Sam Kajjo, Devon Chandler-Brown, Jan Skotheim, Adam Rudner, Amy Ikui. PP2ACdc55 dephosphorylates Pds1 and inhibits spindle elongation. Journal of cell science. 2020 Jan 01

PMID: 34005308

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