Phosphorylation of the mitotic regulator Pds1/securin by Cdc28 is required for efficient nuclear localization of Esp1/separase.

Sister chromatid separation at the metaphase-to-anaphase transition is induced by the proteolytic cleavage of one of the cohesin complex subunits. This process is mediated by a conserved protease called separase. Separase is associated with its inhibitor, securin, until the time of anaphase initiation, when securin is degraded in an anaphase-promoting ...
complex/cyclosome (APC/C)-dependent manner. In budding yeast securin/Pds1 not only inhibits separase/Esp1, but also promotes its nuclear localization. The molecular mechanism and regulation of this nuclear targeting are presently unknown. Here we show that Pds1 is a substrate of the cyclin-dependent kinase Cdc28. Phosphorylation of Pds1 by Cdc28 is important for efficient binding of Pds1 to Esp1 and for promoting the nuclear localization of Esp1. Our results uncover a previously unknown mechanism for regulating the Pds1-Esp1 interaction and shed light on a novel role for Cdc28 in promoting the metaphase-to-anaphase transition in budding yeast.
Mesh Terms:
Active Transport, Cell Nucleus, Alanine, Amino Acid Sequence, CDC28 Protein Kinase, S cerevisiae, Cell Cycle Proteins, Cell Nucleus, Chromatids, DNA Damage, Endopeptidases, Escherichia coli, Fungal Proteins, Microscopy, Fluorescence, Mitosis, Models, Biological, Molecular Sequence Data, Mutagenesis, Site-Directed, Nuclear Proteins, Phosphoric Monoester Hydrolases, Phosphorylation, Plasmids, Precipitin Tests, Protein Binding, Saccharomyces cerevisiae Proteins, Temperature, Time Factors, Yeasts
Genes Dev.
Date: Jun. 01, 2002
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