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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

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Cdc14-dependent dephosphorylation of Inn1 contributes to Inn1-Cyk3 complex formation

Saravanan Palani1, Franz Meitinger, Martin E Boehm

  • 1Molecular Biology of Centrosomes and Cilia Unit, DKFZ-ZMBH Alliance, German Cancer Research Center (DKFZ), Heidelberg, Germany.

Journal of Cell Science
|March 29, 2012
PubMed

Insights

The Cdc14 phosphatase and its substrate Inn1 are crucial for cell division in Saccharomyces cerevisiae. Cdc14 counteracts M-Cdk1 phosphorylation of Inn1, promoting the Inn1-Cyk3 interaction essential for cytokinesis.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The Cdc14 phosphatase in Saccharomyces cerevisiae reverses mitotic cyclin-dependent kinase (M-Cdk1) phosphorylation, aiding mitotic exit.
  • Cdc14's localization at the cell division site suggests a role in cytokinesis, though it remains poorly understood.

Purpose of the Study:

  • To investigate the role of Cdc14 in cytokinesis by identifying its substrates.
  • To elucidate the mechanism by which Cdc14 regulates cytokinesis.

Main Methods:

  • Identification of Inn1 as a novel substrate of both M-Cdk1 and Cdc14.
  • Analysis of the interaction between Inn1, M-Cdk1, Cdc14, and Cyk3 using co-localization and interaction assays.
  • Investigating the effect of Inn1 phosphorylation on Cyk3 localization at the cell division site.

Main Results:

  • Inn1 is directly phosphorylated by both M-Cdk1 and Cdc14.
  • Cdc14 colocalizes with Inn1 at the cell division site and interacts with its proline-rich domain.
  • M-Cdk1 phosphorylation of Inn1 disrupts its interaction with Cyk3, reducing Cyk3 levels at the division site.

Conclusions:

  • Cdc14 plays a critical role in promoting cytokinesis by counteracting M-Cdk1-mediated phosphorylation of Inn1.
  • This action facilitates the formation of the Inn1-Cyk3 complex, which is essential for proper cell division.

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