Mitotic phosphorylation of the peripheral golgi protein Nir2 by Cdk1 provides a docking mechanism for Plk1 and affects cytokinesis completion

Vladimir Litvak, Rachel Argov, Nili Dahan, Sreekumar Ramachandran, Roy Amarilio, Alla Shainskaya, Sima Lev

Research output: Contribution to journalArticlepeer-review

Abstract

The rearrangement of the Golgi apparatus during mitosis is regulated by several protein kinases, including Cdk1 and Plk1. Several peripheral Golgi proteins that dissociate from the Golgi during mitosis are implicated in regulation of cytokinesis or chromosome segregation, thereby coordinating mitotic and cytokinetic events to Golgi rearrangement. Here we show that, at the onset of mitosis, Cdk1 phosphorylates the peripheral Golgi protein Nir2 at multiple sites; of these, S382 is the most prominent. Phosphorylation of Nir2 by Cdk1 facilitates its dissociation from the Golgi apparatus, and phospho-Nir2(pS382) is localized in the cleavage furrow and midbody during cytokinesis. Mitotic phosphorylation of Nir2 is required for docking of the phospho-Ser/Thr binding module, the Polo box domain of Plk1, and overexpression of a Nir2 mutant, which fails to interact with Plk1, affects the completion of cytokinesis. These results demonstrate a mechanism for coordinating mitotic and cytokinetic events with Golgi rearrangement during cell division.

Original languageEnglish (US)
Pages (from-to)319-330
Number of pages12
JournalMolecular cell
Volume14
Issue number3
DOIs
StatePublished - May 7 2004
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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