Inhibition of endocytic vesicle fusion by Plk1-mediated phosphorylation of vimentin during mitosis

Cell Cycle. 2014;13(1):126-37. doi: 10.4161/cc.26866. Epub 2013 Oct 25.

Abstract

Endocytic vesicle fusion is inhibited during mitosis, but the molecular pathways that mediate the inhibition remain unclear. Here we uncovered an essential role of Polo-like kinase 1 (Plk1) in this mechanism. Phosphoproteomic analysis revealed that Plk1 phosphorylates the intermediate filament protein vimentin on Ser459, which is dispensable for its filament formation but is necessary for the inhibition of endocytic vesicle fusion in mitosis. Furthermore, this mechanism is required for integrin trafficking toward the cleavage furrow during cytokinesis. Our results thus identify a novel mechanism for fusion inhibition in mitosis and implicate its role in vesicle trafficking after anaphase onset.

Keywords: Plk1; endosome; mitosis; vesicle fusion; vimentin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anaphase / genetics
  • Cell Cycle Proteins / genetics*
  • Cell Cycle Proteins / metabolism
  • Cytokinesis
  • HeLa Cells
  • Humans
  • Mitosis / genetics*
  • Phosphorylation / genetics
  • Protein-Serine-Threonine Kinases / genetics*
  • Protein-Serine-Threonine Kinases / metabolism
  • Proto-Oncogene Proteins / genetics*
  • Proto-Oncogene Proteins / metabolism
  • Transport Vesicles / genetics*
  • Transport Vesicles / metabolism
  • Vimentin / metabolism*

Substances

  • Cell Cycle Proteins
  • Proto-Oncogene Proteins
  • Vimentin
  • Protein-Serine-Threonine Kinases
  • polo-like kinase 1