Drosophila F-BAR protein Syndapin contributes to coupling the plasma membrane and contractile ring in cytokinesis

Tetsuya Takeda, Iain M. Robinson, Matthew M. Savoian, John R. Griffiths, Anthony D. Whetton, Harvey T. McMahon, David M. Glover

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Cytokinesis is a highly ordered cellular process driven by interactions between central spindle microtubules and the actomyosin contractile ring linked to the dynamic remodelling of the plasma membrane. The mechanisms responsible for reorganizing the plasma membrane at the cell equator and its coupling to the contractile ring in cytokinesis are poorly understood. We report here that Syndapin, a protein containing an F-BAR domain required for membrane curvature, contributes to the remodelling of the plasma membrane around the contractile ring for cytokinesis. Syndapin colocalizes with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) at the cleavage furrow, where it directly interacts with a contractile ring component, Anillin. Accordingly, Anillin is mislocalized during cytokinesis in Syndapin mutants. Elevated or diminished expression of Syndapin leads to cytokinesis defects with abnormal cortical dynamics. The minimal segment of Syndapin, which is able to localize to the cleavage furrow and induce cytokinesis defects, is the F-BAR domain and itsimmediate C-terminal sequences. Phosphorylation of this region prevents this functional interaction, resulting in reduced ability of Syndapin to bind to and deform membranes. Thus, the dephosphorylated form of Syndapin mediates both remodelling of the plasma membrane and its proper coupling to the cytokinetic machinery.

Original languageEnglish
Article number130081
JournalOpen Biology
Volume3
Issue numberAUG
DOIs
Publication statusPublished - Aug 7 2013
Externally publishedYes

Fingerprint

Cytokinesis
Cell membranes
Drosophila
Cell Membrane
Proteins
Membranes
Actomyosin
Defects
Phosphorylation
Phosphatidylinositols
Machinery
Microtubules
anillin

Keywords

  • Actomyosin contractile ring
  • Cytokinesis
  • F-BAR
  • Membrane
  • Phosphorylation
  • Tetsuya Takeda

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Neuroscience(all)
  • Immunology
  • Medicine(all)

Cite this

Takeda, T., Robinson, I. M., Savoian, M. M., Griffiths, J. R., Whetton, A. D., McMahon, H. T., & Glover, D. M. (2013). Drosophila F-BAR protein Syndapin contributes to coupling the plasma membrane and contractile ring in cytokinesis. Open Biology, 3(AUG), [130081]. https://doi.org/10.1098/rsob.130081

Drosophila F-BAR protein Syndapin contributes to coupling the plasma membrane and contractile ring in cytokinesis. / Takeda, Tetsuya; Robinson, Iain M.; Savoian, Matthew M.; Griffiths, John R.; Whetton, Anthony D.; McMahon, Harvey T.; Glover, David M.

In: Open Biology, Vol. 3, No. AUG, 130081, 07.08.2013.

Research output: Contribution to journalArticle

Takeda, T, Robinson, IM, Savoian, MM, Griffiths, JR, Whetton, AD, McMahon, HT & Glover, DM 2013, 'Drosophila F-BAR protein Syndapin contributes to coupling the plasma membrane and contractile ring in cytokinesis', Open Biology, vol. 3, no. AUG, 130081. https://doi.org/10.1098/rsob.130081
Takeda, Tetsuya ; Robinson, Iain M. ; Savoian, Matthew M. ; Griffiths, John R. ; Whetton, Anthony D. ; McMahon, Harvey T. ; Glover, David M. / Drosophila F-BAR protein Syndapin contributes to coupling the plasma membrane and contractile ring in cytokinesis. In: Open Biology. 2013 ; Vol. 3, No. AUG.
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