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Published August 2013 | Published + Supplemental Material
Journal Article Open

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

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 its immediate 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.

Additional Information

© 2013 The Authors. Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/3.0/, which permits unrestricted use, provided the original author and source are credited. Received: 17 May 2013. Accepted: 4 July 2013. We thank J. Brill, R. Karess, M. Mishima and A. Kiger for providing us with reagents, Bloomington Fly Stock centre for flies and Developmental Studies Hybridoma Bank for anti-Rho1 antibody. We also thank T. Naughton, A. C. Field and S. Takeda for their technical support and J. Dębski for the mass spectrometry analyses, and P. P. D'Avino, C. Lindon, M. Przewloka and M. Takeda for their critical reading of the manuscript and discussion. This work was supported by a Medical Research Council grant (G0802208) to I.M.R., a grant from Leukemia Lymphoma Research to A.D.W., Medical Research Council grant (U105178795) to H.T.M. and a Cancer Research UK Program grant (C3/A11431) to D.M.G.

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Created:
August 19, 2023
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