FEBS Letters
Volume 583, Issue 21 , Pages 3401-3404, 3 November 2009

The direction of actin polymerization for vesicle fission suggested from membranes tubulated by the EFC/F-BAR domain protein FBP17

Edited by Felix Wieland

  • Shiro Suetsugu

      Affiliations

    • Corresponding Author InformationAddress: Laboratory of Membrane and Cytoskeleton Dynamics, Institute of Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.

Laboratory of Membrane and Cytoskeleton Dynamics, Institute of Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan

PRESTO, Japan Science and Technology Agency, Kawaguchi-shi, Saitama 332-0012, Japan

Received 10 September 2009; received in revised form 5 October 2009; accepted 6 October 2009. published online 13 October 2009.

Abstract 

Actin polymerization mediated by the Arp2/3 complex is essential for membrane tubulation, vesicle formation and fission during clathrin-dependent endocytosis. However, the mechanism by which the polymerizing actin filaments participate in vesicle formation and fission has remained unclear. Our analyses revealed that actin polymerization occurs toward FBP17-induced membrane tubules, which are considered to be generated during endocytic vesicle formation. The tubulated membrane between the future endocytic vesicle and the plasma membrane is proposed to form an arc upon scission of the endocytic vesicle. Therefore, the actin polymerization toward the tubulated membrane may be gradually converted to those toward both the vesicles and the plasma membrane.

Keywords: Actin, Neural Wiskott–Aldrich syndrome protein, Endocytosis, Extended FCH domain, F-BAR domain, Vesicle movement

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PII: S0014-5793(09)00791-1

doi:10.1016/j.febslet.2009.10.019

FEBS Letters
Volume 583, Issue 21 , Pages 3401-3404, 3 November 2009

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