BAR domain scaffolds in dynamin-mediated membrane fission.

Daumke O; Roux A; Haucke V

doi:10.1016/j.cell.2014.02.017

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Journal article

BAR domain scaffolds in dynamin-mediated membrane fission.

Daumke O Max-Delbrück Centrum für Molekulare Medizin, Robert-Rössle-Strasse 10, 13125 Berlin, Germany; Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustraße 6, 14195 Berlin, Germany. Electronic address: oliver.daumke@mdc-berlin.de.
Roux A University of Geneva, Department of Biochemistry, 30 quai Ernest Ansermet, 1211 Geneva 4, Switzerland, and Swiss National Centre for Competence in Research Programme Chemical Biology, 1211 Geneva, Switzerland. Electronic address: aurelien.roux@unige.ch.
Haucke V Leibniz Institut für Molekulare Pharmakologie (FMP), Robert-Rössle-Strasse 10, 13125 Berlin, Germany; NeuroCure Cluster of Excellence, Charité Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany. Electronic address: haucke@fmp-berlin.de.

2014-03-04

Published in:

Cell. - 2014

English Biological membranes undergo constant remodeling by membrane fission and fusion to change their shape and to exchange material between subcellular compartments. During clathrin-mediated endocytosis, the dynamic assembly and disassembly of protein scaffolds comprising members of the bin-amphiphysin-rvs (BAR) domain protein superfamily constrain the membrane into distinct shapes as the pathway progresses toward fission by the GTPase dynamin. In this Review, we discuss how BAR domain protein assembly and disassembly are controlled in space and time and which structural and biochemical features allow the tight regulation of their shape and function to enable dynamin-mediated membrane fission.

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