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BAR domain scaffolds in dynamin-mediated membrane fission

Official URL:https://doi.org/10.1016/j.cell.2014.02.017
PubMed:View item in PubMed
Creators Name:Daumke, O. and Roux, A. and Haucke, V.
Journal Title:Cell
Journal Abbreviation:Cell
Volume:156
Number:5
Page Range:882-892
Date:27 February 2014
Keywords:Cell Membrane, Clathrin-Coated Vesicles, Dynamins, Endocytosis, Tertiary Protein Structure, Animals
Abstract: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.
ISSN:0092-8674
Publisher:Cell Press / Elsevier (U.S.A.)
Item Type:Review

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