Helmholtz Gemeinschaft

Search
Browse
Statistics
Feeds

BAR domain scaffolds in dynamin-mediated membrane fission

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

Repository Staff Only: item control page

Open Access
MDC Library