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Let's go bananas: revisiting the endocytic BAR code.

Authors
  • Qualmann, Britta
  • Koch, Dennis
  • Kessels, Michael Manfred
Type
Published Article
Journal
The EMBO Journal
Publisher
EMBO
Publication Date
Aug 31, 2011
Volume
30
Issue
17
Pages
3501–3515
Identifiers
DOI: 10.1038/emboj.2011.266
PMID: 21878992
Source
Medline
License
Unknown

Abstract

Against the odds of membrane resistance, members of the BIN/Amphiphysin/Rvs (BAR) domain superfamily shape membranes and their activity is indispensable for a plethora of life functions. While crystal structures of different BAR dimers advanced our understanding of membrane shaping by scaffolding and hydrophobic insertion mechanisms considerably, especially life-imaging techniques and loss-of-function studies of clathrin-mediated endocytosis with its gradually increasing curvature show that the initial idea that solely BAR domain curvatures determine their functions is oversimplified. Diagonal placing, lateral lipid-binding modes, additional lipid-binding modules, tilde shapes and formation of macromolecular lattices with different modes of organisation and arrangement increase versatility. A picture emerges, in which BAR domain proteins create macromolecular platforms, that recruit and connect different binding partners and ensure the connection and coordination of the different events during the endocytic process, such as membrane invagination, coat formation, actin nucleation, vesicle size control, fission, detachment and uncoating, in time and space, and may thereby offer mechanistic explanations for how coordination, directionality and effectiveness of a complex process with several steps and key players can be achieved.

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