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PMID: 21878992 Published · epublish English Journal Article Research Support, Non-U.S. Gov't Review

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

The EMBO journal ·Vol. 30 ·No. 17 ·2011-08-31 ·Pages 3501-15

Qualmann B, Koch D, Kessels MM

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.

MeSH Terms
Animals Cell Membrane/chemistry,metabolism Clathrin/chemistry,metabolism Endocytosis/physiology Humans Membrane Proteins/chemistry,metabolism Mice Nerve Tissue Proteins/chemistry,metabolism Protein Structure, Tertiary Transport Vesicles/chemistry,metabolism
Chemicals
Clathrin Membrane Proteins Nerve Tissue Proteins amphiphysin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Qualmann Britta
Institute for Biochemistry I, University Hospital Jena-Friedrich Schiller University Jena, Germany. [email protected]
Koch Dennis
Kessels Michael Manfred
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
1460-2075
Published
2011-08-31
Epub
2011-00-31
Pages
3501-15
Language
English
Region
England
NLM ID
8208664
PMCID
PMC3181480
Subset
IM
Analysis Services
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