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Mechanistic Insights into Membrane Remodeling Through BAR‐Domain Proteins
Author(s) -
Frost Adam,
Mim Carsten,
Perera Rushika,
Spasov Krasimir,
Egelman Edward,
De Camilli Pietro,
Unger Vinzenz M
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.82.2
Subject(s) - membrane curvature , context (archaeology) , membrane , bar (unit) , biophysics , membrane biophysics , chemistry , domain (mathematical analysis) , membrane protein , microbiology and biotechnology , biology , lipid bilayer , physics , biochemistry , paleontology , mathematical analysis , mathematics , meteorology
Critical to cellular physiology, cells constantly manipulate the shape of their constituent membranes through processes whose mechanisms are poorly understood. A major limitation in the study of membrane remodeling is the lack of structural information that visualizes membrane‐remodeling domains in the context of their bilayer substrates. Overcoming this bottleneck, we obtained structural models for two membrane‐bound states of F‐BAR domains by electron cryomicroscopy and image reconstruction. The models suggest that F‐BAR domains can engage bilayers through two very different molecular surfaces that are aligned with functional states prior to, and after induction of membrane curvature. Moreover, the reconstructions reveal how curvature is generated through the cooperative assembly of a highly organized protein scaffold, and how subtle changes in the orientation of dimeric F‐BAR modules facilitate the generation of structures with a range of different curvatures. Supported by PHS grant DA024101