|PROSITE documentation PDOC51741|
All eukaryotic cells are surrounded by a plasma membrane, and they also contain multiple membrane-based organelles and structures inside cells. Thus membrane remodeling is likely to be important for most cellular activities and development. The Bin-Amphiphysin-Rvs (BAR) domain superfamily of proteins has been found to play a major role in remodeling cellular membranes linked with organelle biogenesis, membrane trafficking, cell division, cell morphology and cell migration. The BAR domain superfamily of proteins is evolutionarily conserved with representative members present from yeast to man. Currently there are three distinct families of BAR domain proteins: classical BAR (see <PDOC51021>), F-BAR (FCH-BAR e.g., Fes/CIP4 homology BAR e.g., Toca-1) and I-BAR (inverse-BAR e.g., IRSp53). The classical BAR, F-BAR, and I-BAR domains are structurally similar homodimeric modules with antiparallel arrangement of monomers [1,2].
The F-BAR domain is emerging as an important player in membrane remodeling pathways. F-BAR domain proteins couple membrane remodeling with actin dynamics associated with endocytic pathways and filopodium formation. F-BAR domain containing proteins can be categorized into five sub-families based on their phylogeny which is consistent with the additional protein domains they possess, for example, RhoGAP domains (see <PDOC50238>), Cdc42 binding sites, SH2 domains (see <PDOC50001>), SH3 domains (see <PDOC50002>) and tyrosine kinase domains (see <PDOC00100>) :
The N-terminal part (about one third) of the F-BAR domain was previously characterized as an FCH (FER-CIP4 homology) domain. However, the region of sequence similarity extends to an adjacent region with a coiled-coil (CC) structure. Hence, the F-BAR domain (FCH+CC, ~300 amino acids) has also been called extended FC (EFC) domain. The F-BAR domain plays a role in dimerization and membrane phospholipid binding. It binds specifically to certain kinds of lipids and acts as a a dimeric membrane-binding curvature effector [2,3,4].
The F-BAR domain is composed of five helices. Its structure is composed of a short N-terminal helix, three long α helices, and a short C-terminal helix followed by an extended peptide of 17 amino acids (see <PDB:2EFK>) [2,5].
The profile we developed covers the entire F-BAR domain.Last update:
December 2014 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Ahmed S. Bu W. Lee R.T. Maurer-Stroh S. Goh W.I.|
|Title||F-BAR domain proteins: Families and function.|
|Source||Commun. Integr. Biol. 3:116-121(2010).|
|2||Authors||Henne W.M. Kent H.M. Ford M.G.J. Hegde B.G. Daumke O. Butler P.J.G. Mittal R. Langen R. Evans P.R. McMahon H.T.|
|Title||Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature.|
|3||Authors||Itoh T. Erdmann K.S. Roux A. Habermann B. Werner H. De Camilli P.|
|Title||Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins.|
|Source||Dev. Cell 9:791-804(2005).|
|4||Authors||Tsujita K. Suetsugu S. Sasaki N. Furutani M. Oikawa T. Takenawa T.|
|Title||Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis.|
|Source||J. Cell Biol. 172:269-279(2006).|
|5||Authors||Shimada A. Niwa H. Tsujita K. Suetsugu S. Nitta K. Hanawa-Suetsugu K. Akasaka R. Nishino Y. Toyama M. Chen L. Liu Z.-J. Wang B.-C. Yamamoto M. Terada T. Miyazawa A. Tanaka A. Sugano S. Shirouzu M. Nagayama K. Takenawa T. Yokoyama S.|
|Title||Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis.|