|SMART accession number:||SM00721
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|Interpro abstract (IPR004148):
Endocytosis and intracellular transport involve several mechanistic steps:
Members of the Amphiphysin protein family are key regulators in the early steps of endocytosis, involved in the formation of clathrin-coated vesicles by promoting the assembly of a protein complex at the plasma membrane and directly assist in the induction of the high curvature of the membrane at the neck of the vesicle. Amphiphysins contain a characteristic domain, known as the BAR (Bin-Amphiphysin-Rvs)-domain, which is required for their in vivo function and their ability to tubulate membranes [(PUBMED:14993925)].
- (1) for the internalisation of cargo molecules, the membrane needs to bend to form a vesicular structure, which requires membrane curvature and a rearrangement of the cytoskeleton;
- (2) following its formation, the vesicle has to be pinched off the membrane;
- (3) the cargo has to be subsequently transported through the cell and the vesicle must fuse with the correct cellular compartment.
The crystal structure of these proteins suggest the domain forms a crescent-shaped dimer of a three-helix coiled coil with a characteristic set of conserved hydrophobic, aromatic and hydrophilic amino acids. Proteins containing this domain have been shown to homodimerise, heterodimerise or, in a few cases, interact with small GTPases.
|GO component:||cytoplasm (GO:0005737)|
|GO function:||protein binding (GO:0005515)|
There are 2778 BAR domains in 2753 proteins in SMART's nrdb database.
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- Evolution (species in which this domain is found)
- Literature (relevant references for this domain)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
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