Structural characteristics of BAR domain superfamily to sculpt the membrane.
Membrane dynamics is an essential process for cell locomotion, cytokinesis, vesicular transport and organelle morphogenesis. Formation of tubes or buds from a nearly flat membrane is a widely spread feature of the membrane shape changes. The BAR (Bin/Amphiphysin/Rvs-homology) domain dimers exhibit long extended curved shapes and appear to be outstandingly suitable modules for this purpose. So far, crystal structures of 18 independent BAR domains including inverse-BAR domains and FCH-BAR domains have been reported. These atomic models show a vast variation of dimer shapes on a common and simple basic framework. Comparison of the structural variations with respect to differences in membrane sculpting properties provide useful clues about the mechanisms for modifying the framework into a particular dimer that generates and/or senses a distinct curvature set of the membrane.
Masuda
Michitaka
M
Department of Structural Analysis, National Cardiovascular Center Research Institute, 5-7-1 Fujishiro-dai, Suita, Osaka 565-0865, Japan. masuda61@ri.ncvc.go.jp
Mochizuki
Naoki
N
D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry* / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D002462:Cell Membrane / Q000737:chemistry / Q000648:ultrastructure; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000235:genetics; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D048868:Adaptor Proteins, Signal Transducing; D009419:Nerve Tissue Proteins; C075637:amphiphysin