Ontology highlight
ABSTRACT:
SUBMITTER: Frost A
PROVIDER: S-EPMC2384079 | biostudies-literature | 2008 Mar
REPOSITORIES: biostudies-literature
Frost Adam A Perera Rushika R Roux Aurélien A Spasov Krasimir K Destaing Olivier O Egelman Edward H EH De Camilli Pietro P Unger Vinzenz M VM
Cell 20080301 5
BAR superfamily domains shape membranes through poorly understood mechanisms. We solved structures of F-BAR modules bound to flat and curved bilayers using electron (cryo)microscopy. We show that membrane tubules form when F-BARs polymerize into helical coats that are held together by lateral and tip-to-tip interactions. On gel-state membranes or after mutation of residues along the lateral interaction surface, F-BARs adsorb onto bilayers via surfaces other than their concave face. We conclude t ...[more]