期刊
CELL
卷 132, 期 5, 页码 807-817出版社
CELL PRESS
DOI: 10.1016/j.cell.2007.12.041
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资金
- NCI NIH HHS [CA46128, P01 CA046128] Funding Source: Medline
- NCRR NIH HHS [P41 RR017573, P41 RR17573] Funding Source: Medline
- NIBIB NIH HHS [EB001567, R01 EB001567] Funding Source: Medline
- NIDA NIH HHS [P30 DA018343, DA024101, R21 DA024101-01, R21 DA024101] Funding Source: Medline
- NIDDK NIH HHS [DK45735, P30 DK045735] Funding Source: Medline
- NIGMS NIH HHS [R01 GM071590-03, 5T32GM07205, R01 GM071590, R01 GM071590-02, GM071590, T32 GM007205] Funding Source: Medline
- PHS HHS [NCRR 19895-02] Funding Source: Medline
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 that membrane binding is separable from membrane bending, and that imposition of the module's concave surface forces fluid-phase bilayers to bend locally. Furthermore, exposure of the domain's lateral interaction surface through a change in orientation serves as the crucial trigger for assembly of the helical coat and propagation of bilayer bending. The geometric constraints and sequential assembly of the helical lattice explain how F-BAR and classical BAR domains segregate into distinct microdomains, and provide insight into the spatial regulation of membrane invagination.
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