FNBP1L
Domain
The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation (By similarity).
Function
Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. May bind to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promote membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by activating the WASL/N-WASP-WASPIP/WIP complex, the predominant form of WASL/N-WASP in cells. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Essential for autophagy of intracellular bacterial pathogens.
Sequence Similarities
Belongs to the FNBP1 family.
Cellular localization
- Cytoplasm
- Cytoplasm
- Cytoskeleton
- Cytoplasm
- Cell cortex
- Cytoplasmic vesicle
- Cell membrane
- Peripheral membrane protein
- Cytoplasmic side
Alternative names
C1orf39, TOCA1, FNBP1L, Formin-binding protein 1-like, Transducer of Cdc42-dependent actin assembly protein 1, Toca-1