| First Author | Becalska AN | Year | 2013 |
| Journal | Mol Biol Cell | Volume | 24 |
| Issue | 15 | Pages | 2406-18 |
| PubMed ID | 23761074 | Mgi Jnum | J:269553 |
| Mgi Id | MGI:6274959 | Doi | 10.1091/mbc.E13-05-0271 |
| Citation | Becalska AN, et al. (2013) Formation of membrane ridges and scallops by the F-BAR protein Nervous Wreck. Mol Biol Cell 24(15):2406-18 |
| abstractText | Eukaryotic cells are defined by extensive intracellular compartmentalization, which requires dynamic membrane remodeling. FER/Cip4 homology-Bin/amphiphysin/Rvs (F-BAR) domain family proteins form crescent-shaped dimers, which can bend membranes into buds and tubules of defined geometry and lipid composition. However, these proteins exhibit an unexplained wide diversity of membrane-deforming activities in vitro and functions in vivo. We find that the F-BAR domain of the neuronal protein Nervous Wreck (Nwk) has a novel higher-order structure and membrane-deforming activity that distinguishes it from previously described F-BAR proteins. The Nwk F-BAR domain assembles into zigzags, creating ridges and periodic scallops on membranes in vitro. This activity depends on structural determinants at the tips of the F-BAR dimer and on electrostatic interactions of the membrane with the F-BAR concave surface. In cells, Nwk-induced scallops can be extended by cytoskeletal forces to produce protrusions at the plasma membrane. Our results define a new F-BAR membrane-deforming activity and illustrate a molecular mechanism by which positively curved F-BAR domains can produce a variety of membrane curvatures. These findings expand the repertoire of F-BAR domain mediated membrane deformation and suggest that unique modes of higher-order assembly can define how these proteins sculpt the membrane. |
