Structural highlights
Function
[G5ECA1_CAEEL]
Publication Abstract from PubMed
Fusogens are membrane proteins that remodel lipid bilayers to facilitate membrane merging. Although several fusogen ectodomain structures have been solved, structural information on full-length, natively membrane-anchored fusogens is scarce. Here we present the electron cryo microscopy three-dimensional reconstruction of the Caenorhabditis elegans epithelial fusion failure 1 (EFF-1) protein natively anchored in cell-derived membrane vesicles. This reveals a membrane protruding, asymmetric, elongated monomer. Flexible fitting of a protomer of the EFF-1 crystal structure, which is homologous to viral class-II fusion proteins, shows that EFF-1 has a hairpin monomeric conformation before fusion. These structural insights, when combined with our observations of membrane-merging intermediates between vesicles, enable us to propose a model for EFF-1 mediated fusion. This process, involving identical proteins on both membranes to be fused, follows a mechanism that shares features of SNARE-mediated fusion while using the structural building blocks of the unilaterally acting class-II viral fusion proteins.
The full-length cell-cell fusogen EFF-1 is monomeric and upright on the membrane.,Zeev-Ben-Mordehai T, Vasishtan D, Siebert CA, Grunewald K Nat Commun. 2014 May 28;5:3912. doi: 10.1038/ncomms4912. PMID:24867324[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zeev-Ben-Mordehai T, Vasishtan D, Siebert CA, Grunewald K. The full-length cell-cell fusogen EFF-1 is monomeric and upright on the membrane. Nat Commun. 2014 May 28;5:3912. doi: 10.1038/ncomms4912. PMID:24867324 doi:http://dx.doi.org/10.1038/ncomms4912
