Journal
CELL
Volume 157, Issue 2, Pages 407-419Publisher
CELL PRESS
DOI: 10.1016/j.cell.2014.02.020
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Funding
- French Agence Nationale pour la Recherche [ANR-2010-BLAN-1211 01]
- Institut Pasteur
- CNRS
- Merck-Serono
- ERC [268843]
- Israel Science Foundation (ISF) [1542/07, 826/08]
- European Research Council (ERC) [268843] Funding Source: European Research Council (ERC)
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Cell-cell fusion proteins are essential in development. Here we show that the C. elegans cell-cell fusion protein EFF-1 is structurally homologous to viral class II fusion proteins. The 2.6 angstrom crystal structure of the EFF-1 trimer displays the same 3D fold and quaternary conformation of postfusion class II viral fusion proteins, although it lacks a nonpolar fusion loop, indicating that it does not insert into the target membrane. EFF-1 was previously shown to be required in both cells for fusion, and we show that blocking EFF-1 trimerization blocks the fusion reaction. Together, these data suggest that whereas membrane fusion driven by viral proteins entails leveraging of a nonpolar loop, EFF-1-driven fusion of cells entails trans-trimerization such that transmembrane segments anchored in the two opposing membranes are brought into contact at the tip of the EFF-1 trimer to then, analogous to SNARE-mediated vesicle fusion, zip the two membranes into one.
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