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- Title
The F-BAR domain of SRGP-1 facilitates cell-cell adhesion during C. elegans morphogenesis.
- Authors
Zaidel-Bar, Ronen; Joyce, Michael J.; Lynch, Allison M.; Witte, Kristen; Audhya, Anjon; Hardin, Jeff
- Abstract
Robust cell-cell adhesion is critical for tissue integrity and morphogenesis, yet little is known about the molecular mechanisms controlling cell-cell junction architecture and strength. We discovered that SRGP-1 is a novel component of cell-cell junctions in Caenorhabditis elegans, localizing via its F-BAR (Bin1, Amphiphysin, and RVS167) domain and a flanking 200-amino acid sequence. SRGP-1 activity promotes an increase in membrane dynamics at nascent cell-cell contacts and the rapid formation of new junctions; in addition, srgp-1 loss of function is lethal in embryos with compromised cadherin-catenin complexes. Conversely, excess SRGP-1 activity leads to outward bending and projections of junctions. The C-terminal half of SRGP-1 interacts with the N-terminal F-BAR domain and negatively regulates its activity. Significantly, in vivo structure-function analysis establishes a role for the F-BAR domain in promoting rapid and robust cell adhesion during embryonic closure events, independent of the Rho guanosine triphosphatase-activating protein domain. These studies establish a new role for this conserved protein family in modulating cell-cell adhesion.
- Subjects
CELL adhesion; CELL communication; CAENORHABDITIS elegans; AMINO acid sequence; GUANOSINE triphosphatase
- Publication
Journal of Cell Biology, 2010, Vol 191, Issue 4, p761
- ISSN
0021-9525
- Publication type
Article
- DOI
10.1083/jcb.201005082