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J Cell Biol. 2010 Nov 15;191(4):761-9. doi: 10.1083/jcb.201005082. Epub 2010 Nov 8.

The F-BAR domain of SRGP-1 facilitates cell-cell adhesion during C. elegans morphogenesis.

Author information

1
Department of Zoology, University of Wisconsin-Madison, Madison, WI 53706, USA. biezbr@nus.edu.sg

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.

PMID:
21059849
PMCID:
PMC2983056
DOI:
10.1083/jcb.201005082
[Indexed for MEDLINE]
Free PMC Article

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