Journal
JOURNAL OF CELL BIOLOGY
Volume 191, Issue 4, Pages 761-769Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201005082
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Funding
- National Institutes of Health [GM078747, GM058038, GM088151]
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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 (Bin 1, 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
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