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Original Article |
Correspondence to: Donald G. Moerman, Department of Zoology, University of British Columbia, 6270 University Blvd., Vancouver, British Columbia V6T 1Z4, Canada. Tel:(604) 822-3365 Fax:(604) 822-2416 E-mail:moerman{at}zoology.ubc.ca.
Embryos homozygous for mutations in the unc-52, pat-2, pat-3, and unc-112 genes of C. elegans exhibit a similar Pat phenotype. Myosin and actin are not organized into sarcomeres in the body wall muscle cells of these mutants, and dense body and M-line components fail to assemble. The unc-52 (perlecan), pat-2 (
-integrin), and pat-3 (ß-integrin) genes encode ECM or transmembrane proteins found at the cell–matrix adhesion sites of both dense bodies and M-lines. This study describes the identification of the unc-112 gene product, a novel, membrane-associated, intracellular protein that colocalizes with integrin at cell–matrix adhesion complexes. The 720–amino acid UNC-112 protein is homologous to Mig-2, a human protein of unknown function. These two proteins share a region of homology with talin and members of the FERM superfamily of proteins.
We have determined that a functional UNC-112::GFP fusion protein colocalizes with PAT-3/ß-integrin in both adult and embryonic body wall muscle. We also have determined that UNC-112 is required to organize PAT-3/ß-integrin after it is integrated into the basal cell membrane, but is not required to organize UNC-52/perlecan in the basement membrane, nor for DEB-1/vinculin to localize with PAT-3/ß-integrin. Furthermore, UNC-112 requires the presence of UNC-52/perlecan and PAT-3/ß-integrin, but not DEB-1/vinculin to become localized to the muscle cell membrane.
Key Words: UNC-112, integrin, muscle development, adhesion complex, FERM superfamily
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