PMID:10893272

Citation	Rogalski, TM, Mullen, GP, Gilbert, MM, Williams, BD and Moerman, DG (2000) The UNC-112 gene in Caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane. J. Cell Biol. 150:253-64
Abstract	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 (alpha-integrin), and pat-3 (beta-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/beta-integrin in both adult and embryonic body wall muscle. We also have determined that UNC-112 is required to organize PAT-3/beta-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/beta-integrin. Furthermore, UNC-112 requires the presence of UNC-52/perlecan and PAT-3/beta-integrin, but not DEB-1/vinculin to become localized to the muscle cell membrane.
Links	PubMed PMC2185566
Keywords	Animals; Caenorhabditis elegans/genetics; Caenorhabditis elegans/metabolism; Caenorhabditis elegans Proteins; Cell Adhesion Molecules/genetics; Cell Adhesion Molecules/metabolism; Cell Membrane/metabolism; Extracellular Matrix/metabolism; Green Fluorescent Proteins; Helminth Proteins/genetics; Helminth Proteins/metabolism; Integrins/genetics; Integrins/metabolism; Luminescent Proteins/genetics; Membrane Proteins; Molecular Sequence Data; Muscles/cytology; Muscles/metabolism; Proteoglycans/genetics; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Sequence Analysis, DNA; Sequence Homology, Amino Acid
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