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Published online 10 July 2000. doi:10.1083/jcb.150.1.253
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© The Rockefeller University Press, 0021-9525/2000//253 $5.00
The Journal of Cell Biology, Volume 150, Number 1, , 2000 253-264

Original Article

The UNC-112 Gene in Caenorhabditis elegansEncodes a Novel Component of Cell–Matrix Adhesion Structures Required for Integrin Localization in the Muscle Cell Membrane



Teresa M. Rogalskia, Gregory P. Mullena, Mary M. Gilberta, Benjamin D. Williamsb, and Donald G. Moermana

a Department of Zoology, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada
b Department of Cell and Structural Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801
Department of Zoology, University of British Columbia, 6270 University Blvd., Vancouver, British Columbia V6T 1Z4, Canada.(604) 822-2416(604) 822-3365

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 ({alpha}-integrin), and pat-3 (β-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/β-integrin in both adult and embryonic body wall muscle. We also have determined that UNC-112 is required to organize PAT-3/β-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/β-integrin. Furthermore, UNC-112 requires the presence of UNC-52/perlecan and PAT-3/β-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

© 2000 The Rockefeller University Press

Abbreviations used in this paper: aa, amino acids; ECM, extracellular matrix; FAs, focal adhesion plaques; GFP, green fluorescent protein; ORF(s), open reading frame(s); Pat, paralyzed, arrested elongation at twofold.


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