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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Williams, B. D. Rogalski, T. M. Gilbert, M. M. Mullen, G. P. Moerman, D. G. |
| Description | Author Affiliation: Rogalski TM ( Department of Zoology, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada.) |
| 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 (α-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. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 1 |
| Volume Number | 150 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 2000-07-10 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Caenorhabditis Elegans Proteins Caenorhabditis Elegans Genetics Cell Adhesion Molecules Extracellular Matrix Metabolism Integrins Membrane Proteins Muscles Animals Cell Membrane Green Fluorescent Proteins Helminth Proteins Luminescent Proteins Molecular Sequence Data Cytology Proteoglycans Recombinant Fusion Proteins Sequence Analysis, DNA Sequence Homology, Amino Acid Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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