Localization of a 215-kDa tyrosine-phosphorylated protein that cross-reacts with tensin antibodies. |
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Authors: | S M Bockholt C A Otey J R Glenney K Burridge |
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Affiliation: | Department of Cell Biology and Anatomy, University of North Carolina, Chapel Hill 27599-7090. |
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Abstract: | Tyrosine phosphorylation of cytoskeletal proteins at adhesive junctions has been speculated to play a role in the regulation of cell signaling at these sites. Previously, monoclonal antibodies were generated against phosphotyrosine-containing proteins from Rous sarcoma virus-transformed chick embryo fibroblasts, resulting in two antibodies which recognized antigens of 76 and 215 kDa that localized to focal contacts. We have now localized the 215-kDa antigen to a number of adhesive junctions in vivo, including the zonula adherens, intercalated discs, and myotendinous and neuromuscular junctions. In sections of skeletal muscle and in isolated myofibrils, the 215-kDa protein was localized to the I-band. By immunoprecipitation and immunoblot analysis, we determined that the 215-kDa antigen cross-reacts with a polyclonal anti-tensin antibody. |
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