The Cytoplasmic Domain of the Cell Adhesion Molecule Uvomorulin Associates With Three Independent Proteins Structurally Related in Different Species

摘要: Abstract Uvomorulin belongs to the group of Ca2+-dependent cell adhesion molecules, which are integral membrane proteins with several structural features in common. In particular, cytoplasmic part these is highly conserved different species, suggesting a common biological function. To test this assumption we transfected uvomorulin full-length cDNA into uvomorulin-negative mouse NIH 3T3 and L cells. Immunoprecipitations anti-uvomorulin antibodies detected, addition uvomorulin, three independent 102, 88 80 kd host origin form complexes uvomorulin. Using constructs coding for or extracellular deletions it shown that complex domain Peptide pattern analysis revealed identical When was introduced lines from other such as human HeLa avian fibroblasts, expressed also associated endogenous and, moreover, each showed similarities respective molecule. A panel specific known mol. wts similar those did not react any described components. This suggests constitute new propose nomenclature catenin alpha, beta gamma respectively. The characterization provides first molecular basis possible anchorage cytoskeleton.