The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells.
In C. elegans, the LET-23 receptor tyrosine kinase is localized to the basolateral membranes of polarized vulval epithelial cells. lin-2, lin-7, and lin-10 are required for basolateral localization of LET-23, since LET-23 is mislocalized to the apical membrane in lin-2, lin-7, and lin-10 mutants. Yeast two-hybrid, in vitro binding, and ... in vivo coimmunoprecipitation experiments show that LIN-2, LIN-7, and LIN-10 form a protein complex. Furthermore, compensatory mutations in lin-7 and let-23 exhibit allele-specific suppression of apical mislocalization and signaling-defective phenotypes. These results present a mechanism for basolateral localization of LET-23 receptor tyrosine kinase by direct binding to the LIN-2/LIN-7/LIN-10 complex. Each of the binding interactions within this complex is conserved, suggesting that this complex may also mediate basolateral localization in mammals.
Mesh Terms:
Animals, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Drosophila, Epithelial Cells, Female, Gene Expression Regulation, Enzymologic, Helminth Proteins, Mammals, Membrane Proteins, Multienzyme Complexes, Mutation, Precipitin Tests, Protein Binding, Protein Structure, Tertiary, Proteins, Receptor, Epidermal Growth Factor, Signal Transduction, Substrate Specificity, Vulva, Yeasts
Animals, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Drosophila, Epithelial Cells, Female, Gene Expression Regulation, Enzymologic, Helminth Proteins, Mammals, Membrane Proteins, Multienzyme Complexes, Mutation, Precipitin Tests, Protein Binding, Protein Structure, Tertiary, Proteins, Receptor, Epidermal Growth Factor, Signal Transduction, Substrate Specificity, Vulva, Yeasts
Cell
Date: Sep. 18, 1998
PubMed ID: 9753323
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