The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells

Cell. 1998 Sep 18;94(6):761-71. doi: 10.1016/s0092-8674(00)81735-3.


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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Caenorhabditis elegans / genetics*
  • Caenorhabditis elegans Proteins*
  • Drosophila
  • Epithelial Cells / chemistry
  • Epithelial Cells / enzymology
  • ErbB Receptors / chemistry
  • ErbB Receptors / metabolism*
  • Female
  • Gene Expression Regulation, Enzymologic
  • Helminth Proteins / chemistry
  • Helminth Proteins / isolation & purification
  • Helminth Proteins / metabolism*
  • Mammals
  • Membrane Proteins / chemistry
  • Membrane Proteins / isolation & purification
  • Membrane Proteins / metabolism*
  • Multienzyme Complexes / metabolism
  • Mutation / physiology
  • Precipitin Tests
  • Protein Binding / physiology
  • Protein Structure, Tertiary
  • Proteins*
  • Signal Transduction / physiology
  • Substrate Specificity
  • Vulva / chemistry
  • Vulva / cytology
  • Vulva / enzymology*
  • Yeasts / enzymology


  • Caenorhabditis elegans Proteins
  • Helminth Proteins
  • LIN-7 protein, C elegans
  • Lin-2 protein, C elegans
  • Membrane Proteins
  • Multienzyme Complexes
  • Proteins
  • lin-10 protein, C elegans
  • ErbB Receptors
  • let-23 protein, C elegans