mLin-7 is localized to the basolateral surface of renal epithelia via its NH(2) terminus

Am J Physiol Renal Physiol. 2000 Mar;278(3):F464-75. doi: 10.1152/ajprenal.2000.278.3.F464.

Abstract

In Caenorhabditis elegans, the basolateral localization of the Let-23 growth factor receptor tyrosine kinase requires the expression of three genes: lin-2, lin-7, and lin-10. Mammalian homologs of these three genes have been identified, and a complex of their protein products exists in mammalian neurons. In this paper, we examine the interaction of these mammalian proteins in renal epithelia. Coprecipitation experiments demonstrated that mLin-2/CASK binds to mLin-7, and immunofluorescent labeling showed that these proteins colocalized at the basolateral surface of Madin-Darby canine kidney cells and renal epithelia. Although labeling intensity varied markedly among different renal epithelial cells, those cells strongly expressing mLin-7 also showed intense mLin-2/CASK labeling. We have also demonstrated that mLin-2/CASK binding requires amino acids 12-32 of mLin-7 and have shown that this region of mLin-7 is also necessary for the targeting of mLin-7 to the basolateral surface. Furthermore, the overexpression of mLin-2/CASK mutants in Madin-Darby canine kidney cells caused endogenous mLin-7 to mislocalize. In summary, the NH(2) terminus of mLin-7 is crucial for its basolateral localization, likely through its interaction with mLin-2/CASK.

Publication types

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

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • Cell Line
  • Dogs
  • Epithelium / metabolism
  • Fluorescent Antibody Technique
  • Humans
  • Intracellular Membranes / metabolism
  • Kidney / cytology
  • Kidney / metabolism*
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Rats
  • Rats, Sprague-Dawley
  • Tissue Distribution
  • Vesicular Transport Proteins

Substances

  • Adaptor Proteins, Signal Transducing
  • LIN-7 protein, mammalian
  • LIN7A protein, human
  • LIN7C protein, human
  • Membrane Proteins
  • Vesicular Transport Proteins