Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells

Anne Müsch, David Cohen, Charles Yeaman, W. James Nelson, Enrique Rodriguez-Boulan, Patrick J. Brennwald

Research output: Contribution to journalArticle

155 Scopus citations

Abstract

The Drosophila tumor suppressor protein lethal (2) giant larvae [1(2)gl] is involved in the establishment of epithelial cell polarity during development. Recently, a yeast homolog of the protein has been shown to interact with components of the post-Golgi exocytic machinery and to regulate a late step in protein secretion. Herein, we characterize a mammalian homolog of 1(2)gl, called Mlgl, in the epithelial cell line Madin-Darby canine kidney (MDCK). Consistent with a role in cell polarity, Mlgl redistributes from a cytoplasmic localization to the lateral membrane after contact-naive MDCK cells make cell-cell contacts and establish a polarized phenotype. Phosphorylation within a highly conserved region of Mlgl is required to restrict the protein to the lateral domain, because a recombinant phospho-mutant is distributed in a nonpolar manner. Membrane-bound Mlgl from MDCK cell lysates was coimmunoprecipitated with syntaxin 4, a component of the exocytic machinery at the basolateral membrane, but not with other plasma membrane soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) proteins that are either absent from or not restricted to the basolateral membrane domain. These data suggest that Mlgl contributes to apico-basolateral polarity by regulating basolateral exocytosis.

Original languageEnglish (US)
Pages (from-to)158-168
Number of pages11
JournalMolecular biology of the cell
Volume13
Issue number1
DOIs
StatePublished - Feb 9 2002
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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