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A more recent version of this article appeared on January 1, 2002
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Submitted on August 20, 2001
Revised on October 8, 2001
Accepted on October 17, 2001
1 M. Dyson Vision Research Institute, Weill Medical College of Cornell University, New York, New York
2 Department of Anatomy and Cell Biology, University of Iowa, Iowa City, Iowa, and Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California
3 Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California
4 Department of Cell and Developmental Biology, University of North Carolina, Chapel Hill, North Carolina
* Corresponding author. E-mail address: amuesch{at}mail.med.cornell.edu.
The Drosophila tumor suppressor protein (l(2)gl) is involved in the establishment of epithelial cell polarity during development. Recently, a yeast homologue 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. Here, we characterize a mammalian homologue of l(2)gl, called Mlgl, in the epithelial cell line MDCK. Consistent with a role in cell polarity, Mlgl re-distributes 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, since a recombinant phospho-mutant is distributed in a nonpolar fashion. Membrane bound Mlgl from MDCK cell lysates was co-immunoprecipitated with syntaxin 4, a component of the exocytic machinery at the basolateral membrane, but not with other plasma membrane 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.
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