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Vol. 13, Issue 1, 158-168, January 2002
§
*M. Dyson Vision Research Institute, Weill Medical College of
Cornell University, New York, New York 10021; The Drosophila tumor suppressor protein lethal (2) giant
larvae [l(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 l(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.
Department
of Anatomy and Cell Biology, University of Iowa, Iowa City, Iowa 52242;
§Department of Molecular and Cellular Physiology, Stanford
University School of Medicine, Stanford, California 94305; and
Department of Cell and Developmental Biology, University
of North Carolina, Chapel Hill, North Carolina 27599
Corresponding author. E-mail addresses:
amuesch{at}mail.med.cornell.edu or pjbrennw{at}med.unc.edu.
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