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Originally published In Press as doi:10.1074/jbc.M002450200 on July 7, 2000
J. Biol. Chem., Vol. 275, Issue 38, 29816-29822, September 22, 2000
The Coiled-coil Domain of Occludin Can Act to Organize Structural
and Functional Elements of the Epithelial Tight Junction*
Asma
Nusrat ,
Jason A.
Chen ,
Chris S.
Foley ,
Tony W.
Liang§,
Jeffrey
Tom¶,
M.
Cromwell ,
Cliff
Quan¶, and
Randall J.
Mrsny **
From the Epithelial Pathobiology Research Unit,
Department of Pathology and Laboratory Medicine, Emory University,
Atlanta, Georgia 30322 and the Departments of
§ Immunology, ¶ Bioorganic Chemistry, and
Pharmaceutical Research and Development, Genentech, Inc.,
South San Francisco, California 94080
Occludin is an integral membrane protein that has
been suggested to play a role in the organization and dynamic function
of the epithelial tight junction (TJ). A number of other proteins have
also been described to localize to the TJ. We have used a novel bait
peptide method to investigate potential protein-protein interactions of
the putative coiled-coil domain of occludin with some of these other TJ
proteins. A 27-amino acid peptide of the human occludin sequence was
synthesized, biotinylated at the N terminus, and modified to
contain a photoactive moiety at either its hydrophobic or hydrophilic
surface. These bait peptides were -helical in solution,
characteristic of coiled-coil structures. Photoactivation studies in
the presence and absence of control peptides were used to assess the
potential interactions in polarized sheets of a human intestinal cell
line T84. Although a large number of proteins associated with the TJ or
that are known to be involved in regulatory events of epithelial cells
failed to be specifically labeled, occludin itself, ZO-1, protein
kinase C- , c-Yes, the regulatory subunit of phosphatidylinositol
3-kinase, and the gap junction component connexin 26 were
specifically labeled. Our data demonstrate the potential of one
specific domain of occludin, contained within 27 amino acids, to
coordinate the binding of proteins that have been previously suggested
to modulate TJ structure and function.
*
This work was supported in part by National Institutes of
Health Grant R29-DK55679 (to A. N.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
**
To whom correspondence should be addressed: Drug Delivery/Biology
Group, Genentech, Inc., MS #6, 1 DNA Way, South San Francisco, CA
94080. Tel.: 650-225-2592; Fax: 650-225-4459; E-mail:
mrsny@gene.com.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.
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