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MBC in Press, published online ahead of print January 19, 2005
Mol. Biol. Cell 10.1091/mbc.E04-06-0465

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Submitted on June 9, 2004
Revised on January 6, 2005
Accepted on January 10, 2005

Multiple Protein Interactions Involving Proposed Extracellular Loop Domains of the Tight Junction Protein Occludin

Asma Nusrat,*{dagger} G. Thomas Brown,* Jeffrey Tom,{ddagger} Alex Drake,{sect} Tam T.T. Bui,{sect} Cliff Quan,{ddagger} and Randall J. Mrsny||

*Department of Pathology, Emory University, Atlanta, GA 30322; {ddagger}Bioorganic Chemistry, Genentech, Inc., South San Francisco, CA 94080; {sect}School of Pharmacy, Kings College London, Strand, London WC2R 2LS, United Kingdom; ||Cardiff University, School of Pharmacy, Cardiff, Wales CF10 3XF

Monitoring Editor: Daniel Goodenough

Occludin is a tetraspan integral membrane protein in epithelial and endothelial tight junction (TJ) structures that is projected to have two extracellular loops. We have used peptides emulating central regions of human occludin’s first and second loops, termed O-A:101-121 and O-B:210-228, respectively, to examine potential molecular interactions between these two regions of occludin and other TJ proteins. A superficial biophysical assessment of A:101-121 and O-B:210-228 showed them to have dissimilar solution conformation characteristics. While O-A:101-121 failed to strongly interact with protein components of the human epithelial intestinal cell line T84, O-B:210-228 selectively associated with occludin, claudin-1 and the junctional adhesion molecule (JAM)-A. Further, the presence of O-B:210-228, but not O-A:101-121, impeded the recovery of functional TJ structures. A scrambled peptide sequences of O-B:210-228 failed to influence TJ assembly. These studies demonstrate distinct properties for these two extracellular segments of the occludin protein and provide an improved understanding of how specific domains of occludin may interact with proteins present at TJ structures.

{dagger}Corresponding author. E-mail: anusrat{at}emory.edu




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