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The Journal of Immunology, 2002, 168: 3740-3746.
Copyright © 2002 by The American Association of Immunologists

Polar Redistribution of the Sialoglycoprotein CD43: Implications for T Cell Function1

Nigel D. L. Savage*, Stephanie L. Kimzey*, Shannon K. Bromley{dagger}, Kenneth G. Johnson{dagger}, Michael L. Dustin{ddagger} and Jonathan M. Green2,*,{dagger}

Departments of * Medicine and {dagger} Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110; and {ddagger} Program in Molecular Pathogenesis, Skirball Institute of Biomolecular Medicine, New York, NY 10016

Contact between T cells and APCs results in the orchestrated segregation of molecules at the cell-cell interface and formation of a specialized structure termed the immunological synapse. This model predicts the topological seclusion of large molecules such as CD43 from the site of closest contact between the T cell and APC, allowing for the close apposition of cell membranes and effective TCR engagement. Similarly, during T cell migration segregation of CD43 to the uropod is thought to aid integrin adhesion at the leading edge of the cell by removing steric hindrance. We show in this work that CD43 distribution on T cells is regulated by a membrane proximal ezrin binding site and that failure to displace CD43 from the immunological synapse has no inhibitory effects on primary T cell activation. We also report that CD43 expression at the contact zone between T cells and matrix does not negatively regulate motility but may regulate LFA-1 de-adhesion. These results suggest that the steric barrier model of CD43 is inadequate and that alternative mechanisms account for the negative regulatory properties of CD43.




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