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Recognition of antigen by T cells requires the formation of a specialized junction between the T cell and the antigen-presenting cell. This junction is generated by the recruitment and the exclusion of specific proteins from the contact area. The mechanisms that regulate these events are unknown. Here we demonstrate that ligand engagement of the adhesion molecule, CD2, initiates a process of protein segregation, CD2 clustering, and cytoskeletal polarization. Although protein segregation was not dependent on the cytoplasmic domain of CD2, CD2 clustering and cytoskeletal polarization required an interaction of the CD2 cytoplasmic domain with a novel SH3-containing protein. This novel protein, called CD2AP, is likely to facilitate receptor patterning in the contact area by linking specific adhesion receptors to the cytoskeleton.

Original publication

DOI

10.1016/s0092-8674(00)81608-6

Type

Journal article

Journal

Cell

Publication Date

09/1998

Volume

94

Pages

667 - 677

Addresses

Department of Pathology and Center for Immunology, Washington University School of Medicine, Saint Louis, Missouri 63110, USA.

Keywords

T-Lymphocytes, Cytoplasm, Cytoskeleton, Animals, Humans, Mice, Adaptor Proteins, Signal Transducing, Proteins, Cytoskeletal Proteins, Receptors, Cell Surface, Receptors, Cytoplasmic and Nuclear, Antigens, CD2, Ligands, Cell Communication, Cell Polarity, Receptor Aggregation, Antigen Presentation, Amino Acid Sequence, src Homology Domains, Substrate Specificity, Molecular Sequence Data