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Recruitment of CD2 to the immunological synapse in response to antigen is dependent on its proline-rich cytoplasmic tail. A peptide from this region (CD2:322-339) isolated CMS (human CD2AP); a related protein, CIN85; and the actin capping protein, CAPZ from a T cell line. In BIAcore analyses, the N-terminal SH3 domains of CMS and CIN85 bound CD2:322-339 with similar dissociation constants (KD = approximately 100 microm). CAPZ bound the C-terminal half of CMS and CIN85. Direct binding between CMS/CIN85 and CAPZ provides a link with the actin cytoskeleton. Overexpression of a fragment from the C-terminal half or the N-terminal SH3 domain of CD2AP in a mouse T cell hybridoma resulted in enhanced interleukin-2 production and reduced T cell receptor down-modulation in response to antigen. These adaptor proteins are important in T cell signaling consistent with a role for CD2 in regulating pathways initiated by CMS/CIN85 and CAPZ.

Original publication




Journal article


J Biol Chem

Publication Date





22396 - 22403


Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Antigens, CD, Binding Sites, CD2 Antigens, CapZ Actin Capping Protein, Carrier Proteins, Cytoskeletal Proteins, Humans, Jurkat Cells, Kinetics, Microfilament Proteins, Molecular Sequence Data, Muscle Proteins, Peptide Fragments, Signal Transduction, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, T-Lymphocytes, src Homology Domains