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Identification and Functional Characterization of the -Chain Dimerization Motif for TCR Surface Expression¹

Basel Institute for Immunology, Basel, Switzerland

We recognized a common dimerization motif between the transmembrane (TM) domain of -chain family members and glycophorin A. We have shown that a glycine within the -dimerization motif is critical for -homodimerization and also for its association with the TCR/CD3 complex. Similarly, two residues within the CD3 TM domains have proven to be critical for their interaction with the -homodimer. A three-dimensional homology model of the -chain TM domain highlights potential residues preferentially involved either in the ₂-CD3 or ₂-TCRß association, confirming our experimental findings. These results indicate that, for symmetrical reasons, the -homodimer participates in the TCR/CD3 complex assembly by interacting with CD3 TM domains, thereby masking their degradation signals located in the cytoplasmic tails.

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