We recognized a common dimerization motif between the transmembrane (TM) domain of ζ-chain family members and glycophorin A. We have shown that a glycine within the ζ-dimerization motif is critical for ζ-homodimerization and also for its association with the TCR/CD3 complex. Similarly, two residues within the CD3δγ TM domains have proven to be critical for their interaction with the ζ-homodimer. A three-dimensional homology model of the ζ-chain TM domain highlights potential residues preferentially involved either in the ζ2-CD3 or ζ2-TCRαβ association, confirming our experimental findings. These results indicate that, for symmetrical reasons, the ζ-homodimer participates in the TCR/CD3 complex assembly by interacting with CD3γδ TM domains, thereby masking their degradation signals located in the cytoplasmic tails.
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Bolliger et al. (1999) studied this question.