The short length of the extracellular domain of ζ is crucial for T cell antigen receptor function

Susana Minguet, Mahima Swamy, Wolfgang W.A. Schamel (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


The T cell antigen receptor (TCR-CD3) consists of the pMHC-binding TCRαβ heterodimer and the signalling dimers CD3δε, CD3γε and ζζ. The very short length of the extracellular domain (EC) of the ζ chain is preserved through evolution, however a rational explanation for this observation has not been elucidated. Here, we show that TCR-CD3 assembly is clearly defective when the murine ζ EC domain is artificially enlarged. Under these conditions, the TCR-CD3 complex is super-competent in transducing activation signals upon engagement. Furthermore, the TCR-CD3 complexes containing enlarged ζ EC domains underwent ligand-induced conformation changes with higher efficiency than TCR-CD3 complexes with an unmodified ζ EC domain. Together these data suggest that a short ζ EC domain is needed to correctly assemble the TCR-CD3 complex. When this domain is enlarged, the resulting TCR-CD3 complex is distorted leading to a hyperactive phenotype and enhanced T cell activation.

Original languageEnglish
Pages (from-to)195-202
Number of pages8
JournalImmunology Letters
Issue number2
Publication statusPublished - 15 Mar 2008


  • Activation
  • Conformational change
  • Signalling
  • T cell antigen receptor
  • TCR zeta chain
  • TCR-CD3 complex

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology


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