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Recruitment of Nck by CD3 epsilon reveals a ligand-induced conformational change essential for T cell receptor signaling and synapse formation.

How membrane receptors initiate signal transduction upon ligand binding is a matter of intense scrutiny. The T cell receptor complex (TCR-CD3) is composed of TCR alpha/beta ligand binding subunits bound to the CD3 subunits responsible for signal transduction. Although it has long been speculated that TCR-CD3 may undergo a conformational change, confirmation is still lacking. We present strong evidence that ligand engagement of TCR-CD3 induces a conformational change that exposes a proline-rich sequence in CD3 epsilon and results in recruitment of the adaptor protein Nck. This occurs earlier than and independently of tyrosine kinase activation. Finally, by interfering with Nck-CD3 epsilon association in vivo, we demonstrate that TCR-CD3 recruitment of Nck is critical for maturation of the immune synapse and for T cell activation.

Pubmed ID: 12110186


  • Gil D
  • Schamel WW
  • Montoya M
  • Sánchez-Madrid F
  • Alarcón B



Publication Data

June 28, 2002

Associated Grants


Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Sequence
  • Animals
  • Antigen-Presenting Cells
  • Antigens, CD3
  • Binding Sites
  • Humans
  • Jurkat Cells
  • Ligands
  • Lymphocyte Activation
  • Mice
  • Molecular Sequence Data
  • Oncogene Proteins
  • Phosphorylation
  • Phosphotyrosine
  • Proline
  • Protein Binding
  • Receptors, Antigen, T-Cell
  • Signal Transduction
  • T-Lymphocytes
  • src Homology Domains