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Immunol Lett. 2014 Sep;161(1):113-7. doi: 10.1016/j.imlet.2014.05.007. Epub 2014 May 27.

Crammed signaling motifs in the T-cell receptor.

Author information

1
TCR Signal Transduction Laboratory, Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas, 28049 Madrid, Spain.
2
Bioinformatics Unit, Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas, 28049 Madrid, Spain.
3
TCR Signal Transduction Laboratory, Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas, 28049 Madrid, Spain. Electronic address: balarcon@cbm.uam.es.

Abstract

Although the T cell antigen receptor (TCR) is long known to contain multiple signaling subunits (CD3γ, CD3δ, CD3ɛ and CD3ζ), their role in signal transduction is still not well understood. The presence of at least one immunoreceptor tyrosine-based activation motif (ITAM) in each CD3 subunit has led to the idea that the multiplication of such elements essentially serves to amplify signals. However, the evolutionary conservation of non-ITAM sequences suggests that each CD3 subunit is likely to have specific non-redundant roles at some stage of development or in mature T cell function. The CD3ɛ subunit is paradigmatic because in a relatively short cytoplasmic sequence (∼55 amino acids) it contains several docking sites for proteins involved in intracellular trafficking and signaling, proteins whose relevance in T cell activation is slowly starting to be revealed. In this review we will summarize our current knowledge on the signaling effectors that bind directly to the TCR and we will propose a hierarchy in their response to TCR triggering.

KEYWORDS:

CD3epsilon; TCR signaling

PMID:
24877875
DOI:
10.1016/j.imlet.2014.05.007
[Indexed for MEDLINE]

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