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Selected signalling proteins recruited to the T‐cell receptor–CD3 complex
Authors:Jatuporn Ngoenkam  Wolfgang W. Schamel  Sutatip Pongcharoen
Affiliation:1. Department of Microbiology and Parasitology, Faculty of Medical Science, Naresuan University, Phitsanulok, Thailand;2. Department of Immunology, Institute for Biology III, Faculty of Biology, University of Freiburg, Freiburg, Germany;3. BIOSS Centre for Biological Signalling Studies, University of Freiburg, Freiburg, Germany;4. Centre for Chronic Immunodeficiency (CCI), Medical Centre‐University of Freiburg, Faculty of Medicine, University of Freiburg, Freiburg, Germany;5. Centre of Excellence in Medical Biotechnology, Faculty of Medical Science, Naresuan University, Phitsanulok, Thailand;6. Centre of Excellence in Petroleum, Petrochemicals and Advanced Materials, Faculty of Science, Naresuan University, Phitsanulok, Thailand;7. Department of Medicine, Faculty of Medicine, Naresuan University, Phitsanulok, Thailand
Abstract:The T‐cell receptor (TCR)–CD3 complex, expressed on T cells, determines the outcome of a T‐cell response. It consists of the TCR‐αβ heterodimer and the non‐covalently associated signalling dimers of CD3εγ, CD3εδ and CD3ζζ. TCR‐αβ binds specifically to a cognate peptide antigen bound to an MHC molecule, whereas the CD3 subunits transmit the signal into the cytosol to activate signalling events. Recruitment of proteins to specialized localizations is one mechanism to regulate activation and termination of signalling. In the last 25 years a large number of signalling molecules recruited to the TCR–CD3 complex upon antigen binding to TCR‐αβ have been described. Here, we review knowledge about five of those interaction partners: Lck, ZAP‐70, Nck, WASP and Numb. Some of these proteins have been targeted in the development of immunomodulatory drugs aiming to treat patients with autoimmune diseases and organ transplants.
Keywords:protein–  protein interaction  signal transduction  T‐cell activation  T‐cell receptor–  CD3 complex
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