International Immunology Advance Access originally published online on January 12, 2007
International Immunology 2007 19(3):239-248; doi:10.1093/intimm/dxl141
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CD2 and TCR synergize for the activation of phospholipase C
1/calcium pathway at the immunological synapse
1 INSERM U563, Lymphocyte Interaction Group, Institut Claude de Préval, CHU Purpan, 31059 Toulouse, France
2 Faculty of Life-Sciences, University Toulouse III, Toulouse, France
3 Present address: Cancer Research UK, London Research Institute, London, WC2A 3PX, UK
4 Present address: School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, UK
Correspondence to: S. Valitutti; E-mail: svalitu{at}toulouse.inserm.fr
Upon conjugation with cognate antigen-presenting cells (APCs), T lymphocytes undergo a sustained [Ca2+]i increase resulting from the engagement of TCR and of accessory molecules with ligands expressed on the surface of APCs. We investigated the contribution of the accessory molecule CD2 to the activation of phospholipase C
1 (PLC
1)/calcium pathway in antigen-stimulated T cells. We show that CD2 binding with its ligand CD58 expressed on the surface of APCs augments and sustains antigen-induced [Ca2+]i increase in individual T cells interacting with APCs. We also show that in conditions in which CD2CD58 interaction is impeded, the recruitment of PLC
1 to the immunological synapse (IS) is reduced. Interestingly, in these conditions PLC
1 phosphorylation in the regulatory tyrosine 783 is also defective. Our results indicate that TCR- and CD2-derived signals converge for the recruitment and activation of PLC
1 at the IS and shed new light on the accessory function of CD2 in T cell activation by specific antigen.
Keywords: antigen-presenting cells, CD58, signal transduction, T cell activation
Transmitting editor: J. Borst
Received 15 June 2006, accepted 13 December 2006.
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