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Papers In Press, published online ahead of print December 31, 2003
Molecular Immunology and Allergy, Graduate School of Medicine, Kyoto University, Kyoto, Kyoto 606-8501
Corresponding Author: tkinashi{at}mfour.med.kyoto-u.ac.jp
The small GTPase, Rap1, is a potent activator of leukocyte integrins and enhances the adhesive activity of LFA-1 when stimulated by the T cell receptor (TCR) or chemokines. However, the mechanism by which Rap1 is activated remains unclear. Here, we demonstrate that PLC-g1 plays a critical role in the signaling pathway leading to Rap1 activation triggered by the TCR. In Jurkat T cells, TCR crosslinking triggered persistent Rap1 activation, and SDF-1 (CXCL12) activated Rap1 transiently. A phospholipase C inhibitor, U73122, abrogated Rap1 activation triggered by both the TCR and SDF-1 (CXCL12). PLC-g1-deficient Jurkat T cells showed a marked reduction of TCR-triggered Rap1 activation and adhesion to ICAM-1 mediated by LFA-1. In contrast, SDF-1 triggered Rap1 activation and adhesion were not affected in these cells. Transfection of these cells with an expression plasmid encoding PLC-g1 restored Rap1 activation by the TCR and the ability to adhere to ICAM-1, accompanied by polarized LFA-1 surface clustering colocalized with RAPL. Furthermore, when expressed in Jurkat cells, CalDAG-GEFI, a calcium and diacylglycerol-responsive Rap1 exchange factor, associated with Rap1, and resulted in enhanced Rap1 activation and adhesion triggered by the TCR. Our results demonstrate that TCR activation of Rap1 depends on PLC-g1. This activity is likely to be mediated by CalDAG-GEFI, which is required to activate LFA-1.
J. Biol. Chem, 10.1074/jbc.M310717200
Submitted on September 29, 2003
Revised on December 28, 2003
Accepted on December 31, 2003
Rap1-mediated LFA-1 activation by the T cell antigen receptor is dependent on PLC-gamma1
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