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Tec Kinase Migrates to the T Cell-APC Interface Independently of Its Pleckstrin Homology Domain¹

Fabien Garçon^*, Georges Bismuth, Daniel Isnardon, Daniel Olive^* and Jacques A. Nunès^2,*

^* Institut National de la Santé et de la Recherche Médicale Unité Mixte de Recherche 599, Institut du Cancer de Marseille, Equipe labellisée 2001 par la Ligue Nationale contre le Cancer, Institut Fédératif de Recherche 137, Université de la Méditerranée, Marseille, France; Département de Biologie Cellulaire, Institut Cochin, Institut National de la Santé et de la Recherche Médicale Unité 537, Centre National de la Recherche Scientifique Unité Mixte de Recherche 7627, Université René Descartes, Paris, France; and Atelier de Bio-Imagerie, Institut Paoli-Calmettes, Marseille, France

Tec is the prototypical member of the Tec tyrosine kinases family, which plays an important role in T cell signaling. We show in this study that Tec translocates to the immunological synapse when a T cell contacts a dendritic cell. Surprisingly, the presence of the pleckstrin homology (PH) domain of Tec is not required for this accumulation, and despite a strong activation of 3'-phosphorylated phosphoinositide lipids synthesis during the synapse formation, the Tec PH domain is not redistributed to the T cell plasma membrane. In contrast, we demonstrate that an active Src homology 3 domain is absolutely required, underlining the essential role played by this part of the molecule in the recruitment and/or stabilization of Tec at the immunological synapse. Our results nevertheless suggest that the PH domain controls the kinase activity of the molecule in vivo. We finally demonstrate that the two domains are necessary to trigger transcriptional events following Ag presentation. These data support a model in which the plasma membrane recruitment of the PH-containing protein Tec is not dependent on the production of 3'-phosphorylated phosphoinositide lipids by the PI3K, but rather on an intact Src homology 3 domain.

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