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Phosphoinositide 3–kinase γ participates in T cell receptor–induced T cell activation

  • Alcázar, Isabela Department of Immunology and Oncology, Centro Nacional de Biotecnología (CNB)/Consejo Superior de Investigaciones Cientificas, Madrid 28049, Spain
  • Marqués, Miriam Department of Immunology and Oncology, Centro Nacional de Biotecnología (CNB)/Consejo Superior de Investigaciones Cientificas, Madrid 28049, Spain
  • Kumar, Amit Department of Immunology and Oncology, Centro Nacional de Biotecnología (CNB)/Consejo Superior de Investigaciones Cientificas, Madrid 28049, Spain
  • Hirsch, Emilio Department of Genetics Biology and Biochemistry, Center for Molecular Biotechnology, University of Torino, 10126 Turin, Italy
  • Wymann, Matthias Department of Clinical and Biological Sciences, Institute of Biochemistry and Genetics, University of Basel, 4058 Basel, Switzerland
  • Carrera, Ana C. Department of Immunology and Oncology, Centro Nacional de Biotecnología (CNB)/Consejo Superior de Investigaciones Cientificas, Madrid 28049, Spain
  • Barber, Domingo F. Department of Immunology and Oncology, Centro Nacional de Biotecnología (CNB)/Consejo Superior de Investigaciones Cientificas, Madrid 28049, Spain
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  • 2007-11-12
Veröffentlicht in:
  • Journal of Experimental Medicine. - Rockefeller University Press. - 2007, Bd. 204, Nr. 12, S. 2977-2987
Immunology
Immunology and Allergy
Englisch Class I phosphoinositide 3–kinases (PI3Ks) constitute a family of enzymes that generates 3-phosphorylated polyphosphoinositides at the cell membrane after stimulation of protein tyrosine (Tyr) kinase–associated receptors or G protein–coupled receptors (GPCRs). The class I PI3Ks are divided into two types: class IA p85/p110 heterodimers, which are activated by Tyr kinases, and the class IB p110γ isoform, which is activated by GPCR. Although the T cell receptor (TCR) is a protein Tyr kinase–associated receptor, p110γ deletion affects TCR-induced T cell stimulation. We examined whether the TCR activates p110γ, as well as the consequences of interfering with p110γ expression or function for T cell activation. We found that after TCR ligation, p110γ interacts with Gαq/11, lymphocyte-specific Tyr kinase, and ζ-associated protein. TCR stimulation activates p110γ, which affects 3-phosphorylated polyphosphoinositide levels at the immunological synapse. We show that TCR-stimulated p110γ controls RAS-related C3 botulinum substrate 1 activity, F-actin polarization, and the interaction between T cells and antigen-presenting cells, illustrating a crucial role for p110γ in TCR-induced T cell activation.
Sprache
  • Englisch
Open Access Status
bronze
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https://sonar.ch/global/documents/207236
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