期刊
JOURNAL OF IMMUNOLOGY
卷 182, 期 7, 页码 3974-3978出版社
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.0804172
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资金
- Institut National de la Sanre et de la Recherche Medicale
- Institut National du Cancer [PL-06026]
- Association pour la Recherche stir le Cancer [4202]
- Agence Nationale de Recherches Programme Blanc [0065-01]
- Fund for Scientific Research-Flanders
- Belgian Federation against Cancer
- Concerted Actions Program
- Research Fund of the Katholieke Universiteit Leuven
Downstream of tyrosine kinase (Dok) proteins Dok-1 and Dok-2 are involved in T cell homeostasis maintenance. Dok protein tyrosine phosphorylation plays a key role in establishing negative feedback loops of T cell signaling. These structurally related adapter molecules contain a pleckstrin homology (PH) domain generally acting as a lipid/protein-interacting module. We show that the presence of this PH domain is necessary for the tyrosine phosphorylation of Dok proteins and their negative functions in T cells. We find that Dok-1/Dok-2 PH domains bind in vitro to the rare phosphoinositide species, phosphatidylinositol 5-phosphate (PtdIns5P). Dok tyrosine phosphorylation correlates with PtdIns5P production in T cells upon TCR triggering. Furthermore, we demonstrate that PtdIns5P increase regulates Dok tyrosine phosphorylation in vivo. Together, our data identify a novel lipid mediator in T cell signaling and suggest that PH-PtdIns5P interactions regulate T cell responses. The Journal of Immunology, 2009, 182: 3974-3978.
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