Actin reorganization at the immunological synapse is required for the amplification and generation of a functional immune response. Using small interfering RNA, we show here that dynamin 2 (Dyn2), a large GTPase involved in receptor-mediated internalization, did not alter antibody-mediated T cell receptor internalization but considerably affected T cell receptor-stimulated T cell activation by regulating multiple biochemical signaling pathways and the accumulation of F-actin at the immunological synapse. Moreover, Dyn2 interacted directly with the Rho family guanine nucleotide exchange factor Vav1, and this interaction was required for T cell activation. These data identify a functionally important interaction between Dyn2 and Vav1 that regulates actin reorganization and multiple signaling pathways in T lymphocytes.
Pubmed ID: 15696170 RIS Download
Mesh terms: Actins | Base Sequence | Biopolymers | Cell Cycle Proteins | Dynamin II | Humans | Lymphocyte Activation | Membrane Proteins | Molecular Sequence Data | Proto-Oncogene Proteins | Proto-Oncogene Proteins c-vav | Receptors, Antigen, T-Cell | Signal Transduction | T-Lymphocytes
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