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The immunological synapse (IS) serves a dual role for sustained T cell receptor (TCR) signaling and for TCR downregulation. TC21 (Rras2) is a RRas subfamily GTPase that constitutively associates with the TCR and is implicated in tonic TCR signaling by activating phosphatidylinositol 3-kinase. In this study, we demonstrate that TC21 both cotranslocates with the TCR to the IS and is necessary for TCR internalization from the IS through a mechanism dependent on RhoG, a small GTPase previously associated with phagocytosis. Indeed, we found that the TCR triggers T cells to phagocytose 1-6 μm beads through a TC21- and RhoG-dependent pathway. We further show that TC21 and RhoG are necessary for the TCR-promoted uptake of major histocompatibility complex (MHC) from antigen-presenting cells. Therefore, TC21 and RhoG dependence underlie the existence of a common phagocytic mechanism that drives TCR internalization from the IS together with its peptide-MHC ligand.

Original publication

DOI

10.1016/j.immuni.2011.06.003

Type

Journal article

Journal

Immunity

Publication Date

26/08/2011

Volume

35

Pages

208 - 222

Keywords

Animals, Antigen Presentation, Antigens, Cell Communication, Histocompatibility Antigens Class II, Humans, Immunological Synapses, Jurkat Cells, Membrane Proteins, Mice, Mice, Knockout, Mice, Transgenic, Monomeric GTP-Binding Proteins, Peptide Fragments, Phagocytosis, Protein Transport, Receptors, Antigen, T-Cell, Signal Transduction, rho GTP-Binding Proteins