期刊
IMMUNITY
卷 35, 期 2, 页码 208-222出版社
CELL PRESS
DOI: 10.1016/j.immuni.2011.06.003
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资金
- CICYT [SAF2006-01391, SAF2010-14912]
- Comunidad de Madrid [SAL-0159/2006]
- RETICS [RD06/0020/1002, RD06/0020/0001]
- EU
- Fundacion Cientifica de la Asociacion Espanola Contra el Cancer
- MRC [G0601618] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BBS/E/B/00001207, BBS/E/B/0000C207, BBS/E/B/0000C206] Funding Source: researchfish
- Medical Research Council [G0601618] Funding Source: researchfish
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 mu m 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.
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