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Stoichiometry and intracellular fate of TRIM-containing TCR complexes

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Swamy,  Mahima
Research Group and Chair of Molecular Immunology of the University of Freiburg, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Siegers,  Gabrielle M.
Research Group and Chair of Molecular Immunology of the University of Freiburg, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Fiala,  Gina J.
Research Group and Chair of Molecular Immunology of the University of Freiburg, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Molnar,  Eszter
Max Planck Society;

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Dopfer,  Elaine P.
Research Group and Chair of Molecular Immunology of the University of Freiburg, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Schamel,  Wolfgang W. A.
Research Group and Chair of Molecular Immunology of the University of Freiburg, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Citation

Swamy, M., Siegers, G. M., Fiala, G. J., Molnar, E., Dopfer, E. P., Fisch, P., et al. (2010). Stoichiometry and intracellular fate of TRIM-containing TCR complexes. Cell Communication and Signaling, 8, 1-10.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-8EE2-9
Abstract
BACKGROUND: Studying the stoichiometry and intracellular trafficking of the T cell antigen receptor (TCR) is pivotal in understanding its mechanisms of activation. The αβTCR includes the antigen-binding TCRaαβ heterodimer as well as the signal transducing CD3εγ, CD3εδ and ζ2 subunits. Although the TCR-interacting molecule (TRIM) is also part of the αβTCR complex, it has not been included in most reports so far. RESULTS: We used the native antibody-based mobility shift (NAMOS) assay in a first dimension (1D) blue native (BN)-PAGE and a 2D BN-/BN-PAGE to demonstrate that the stoichiometry of the digitonin-solublized TRIM-containing αβTCR is TCRαβCD3 ε2γδζ2TRIM2. Smaller αβTCR complexes possess a TCRαβ CD3 ε2γδζ2 stoichiometry. Complexes of these sizes were detected in T cell lines as well as in primary human and mouse T cells. Stimulating the αβTCR with anti-CD3 antibodies, we demonstrate by confocal laser scanning microscopy that CD3ε colocalizes with ζ and both are degraded upon prolonged stimulation, possibly within the lysosomal compartment. In contrast, a substantial fraction of TRIM does not colocalize with ζ. Furthermore, TRIM neither moves to lysosomes nor is degraded. Immunoprecipitation studies and BN-PAGE indicate that TRIM also associates with the γδ TCR. CONCLUSIONS: Small αβTCR complexes have a TCRαβ CD3ε2γδζ2 stoichiometry; whereas those associated with one TRIM dimer are TCRαβ CD3ε2γδζ2TRIM2. TRIM is differentially processed compared to CD3 and ζ subunits after T cell activation and is not degraded. The γδTCR also associates with TRIM.