Stoichiometry and intracellular fate of TRIM-containing TCR complexes

Studying the stoichiometry and intracellular trafficking of the T cell antigen receptor (TCR) is pivotal in understanding its mechanisms of activation. Although the TCR-interacting molecule (TRIM) is part of the TCR complex, it was not included in such 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 alphabetaTCR is alpha beta epsilon2 gamma delta zeta2 TRIM2 (abe2gdz2TRIM2).

Smaller alphabetaTCR complexes possess a abe2gdz2 stoichiometry. Stimulating the alphabetaTCR with anti-CD3 antibodies, we demonstrate by confocal laser scanning microscopy that CD3epsilon colocalizes with zeta and both are degraded upon prolonged stimulation, possibly within the lysosomal compartment.

In contrast, a substantial fraction of TRIM does not colocalize with zeta. Furthermore, TRIM neither moves to lysosomes nor is degraded.

Immunoprecipitation studies and BN-PAGE indicate that TRIM also associates with the gammadeltaTCR.

Conclusions: Small alphabetaTCR complexes have a abe2gdz2 stoichiometry; whereas those associated with one TRIM dimer are abe2gdz2TRIM2. TRIM is differentially processed compared to CD3 and zeta subunits after T cell activation and not degraded.

The gammadeltaTCR also associates with TRIM.

Author: Mahima SwamyGabrielle SiegersGina FialaEszter MolnarElaine DopferPaul FischBurkhart SchravenWolfgang Schamel
Credits/Source: Cell Communication and Signaling 2010, 8:5

Published on: 2010-03-18

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