Evidence map›Paper›PMID 20298603›Full record

ArticleCell communication and signaling : CCS2010

Stoichiometry and intracellular fate of TRIM-containing TCR complexes.

Mahima Swamy, Gabrielle M Siegers, Gina J Fiala, Eszter Molnar, Elaine P Dopfer, Paul Fisch, Burkhart Schraven, Wolfgang Wa Schamel

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Article in Cell communication and signaling : CCS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

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6citing papers in PubMed
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3 · Its place in the literature

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6 citing papers in PubMed.

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  6. Meeting report: Signal transduction meets systems biology.Cell communication and signaling : CCS · 2012
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5 · Who and what money

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8 authors.

Mahima SwamyDepartment of Molecular Immunology, Max Planck-Institute of Immunobiology and Institute for Biology III, Albert Ludwigs University Freiburg, Stübeweg 51, 79108 Freiburg, Germany. schamel@immunbio.mpg.de.
Gabrielle M Siegers
Gina J Fiala
Eszter Molnar
Elaine P Dopfer
Paul Fisch
Burkhart Schraven
Wolfgang Wa Schamel

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundStudying the stoichiometry and intracellular trafficking of the T cell antigen receptor (TCR) is pivotal in understanding its mechanisms of activation. The alphabetaTCR includes the antigen-binding TCRalphabeta heterodimer as well as the signal transducing CD3epsilongamma, CD3epsilondelta and zeta2 subunits. Although the TCR-interacting molecule (TRIM) is also part of the alphabetaTCR complex, it has not been included in most reports so far.

resultsWe 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 TCRalphabetaCD3epsilon2gammadeltazeta2TRIM2. Smaller alphabetaTCR complexes possess a TCRalphabeta CD3epsilon2gammadeltazeta2 stoichiometry. Complexes of these sizes were detected in T cell lines as well as in primary human and mouse T cells. 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.

conclusionsSmall alphabetaTCR complexes have a TCRalphabeta CD3epsilon2gammadeltazeta2 stoichiometry; whereas those associated with one TRIM dimer are TCRalphabeta CD3epsilon2gammadeltazeta2TRIM2. TRIM is differentially processed compared to CD3 and zeta subunits after T cell activation and is not degraded. The gammadeltaTCR also associates with TRIM.

Identifiers

PMID20298603
PMCPMC2848047

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.