ArticleImmunity2018
The T Cell Antigen Receptor α Transmembrane Domain Coordinates Triggering through Regulation of Bilayer Immersion and CD3 Subunit Associations.
Article in Immunity, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
47 citing papers in PubMed, 78 citations in OpenAlex.
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- Genomic characterization of the T-cell receptor loci inFrontiers in immunology · 2025Article
- Engineered allogeneic T cells decoupling T-cell-receptor and CD3 signalling enhance the antitumour activity of bispecific antibodies.Nature biomedical engineering · 2024Article
- Focusing on CD8Journal of experimental & clinical cancer research : CR · 2024Review
- TMX1, a disulfide oxidoreductase, is necessary for T cell function through regulation of CD3ζ.bioRxiv : the preprint server for biology · 2024Article
- Parsing digital or analog TCR performance through piconewton forces.Science advances · 2024Article
- Mechanical forces amplify TCR mechanotransduction in T cell activation and function.Applied physics reviews · 2024Review
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- Rigid crosslinking of the CD3 complex leads to superior T cell stimulation.Frontiers in immunology · 2024Article
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- Harnessing αβ T cell receptor mechanobiology to achieve the promise of immuno-oncology.Proceedings of the National Academy of Sciences of the United States of America · 2023Review
- Characterizing Biophysical Parameters of Single TCR-pMHC Interactions Using Optical Tweezers.Methods in molecular biology (Clifton, N.J.) · 2023Article
- A bead-based method for high-throughput mapping of the sequence- and force-dependence of T cell activation.Nature methods · 2022Article
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Authors and funding
15 authors at 6 institutions in 2 countries.
Funding
Abstract
Initial molecular details of cellular activation following αβT cell antigen receptor (TCR) ligation by peptide-major histocompatibility complexes (pMHC) remain unexplored. We determined the nuclear magnetic resonance (NMR) structure of the TCRα subunit transmembrane (TM) domain revealing a bipartite helix whose segmentation fosters dynamic movement. Positively charged TM residues Arg251 and Lys256 project from opposite faces of the helix, with Lys256 controlling immersion depth. Their modification caused stepwise reduction in TCR associations with CD3ζζ homodimers and CD3εγ plus CD3εδ heterodimers, respectively, leading to an activated transcriptome. Optical tweezers revealed that Arg251 and Lys256 mutations altered αβTCR-pMHC bond lifetimes, while mutations within interacting TCRα connecting peptide and CD3δ CxxC motif juxtamembrane elements selectively attenuated signal transduction. Our findings suggest that mechanical forces applied during pMHC ligation initiate T cell activation via a dissociative mechanism, shifting disposition of those basic sidechains to rearrange TCR complex membrane topology and weaken TCRαβ and CD3 associations.
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Registered trials
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.