ArticleThe Journal of biological chemistry2009
Peptide-major histocompatibility complex dimensions control proximal kinase-phosphatase balance during T cell activation.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed, 50 citations in OpenAlex.
- Ligand-induced segregation from large cell-surface phosphatases is a critical step in γδ TCR triggering.Cell reports · 2024Article
- TCR/CD3-based synthetic antigen receptors (TCC) convey superior antigen sensitivity combined with high fidelity of activation.Science advances · 2024Article
- Understanding How Cells Probe the World: A Preliminary Step towards Modeling Cell Behavior?International journal of molecular sciences · 2023Article
- The interplay between membrane topology and mechanical forces in regulating T cell receptor activity.Communications biology · 2022Review
- Nanoscale Colocalization of NK Cell Activating and Inhibitory Receptors Controls Signal Integration.Frontiers in immunology · 2022Article
- T Cell Activation Machinery: Form and Function in Natural and Engineered Immune Receptors.International journal of molecular sciences · 2020Review
- Signaling from T cell receptors (TCRs) and chimeric antigen receptors (CARs) on T cells.Cellular & molecular immunology · 2020Review
- Synergistic factors control kinase-phosphatase organization in B-cells engaged with supported bilayers.Molecular biology of the cell · 2020Article
- TCR-pMHC bond conformation controls TCR ligand discrimination.Cellular & molecular immunology · 2020Article
- Synthetic TRuC receptors engaging the complete T cell receptor for potent anti-tumor response.Nature communications · 2019Article
- T-Cell Mechanobiology: Force Sensation, Potentiation, and Translation.Frontiers in physics · 2019Article
- High-Affinity Ligands Can Trigger T Cell Receptor Signaling Without CD45 Segregation.Frontiers in immunology · 2018Article
- The Affinity of Elongated Membrane-Tethered Ligands Determines Potency of T Cell Receptor Triggering.Frontiers in immunology · 2017Article
- Action and Traction: Cytoskeletal Control of Receptor Triggering at the Immunological Synapse.Frontiers in immunology · 2016Review
- Costimulation of IL-2 Production through CD28 Is Dependent on the Size of Its Ligand.Journal of immunology (Baltimore, Md. : 1950) · 2015Article
- Designing chimeric antigen receptors to effectively and safely target tumors.Current opinion in immunology · 2015Review
- Regulation of T-cell receptor signaling by the actin cytoskeleton and poroelastic cytoplasm.Immunological reviews · 2013Review
- "Cell biology meets physiology: functional organization of vertebrate plasma membranes"--the immunological synapse.Current topics in membranes · 2013Article
- Properties and applications of single-chain major histocompatibility complex class I molecules.Antioxidants & redox signaling · 2011Review
- Mechanisms for size-dependent protein segregation at immune synapses assessed with molecular rulers.Biophysical journal · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
T cell antigen recognition requires binding of the T cell receptor (TCR) to a complex between peptide antigen and major histocompatibility complex molecules (pMHC), and this recognition occurs at the interface between the T cell and the antigen-presenting cell. The TCR and pMHC molecules are small compared with other abundant cell surface molecules, and it has been suggested that small size is functionally important. We show here that elongation of both mouse and human MHC class I molecules abrogates T cell antigen recognition as measured by cytokine production and target cell killing. This elongation disrupted tyrosine phosphorylation and Zap70 recruitment at the contact region without affecting TCR or coreceptor binding. Contact areas with elongated forms of pMHC showed an increase in intermembrane distance and less efficient segregation of CD3 from the large tyrosine phosphatase CD45. These findings demonstrate that T cell antigen recognition is strongly dependent on pMHC size and are consistent with models of TCR triggering requiring segregation or mechanical pulling of the TCR.
Indexed as
Identifiers
What OpenQuestion holds
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.