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Slow phosphorylation of a tyrosine residue in LAT optimizes T cell ligand discrimination

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    SYSNO ASEP0511345
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleSlow phosphorylation of a tyrosine residue in LAT optimizes T cell ligand discrimination
    Author(s) Lo, W.L. (US)
    Shah, N.H. (US)
    Rubin, S. A. (US)
    Zhang, W. (US)
    Horková, Veronika (UMG-J) ORCID
    Fallahee, I. R. (US)
    Štěpánek, Ondřej (UMG-J) RID, ORCID
    Zon, L.I. (US)
    Kuriyan, J. (US)
    Weiss, A. (US)
    Number of authors10
    Source TitleNature Immunology. - : Nature Publishing Group - ISSN 1529-2908
    Roč. 20, č. 11 (2019), s. 1481-1493
    Number of pages13 s.
    Publication formOnline - E
    Languageeng - English
    CountryUS - United States
    Keywordshomology 2 domain ; lymphoproliferative disease ; phospholipase c-gamma-1 ; signaling complexes ; self-peptides ; activation ; receptor ; tcr ; linker ; binding
    Subject RIVEB - Genetics ; Molecular Biology
    OECD categoryImmunology
    R&D ProjectsGJ19-03435Y GA ČR - Czech Science Foundation (CSF)
    Method of publishingLimited access
    Institutional supportUMG-J - RVO:68378050
    UT WOS000492309600018
    DOI https://doi.org/10.1038/s41590-019-0502-2
    AnnotationSelf-non-self discrimination is central to T cell-mediated immunity. The kinetic proofreading model can explain T cell antigen receptor (TCR) ligand discrimination, however, the rate-limiting steps have not been identified. Here, we show that tyrosine phosphorylation of the T cell adapter protein LAT at position Y132 is a critical kinetic bottleneck for ligand discrimination. LAT phosphorylation at Y132, mediated by the kinase ZAP-70, leads to the recruitment and activation of phospholipase C-gamma 1 (PLC-gamma 1), an important effector molecule for T cell activation. The slow phosphorylation of Y132, relative to other phosphosites on LAT, is governed by a preceding glycine residue (G131) but can be accelerated by substituting this glycine with aspartate or glutamate. Acceleration of Y132 phosphorylation increases the speed and magnitude of PLC-gamma 1 activation and enhances T cell sensitivity to weaker stimuli, including weak agonists and self-peptides. These observations suggest that the slow phosphorylation of Y132 acts as a proofreading step to facilitate T cell ligand discrimination.
    WorkplaceInstitute of Molecular Genetics
    ContactNikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217
    Year of Publishing2020
    Electronic addresshttps://www.nature.com/articles/s41590-019-0502-2
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