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The role of prolines and glycine in the transmembrane domain of LAT

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F21%3A00539844" target="_blank" >RIV/61388955:_____/21:00539844 - isvavai.cz</a>

  • Alternative codes found

    RIV/68378050:_____/21:00554617 RIV/00216208:11310/21:10440413

  • Result on the web

    <a href="https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.15713" target="_blank" >https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.15713</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1111/febs.15713" target="_blank" >10.1111/febs.15713</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    The role of prolines and glycine in the transmembrane domain of LAT

  • Original language description

    Linker for activation in T cells (LAT) is a critical regulator of T‐cell development and function. It organises signalling events at the plasma membrane. However, the mechanism, which controls LAT localisation at the plasma membrane, is not fully understood. Here, we studied the impact of helix‐breaking amino acids, two prolines and one glycine, in the transmembrane segment on localisation and function of LAT. Using in silico analysis, confocal and super‐resolution imaging and flow cytometry, we demonstrate that central proline residue destabilises transmembrane helix by inducing a kink. The helical structure and dynamics are further regulated by glycine and another proline residue in the luminal part of LAT transmembrane domain. Replacement of these residues with aliphatic amino acids reduces LAT dependence on palmitoylation for sorting to the plasma membrane. However, surface expression of these mutants is not sufficient to recover function of nonpalmitoylated LAT in stimulated T cells. These data indicate that geometry and dynamics of LAT transmembrane segment regulate its localisation and function in immune cells.n

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2021

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    FEBS Journal

  • ISSN

    1742-464X

  • e-ISSN

    1742-4658

  • Volume of the periodical

    288

  • Issue of the periodical within the volume

    13

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    14

  • Pages from-to

    4039-4052

  • UT code for WoS article

    000617213100001

  • EID of the result in the Scopus database

    2-s2.0-85100974966