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Agonist-induced dimer dissociation as a macromolecular step in G protein-coupled receptor signaling

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F17%3A00100420" target="_blank" >RIV/00216224:14310/17:00100420 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1038/s41467-017-00253-9" target="_blank" >http://dx.doi.org/10.1038/s41467-017-00253-9</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/s41467-017-00253-9" target="_blank" >10.1038/s41467-017-00253-9</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Agonist-induced dimer dissociation as a macromolecular step in G protein-coupled receptor signaling

  • Original language description

    G protein-coupled receptors (GPCRs) constitute the largest family of cell surface receptors. They can exist and act as dimers, but the requirement of dimers for agonist-induced signal initiation and structural dynamics remains largely unknown. Frizzled 6 (FZD6) is a member of Class F GPCRs, which bind WNT proteins to initiate signaling. Here, we show that FZD6 dimerizes and that the dimer interface of FZD6 is formed by the transmembrane a-helices four and five. Most importantly, we present the agonist-induced dissociation/re-association of a GPCR dimer through the use of live cell imaging techniques. Further analysis of a dimerization-impaired FZD6 mutant indicates that dimer dissociation is an integral part of FZD6 signaling to extracellular signal-regulated kinases1/2. The discovery of agonistdependent dynamics of dimers as an intrinsic process of receptor activation extends our understanding of Class F and other dimerizing GPCRs, offering novel targets for dimerinterfering small molecules.

  • 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

    <a href="/en/project/EE2.3.20.0180" target="_blank" >EE2.3.20.0180: Cooperation between Masaryk University and Karolinska Institutet, Stockholm in the field of biomedicine</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2017

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Nature Communications

  • ISSN

    2041-1723

  • e-ISSN

  • Volume of the periodical

    8

  • Issue of the periodical within the volume

    August

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    15

  • Pages from-to

    1-15

  • UT code for WoS article

    000407198800015

  • EID of the result in the Scopus database