All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

Conserved cysteine dioxidation enhances membrane interaction of human Cl(-)intracellular channel 5

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F20%3A00533907" target="_blank" >RIV/61388971:_____/20:00533907 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11310/20:10413570

  • Result on the web

    <a href="https://faseb.onlinelibrary.wiley.com/doi/abs/10.1096/fj.202000399R" target="_blank" >https://faseb.onlinelibrary.wiley.com/doi/abs/10.1096/fj.202000399R</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1096/fj.202000399R" target="_blank" >10.1096/fj.202000399R</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Conserved cysteine dioxidation enhances membrane interaction of human Cl(-)intracellular channel 5

  • Original language description

    The human chloride intracellular channel (hCLIC) family is thought to transition between globular and membrane-associated forms by exposure of a hydrophobic surface. However, the molecular identity of this surface, and the triggering events leading to its exposure, remain elusive. Here, by combining biochemical and structural approaches, together with mass spectrometry (MS) analyses, we show that hCLIC5 is inherently flexible. X-ray crystallography revealed the existence of a globular conformation, while small-angle X-ray scattering showed additional elongated forms consisting of exposure of the conserved hydrophobic inter-domain interface to the bulk phase. Tryptophan fluorescence measurements demonstrated that the transition to the membrane-associated form is enhanced by the presence of oxidative environment and lipids. Using MS, we identified a dose-dependent oxidation of a highly conserved cysteine residue, known to play a key role in the structurally related omega-class of glutathione-S-transferases. Hydrogen/deuterium exchange MS analysis revealed that oxidation of this cysteine facilitates the exposure of the conserved hydrophobic inter-domain interface. Together, our results pinpoint an oxidation of a specific cysteine residue as a triggering mechanism initializing the molecular commitment for membrane interaction in the CLIC family.

  • 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

    10602 - Biology (theoretical, mathematical, thermal, cryobiology, biological rhythm), Evolutionary 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

    2020

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    FASEB Journal

  • ISSN

    0892-6638

  • e-ISSN

  • Volume of the periodical

    34

  • Issue of the periodical within the volume

    8

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    16

  • Pages from-to

    9925-9940

  • UT code for WoS article

    000541773000001

  • EID of the result in the Scopus database

    2-s2.0-85089440364