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
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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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
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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