Dissociated G?GTP and G?? Subunits are the Major Activated Form of Heterotrimeric Gi/o Proteins
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67179843%3A_____%2F14%3A00420933" target="_blank" >RIV/67179843:_____/14:00420933 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Dissociated G?GTP and G?? Subunits are the Major Activated Form of Heterotrimeric Gi/o Proteins
Original language description
While most heterotrimeric G proteins are thought to dissociate into G? and G?? subunits upon activation, the evidence in the Gi/o family has long been inconsistent and contradictory. The Gi/o protein family mediates inhibition of cAMP production and regulates activity of ion channels. Based on experimental evidence, both heterotrimer dissociation and rearrangement have been postulated as crucial steps of Gi/o protein activation and signal transduction. We have now investigated the process of Gi/o activation in living cells, directly by two-photon polarization microscopy and indirectly by observations of G protein-coupled receptor kinase-derived polypeptides. Our observations of existing fluorescently labeled and non-modified G?i/o constructs indicate that the molecular mechanism of G?i/o activation is affected by the presence and localization of the fluorescent label. All investigated non-labeled, non-modified Gi/o complexes extensively dissociate upon activation. The dissociated subun
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Biological Chemistry
ISSN
0021-9258
e-ISSN
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Volume of the periodical
289
Issue of the periodical within the volume
3
Country of publishing house
US - UNITED STATES
Number of pages
18
Pages from-to
1271-1281
UT code for WoS article
000332401700007
EID of the result in the Scopus database
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