Components of the G(s) signaling cascade exhibit distinct changes in mobility and membrane domain localization upon beta(2)-adrenergic receptor activation
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F20%3A43902459" target="_blank" >RIV/60076658:12310/20:43902459 - isvavai.cz</a>
Result on the web
<a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7333016/" target="_blank" >https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7333016/</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1111/tra.12724" target="_blank" >10.1111/tra.12724</a>
Alternative languages
Result language
angličtina
Original language name
Components of the G(s) signaling cascade exhibit distinct changes in mobility and membrane domain localization upon beta(2)-adrenergic receptor activation
Original language description
The G protein signaling cascade is a key player in cell signaling. Cascade activation leads to a redistribution of its members in various cellular compartments. These changes are likely related to the "second wave" of signaling from endosomes. Here, we set out to determine whether G(s) signaling cascade members expressed at very low levels exhibit altered mobility and localize in clathrin-coated structures (CCSs) or caveolae upon activation by beta(2)-adrenergic receptors (beta(2)AR). Activated beta(2)AR showed decreased mobility and sustained accumulation in CCSs but not in caveolae. Arrestin 3 translocated to the plasma membrane after beta(2)AR activation and showed very low mobility and pronounced accumulation in CCSs. In contrast, G alpha(s) and G gamma(2) exhibited a modest reduction in mobility but no detectable accumulation in or exclusion from CCSs or caveolae. The effector adenylyl cyclase 5 (AC5) showed a slight mobility increase upon beta(2)AR stimulation, no redistribution to CCSs, and weak activation-independent accumulation in caveolae. Our findings show an overall decrease in the mobility of most activated G(s) signaling cascade members and confirm that beta(2)AR and arrestin 3 accumulate in CCSs, while G alpha(s), G gamma(2) and AC5 can transiently enter CCSs and caveolae but do not accumulate in and are not excluded from these domains.
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
10601 - Cell biology
Result continuities
Project
<a href="/en/project/GJ20-11563Y" target="_blank" >GJ20-11563Y: Allosteric communication in membrane protein complexes linked to conformational transitions on multiple timescales</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
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
Traffic
ISSN
1398-9219
e-ISSN
—
Volume of the periodical
21
Issue of the periodical within the volume
4
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
324-332
UT code for WoS article
000518877400002
EID of the result in the Scopus database
2-s2.0-85081303588