Components of the G(s) signaling cascade exhibit distinct changes in mobility and membrane domain localization upon beta(2)-adrenergic receptor activation
Identifikátory výsledku
Kód výsledku v 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>
Výsledek na webu
<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>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Components of the G(s) signaling cascade exhibit distinct changes in mobility and membrane domain localization upon beta(2)-adrenergic receptor activation
Popis výsledku v původním jazyce
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.
Název v anglickém jazyce
Components of the G(s) signaling cascade exhibit distinct changes in mobility and membrane domain localization upon beta(2)-adrenergic receptor activation
Popis výsledku anglicky
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.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10601 - Cell biology
Návaznosti výsledku
Projekt
<a href="/cs/project/GJ20-11563Y" target="_blank" >GJ20-11563Y: Alosterická komunikace v membránových proteinových komplexech a její propojení s konformační dynamikou na mnoha časových škálách</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2020
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Traffic
ISSN
1398-9219
e-ISSN
—
Svazek periodika
21
Číslo periodika v rámci svazku
4
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
9
Strana od-do
324-332
Kód UT WoS článku
000518877400002
EID výsledku v databázi Scopus
2-s2.0-85081303588