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Components of the G s signaling cascade exhibit distinct changes in mobility and membrane domain localization upon β 2 ‐adrenergic receptor activation
Author(s) -
Bondar Alexey,
Jang Wonjo,
Sviridova Ekaterina,
Lambert Nevin A.
Publication year - 2020
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12724
Subject(s) - microbiology and biotechnology , caveolae , biology , signal transduction , g protein coupled receptor , receptor , endosome , g protein , caveolin 1 , effector , adenylyl cyclase , biochemistry , intracellular
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 β 2 ‐adrenergic receptors (β 2 AR). Activated β 2 AR showed decreased mobility and sustained accumulation in CCSs but not in caveolae. Arrestin 3 translocated to the plasma membrane after β 2 AR activation and showed very low mobility and pronounced accumulation in CCSs. In contrast, Gα s and Gγ 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 β 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 β 2 AR and arrestin 3 accumulate in CCSs, while Gα s , Gγ 2 and AC5 can transiently enter CCSs and caveolae but do not accumulate in and are not excluded from these domains.

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