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An agonist-occupied  β   2 -adrenergic receptor ( β   2 -AR) recruits G protein receptor kinase-2 (GRK2) which is recruited to the membrane. Thus, the physical proximity of activated  β   2 -AR and PI-3K allows the activation of the latter. In contrast, it has been observed that the  β   1 -AR is unable to activate the PI-3K/Akt pathway. We hypothesized that the difference might be due to molecular determinants present in the carboxy termini of the two  β -AR subtypes. Using transiently transfected HEK 293 cells expressing either  β   1 - or  β   2 -AR, we also observed that in presence of an agonist,  β   2 -AR, but not  β   1 -AR, is able to activate the PI-3K/Akt pathway. Switching the seventh transmembrane domain and the carboxy tail between the two receptors reverses this phenotype; that is,  β   1  ×  β   2 -AR can activate the PI-3K/Akt pathway whereas  β   2  ×  β   1 -AR cannot. Pretreatment with pertussis toxin abolished the activation of PI-3K by  β   2 - or  β   1  ×  β   2 -AR stimulation. Ligand-mediated internalization of the  β   2 -AR induced by a 15-minute stimulation with agonist was abolished in the presence of a dominant negative of PI-3K or following pertussis toxin pretreatment. These results indicate that the subtype-specific differences in the coupling to PI-3K/Akt pathway are due to molecular determinants present in the carboxy tail of the receptor and further that  β   2 -AR activates PI-3K via a pertussis toxin-sensitive mechanism.

international journal of cell biology

Determinants Present in the Receptor Carboxy Tail Are Responsible for Differences in Subtype-Specific Coupling of<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:mi>β</mml:mi></mml:math>-Adrenergic Receptors to Phosphoinositide 3-Kinase

Determinants Present in the Receptor Carboxy Tail Are Responsible for Differences in Subtype-Specific Coupling ofβ-Adrenergic Receptors to Phosphoinositide 3-Kinase