Switching of the coupling of the β2-adrenergic receptor to different G proteins by protein kinase A View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-11

AUTHORS

Yehia Daaka, Louis M. Luttrell, Robert J. Lefkowitz

ABSTRACT

Many of the G-protein-coupled receptors for hormones that bind to the cell surface can signal to the interior of the cell through several different classes of G protein1,2,3,4. For example, although most of the actions of the prototype β2-adrenergic receptor are mediated through Gs proteins and the cyclic-AMP-dependent protein kinase (PKA) system5,6, β-adrenergic receptors can also couple to Gi proteins1,2. Here we investigate the mechanism that controls the specificity of this coupling. We show that in HEK293 cells, stimulation of mitogen-activated protein (MAP) kinase by the β2-adrenergic receptor is mediated by the βγ subunits of pertussis-toxin-sensitive G proteins through a pathway involving the non-receptor tyrosine kinase c-Src and the G protein Ras. Activation of this pathway by the β2-adrenergic receptor requires that the receptor be phosphorylated by PKA because it is blocked by H-89, an inhibitor of PKA. Additionally, a mutant of the receptor, which lacks the sites normally phosphorylated by PKA, can activate adenylyl cyclase5, the enzyme that generates cAMP, but not MAP kinase. Our results demonstrate that a mechanism previously shown to mediate uncoupling of the β2-adrenergic receptor from Gs and thus heterologous desensitization7 (PKA-mediated receptor phosphorylation), also serves to ‘switch’ coupling of this receptor from Gs to Gi and initiate a new set of signalling events. More... »

PAGES

88-91

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/36362

DOI

http://dx.doi.org/10.1038/36362

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1052687659

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9363896


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