Abstract
The alpha subunit (Gsalpha) of the stimulatory heterotrimeric guanosine triphosphate binding protein (G protein) Gs activates all isoforms of mammalian adenylyl cyclase. Adenylyl cyclase (Type V) and its subdomains, which interact with Gsalpha, promoted inactivation of the G protein by increasing its guanosine triphosphatase (GTPase) activity. Adenylyl cyclase and its subdomains also augmented the receptor-mediated activation of heterotrimeric Gs and thereby facilitated the rapid onset of signaling. These findings demonstrate that adenylyl cyclase functions as a GTPase activating protein (GAP) for the monomeric Gsalpha and enhances the GTP/GDP exchange factor (GEF) activity of receptors.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenylyl Cyclases / chemistry
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Adenylyl Cyclases / genetics
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Adenylyl Cyclases / metabolism*
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Animals
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Cell Line
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GTP Phosphohydrolases / metabolism*
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GTP-Binding Protein alpha Subunits, Gs / metabolism*
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GTPase-Activating Proteins
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Guanine Nucleotide Exchange Factors
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Guanosine 5'-O-(3-Thiotriphosphate) / metabolism
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Guanosine Triphosphate / metabolism
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Magnesium / pharmacology
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Proteins / metabolism
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Receptors, Adrenergic, beta-2 / metabolism
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Recombinant Proteins / metabolism
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Signal Transduction*
Substances
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GTPase-Activating Proteins
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Guanine Nucleotide Exchange Factors
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Proteins
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Receptors, Adrenergic, beta-2
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Recombinant Proteins
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Guanosine 5'-O-(3-Thiotriphosphate)
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Guanosine Triphosphate
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GTP Phosphohydrolases
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GTP-Binding Protein alpha Subunits, Gs
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Adenylyl Cyclases
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Magnesium