Phosphorylation of Gi protein by cyclic AMP-dependent protein kinase inhibits its dissociation into α-subunits and βγ-subunits by Mg2+ and GTPγS
European Journal of Pharmacology: Molecular Pharmacology(1991)
摘要
Pretreatment of partially purified inhibitory GTP-binding protein (Gi, 41 kDa) with activated cyclic AMP-dependent protein kinase (PKA) decreases its ADP-ribosylation by islet-activating protein (pertussis toxin, IAP). We examined whether this decrease was associated with dissociation of the trimer of αβγ-subunits of Gi protein into α-subunits and βγ-subunits. Results showed that phosphorylation of the Gi protein by PKA impaired its dissociation into α-subunits and βγ-subunits by 50 mM Mg2+ and 100 μM GTPγS. The results suggested that phosphorylation of the Gi protein by PKA possibly caused a conformational change of the trimer Gi protein.
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关键词
GTP-binding protein (inhibitory),Gi protein,Pertussis toxin,ADP-ribosylation,Phosphorylation,Cyclic AMP-dependent protein kinase
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