GSBS Student Publications


Mutation of glycine 49 to valine in the alpha subunit of GS results in the constitutive elevation of cyclic AMP synthesis

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Biochemistry



Document Type


Medical Subject Headings

Animals; Cell Line; Cricetinae; Cricetulus; Cyclic AMP; DNA; Enzyme Activation; Female; GTP-Binding Proteins; Glycine; Mutation; Plasmids; Protein Kinases; Transfection; Valine


Life Sciences | Medicine and Health Sciences


The G-protein GS couples hormone-activated receptors with adenylyl cyclase and stimulates increased cyclic AMP synthesis. Transient expression in COS-1 cells of cDNAs coding for the GS alpha-subunit (alpha S) or alpha S cDNAs having single amino acid mutations Gly49----Val or Gly225----Thr elevated cyclic AMP levels, resulting in the activation of cyclic AMP dependent protein kinase. Stable expression in Chinese hamster ovary cells of alpha S Val49 cDNA resulted in a small constitutive elevation of cyclic AMP that was sufficient to persistently activate cyclic AMP dependent protein kinase activity 1.5-2-fold over basal activity. Stable expression of wild-type alpha S or alpha S Thr225 in Chinese hamster ovary cells was less effective in sustaining elevated cyclic AMP synthesis and kinase activation compared to alpha SVal49.

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Citation: Biochemistry. 1989 May 30;28(11):4547-51.

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