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Published on: June 7, 2019
Protein kinase A catalytic subunit isoform PRKACA; History, function and physiology
Rigney E Turnham1, John D Scott1
1Howard Hughes Medical Institute, Department of Pharmacology, Box 357750, University of Washington School of Medicine, 1959 Pacific St. NE, Seattle, WA 98195, United States.
Abstract:
Our appreciation of the scope and influence of second messenger signaling has its origins in pioneering work on the cAMP-dependent protein kinase. Also called protein kinase A (PKA), this holoenzyme exists as a tetramer comprised of a regulatory (R) subunit dimer and two catalytic (C) subunits. Upon binding of two molecules of the second messenger cAMP to each R subunit, a conformational change in the PKA holoenzyme occurs to release the C subunits. These active kinases phosphorylate downstream targets to propagate cAMP responsive cell signaling events. This article focuses on the discovery, structure, cellular location and physiological effects of the catalytic subunit alpha of protein kinase A (encoded by the gene PRKACA). We also explore the potential role of this essential gene as a molecular mediator of certain disease states.
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