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PLoS One. 2017 Jul 25;12(7):e0181091. doi: 10.1371/journal.pone.0181091. eCollection 2017.

Evolution of the cAMP-dependent protein kinase (PKA) catalytic subunit isoforms.

Author information

1
Department of Nutrition, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
2
Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
3
Department of Microbiology, Oslo University Hospital Rikshospitalet, Oslo, Norway.
4
Bioinformatics Core Facility, Department of Informatics, University of Oslo, Oslo, Norway.

Abstract

The 3',5'-cyclic adenosine monophosphate (cAMP)-dependent protein kinase, or protein kinase A (PKA), pathway is one of the most versatile and best studied signaling pathways in eukaryotic cells. The two paralogous PKA catalytic subunits Cα and Cβ, encoded by the genes PRKACA and PRKACB, respectively, are among the best understood model kinases in signal transduction research. In this work, we explore and elucidate the evolution of the alternative 5' exons and the splicing pattern giving rise to the numerous PKA catalytic subunit isoforms. In addition to the universally conserved Cα1/Cβ1 isoforms, we find kinase variants with short N-termini in all main vertebrate classes, including the sperm-specific Cα2 isoform found to be conserved in all mammals. We also describe, for the first time, a PKA Cα isoform with a long N-terminus, paralogous to the PKA Cβ2 N-terminus. An analysis of isoform-specific variation highlights residues and motifs that are likely to be of functional importance.

PMID:
28742821
PMCID:
PMC5526564
DOI:
10.1371/journal.pone.0181091
[Indexed for MEDLINE]
Free PMC Article

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