Journal
BMC BIOCHEMISTRY
Volume 12, Issue -, Pages -Publisher
BIOMED CENTRAL LTD
DOI: 10.1186/1471-2091-12-40
Keywords
PKA; Catalytic subunit; N-terminal; splice variants
Categories
Funding
- Norwegian Research Council
- University of Oslo
- Deutsche Forschungsgemeinschaft (DFG) [He1818/6]
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Background: The two variants of the a-form of the catalytic (C) subunit of protein kinase A (PKA), designated C alpha 1 and C alpha 2, are encoded by the PRKACA gene. Whereas C alpha 1 is ubiquitous, C alpha 2 expression is restricted to the sperm cell. C alpha 1 and C alpha 2 are encoded with different N-terminal domains. In C alpha 1 but not C alpha 2 the N-terminal end introduces three sites for posttranslational modifications which include myristylation at Gly1, Asp-specific deamidation at Asn2 and autophosphorylation at Ser10. Previous reports have implicated specific biological features correlating with these modifications on C alpha 1. Since C alpha 2 is not modified in the same way as C alpha 1 we tested if they have distinct biochemical activities that may be reflected in different biological properties. Results: We show that C alpha 2 interacts with the two major forms of the regulatory subunit (R) of PKA, RI and RII, to form cAMP-sensitive PKAI and PKAII holoenzymes both in vitro and in vivo as is also the case with C alpha 1. Moreover, using Surface Plasmon Resonance (SPR), we show that the interaction patterns of the physiological inhibitors RI, RII and PKI were comparable for C alpha 2 and C alpha 1. This is also the case for their potency to inhibit catalytic activities of C alpha 2 and C alpha 1. Conclusion: We conclude that the regulatory complexes formed with either C alpha 1 or C alpha 2, respectively, are indistinguishable.
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