Protein kinase A type I activates a CRE-element more efficiently than protein kinase A type II regardless of C subunit isoform |
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| Authors: | Øystein Stakkestad Anja CV Larsen Anne-Katrine Kvissel Sissel Eikvar Sigurd Ørstavik Bjørn S Skålhegg |
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| Institution: | 1.Department of Nutrition, Institute for Basic Medical Sciences,University of Oslo,Blindern, OSLO,Norway;2.Department of Biochemistry, Institute for Basic Medical Sciences,University of Oslo,Blindern, OSLO,Norway;3.Department of Pathology, The Norwegian Radium Hospital,Oslo University Hospital,Oslo,Norway;4.Department of Oncology, Ullev?l Hospital,Oslo University Hospital,Nydalen, OSLO,Norway |
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| Abstract: | Background Protein kinase A type I (PKAI) and PKAII are expressed in most of the eukaryotic cells examined. PKA is a major receptor for
cAMP and specificity is achieved partly through tissue-dependent expression and subcellular localization of subunits with
different biochemical properties. In addition posttranslational modifications help fine tune PKA activity, distribution and
interaction in the cell. In spite of this the functional significance of two forms of PKA in one cell has not been fully determined.
Here we have tested the ability of PKAI and PKAII formed by expression of the regulatory (R) subunits RIα or RIIα in conjunction
with Cα1 or Cβ2 to activate a co-transfected luciferace reporter gene, controlled by the cyclic AMP responsive element-binding
protein (CREB) in vivo. |
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