1. Membrane localization of cAMP-dependent protein kinase amplifies cAMP signaling to the nucleus in PC12 cells
- Author
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Enrico V. Avvedimento, Rita Cerillo, Adriana Gallo, Antonio Porcellini, Max E. Gottesman, Vittoria Buccigrossi, Silvana Cassano, Cassano, S, Gallo, A, Buccigrossi, V, Porcellini, Antonio, Cerillo, R, Gottersman, Me, and Avvedimento, Ve
- Subjects
Gene isoform ,Protein subunit ,A Kinase Anchor Proteins ,Biology ,Biochemistry ,PC12 Cells ,Transcription (biology) ,medicine ,Cyclic AMP ,Animals ,Protein kinase A ,Cyclic AMP Response Element-Binding Protein ,Promoter Regions, Genetic ,Molecular Biology ,Cellular localization ,Adaptor Proteins, Signal Transducing ,Cell Nucleus ,Cell Membrane ,Proteins ,Cell Biology ,Cyclic AMP-Dependent Protein Kinases ,Cell biology ,Rats ,Isoenzymes ,Cytosol ,medicine.anatomical_structure ,biology.protein ,CREB1 ,Carrier Proteins ,Nucleus ,Protein Binding ,Signal Transduction - Abstract
The A126 cell line, in contrast to its PC12 parent, does not differentiate, accumulate nuclear cAMP-dependent protein kinase A (PKA) catalytic subunit, or transcribe cAMP-dependent promoters in response to cAMP. Total PKA is reduced by 50% and is partly resistant to cAMP-induced dissociation in vivo. Unlike PC12, where PKAII is membrane-associated, PKAII is exclusively cytosolic in A126. Cotransfection with the RII anchor protein (AKAP75) and the PKA catalytic subunit (C-PKA) restored cAMP-induced transcription to levels found in PC12. These data indicate that membrane-bound PKAII amplifies cAMP signaling to the nucleus and suggest that cAMP-mediated responses are specified by the type and cellular localization of the PKA isoform.
- Published
- 1996