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J Biol Chem, Vol. 274, Issue 46, 32574-32579, November 12, 1999

Membrane-bound cAMP-dependent Protein Kinase Controls cAMP-induced Differentiation in PC12 Cells

Silvana CassanoDagger , Antonio Di LietoDagger , Rita CerilloDagger , and Enrico V. AvvedimentoDagger §

From the Dagger  Centro di Endocrinologia ed Oncologia Sperimentale del CNR, Dipartimento di Biologia e Patologia Molecolare e Cellulare, Facoltà di Medicina e Chirurgia, Università "Federico II" Napoli, 80131 Napoli, Italy and the § Dipartimento di Medicina Sperimentale e Clinica, Facoltà di Medicina e Chirurgia, Università di Catanzaro "Magna Graecia", 88100 Catanzaro, Italy

The A126 cell line, a derivative of PC12, is defective in cAMP-induced transcription and does not differentiate in the presence of cAMP. In these cells overexpression of a cAMP-dependent protein kinase (PKA) anchor protein, AKAP75, and of the PKA catalytic subunit substantially increased the fraction of PKAII bound to the membrane, stimulated the transcription of cAMP-induced genes, and induced terminal differentiation. Conversely, wild type PC12 cells expressing a derivative of the AKAP75 protein, AKAP45, which binds the PKA regulatory subunits RII, but fails to locate them to the membranes, induced translocation of PKAII to the cytosol. These cells did not efficiently accumulate PKA catalytic subunit in the nuclei when stimulated with cAMP, did not transcribe cAMP-induced genes, and failed to differentiate when exposed to cAMP. These data indicate that membrane-bound PKA positively controls the transcription of cAMP-induced genes and differentiation in PC12 cells.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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