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Role of Regulatory Subunits and Protein Kinase Inhibitor (PKI) in Determining Nuclear Localization and Activity of the Catalytic Subunit of Protein Kinase A -- Wiley et al. 274 (10): 6381 -- Journal of Biological Chemistry HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS QUICK SEARCH: [advanced] Author: Keyword(s): Year: Vol: Page: This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Wiley, J. C. Articles by McKnight, G. S. Search for Related Content PubMed PubMed Citation Articles by Wiley, J. C. Articles by McKnight, G. S. J Biol Chem, Vol. 274, Issue 10, 6381-6387, March 5, 1999 Role of Regulatory Subunits and Protein Kinase Inhibitor (PKI) in Determining Nuclear Localization and Activity of the Catalytic Subunit of Protein Kinase A Jesse C. Wiley, Lauren A. Wailes, Rejean L. Idzerda, and G. Stanley McKnight From the Department of Pharmacology, University of Washington, Seattle, Washington 98195-7750 Regulation of protein kinase A by subcellular localization may be critical to target catalytic subunits to specific substrates. We employed epitope-tagged catalytic subunit to correlate subcellular localization and gene-inducing activity in the presence of regulatory subunit or protein kinase inhibitor (PKI). Transiently expressed catalytic subunit distributed throughout the cell and induced gene expression. Co-expression of regulatory subunit or PKI blocked gene induction and prevented nuclear accumulation. A mutant PKI lacking the nuclear export signal blocked gene induction but not nuclear accumulation, demonstrating that nuclear export is not essential to inhibit gene induction. When the catalytic subunit was targeted to the nucleus with a nuclear localization signal, it was not sequestered in the cytoplasm by regulatory subunit, although its activity was completely inhibited. PKI redistributed the nuclear catalytic subunit to the cytoplasm and blocked gene induction, demonstrating that the nuclear export signal of PKI can override a strong nuclear localization signal. With increasing PKI, the export process appeared to saturate, resulting in the return of catalytic subunit to the nucleus. These results demonstrate that both the regulatory subunit and PKI are able to completely inhibit the gene-inducing activity of the catalytic subunit even when the catalytic subunit is forced to concentrate in the nuclear compartment. Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc. This article has been cited by other articles: N. Gao, K. Asamitsu, Y. Hibi, T. Ueno, and T. Okamoto AKIP1 Enhances NF-{kappa}B-dependent Gene Expression by Promoting the Nuclear Retention and Phosphorylation of p65 J. Biol. Chem., March 21, 2008; 283(12): 7834 - 7843. [Abstract] [Full Text] [PDF] E. Szatmari, K. B. Kalita, G. Kharebava, and M. Hetman Role of Kinase Suppressor of Ras-1 in Neuronal Survival Signaling by Extracellular Signal-Regulated Kinase 1/2 J. Neurosci., October 17, 2007; 27(42): 11389 - 11400. [Abstract] [Full Text] [PDF] X. Chen, J.-C. Dai, S. A. Orellana, and E. M. Greenfield Endogenous Protein Kinase Inhibitor {gamma} Terminates Immediate-early Gene Expression Induced by cAMP-dependent Protein Kinase (PKA) Signaling: TERMINATION DEPENDS ON PKA INACTIVATION RATHER THAN PKA EXPORT FROM THE NUCLEUS J. Biol. Chem., January 28, 2005; 280(4): 2700 - 2707. 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[Abstract] [Full Text] [PDF] HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS All ASBMB Journals Molecular and Cellular Proteomics Journal of Lipid Research ASBMB Today Copyright © 1999 by the American Society for Biochemistry and Molecular Biology. разделы pki