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Originally published In Press as doi:10.1074/jbc.M202560200 on September 5, 2002

J. Biol. Chem., Vol. 277, Issue 45, 43281-43287, November 8, 2002
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The Translational Regulation of Lipoprotein Lipase by Epinephrine Involves an RNA Binding Complex Including the Catalytic Subunit of Protein Kinase A*

Gouri Ranganathan, Dan Phan, Irina D. Pokrovskaya, Joan E. McEwen, Chunling Li, and Philip A. KernDagger

From the Central Arkansas Veterans HealthCare System, and Department of Medicine, Division of Endocrinology, and the Department of Geriatrics, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72205

The balance of lipid flux in adipocytes is controlled by the opposing actions of lipolysis and lipogenesis, which are controlled primarily by hormone-sensitive lipase and lipoprotein lipase (LPL), respectively. Catecholamines stimulate adipocyte lipolysis through reversible phosphorylation of hormone-sensitive lipase, and simultaneously inhibit LPL activity. However, LPL regulation is complex and previous studies have described translational regulation of LPL in response to catecholamines because of an RNA-binding protein that interacts with the 3'-untranslated region of LPL mRNA. In this study, we identified several protein components of an LPL RNA binding complex. Using an LPL RNA affinity column, we identified two of the RNA-binding proteins as the catalytic (C) subunit of cAMP-dependent protein kinase (PKA), and A kinase anchoring protein (AKAP) 121/149, one of the PKA anchoring proteins, which has known RNA binding activity. To determine whether the C subunit was involved in LPL translation inhibition, the C subunit was depleted from the cytoplasmic extract of epinephrine-stimulated adipocytes by immunoprecipitation. This resulted in the loss of LPL translation inhibition activity of the extract, along with decreased RNA binding activity in a gel shift assay. To demonstrate the importance of the AKAPs, inhibition of PKA-AKAP binding with a peptide competitor (HT31) prevented epinephrine-mediated inhibition of LPL translation. C subunit kinase activity was necessary for LPL RNA binding and translation inhibition, suggesting that the phosphorylation of AKAP121/149 or other proteins was an important part of RNA binding complex formation. The hormonal activation of PKA results in the reversible phosphorylation of hormone-sensitive lipase, which is the primary mediator of adipocyte lipolysis. These studies demonstrate a dual role for PKA to simultaneously inhibit LPL-mediated lipogenesis through inhibition of LPL translation.

* This work was supported by a Career Development Award from the American Diabetes Association (to G. R.), Grant DK 39176 from the National Institute of Health, and a Merit Review Grant from the Veterans Administration.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Research, 151 LR, Central Arkansas Veterans Healthcare System, 4300 W. 7th St., Little Rock, AR 72205. Tel.: 501-257-4816; Fax: 501-257-4821; E-mail: kernphilipa@uams.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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