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Originally published In Press as doi:10.1074/jbc.M202476200 on July 11, 2002

J. Biol. Chem., Vol. 277, Issue 37, 33598-33603, September 13, 2002
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Trafficking of L-type Calcium Channels Mediated by the Postsynaptic Scaffolding Protein AKAP79*

Christophe Altierab, Stefan J. Dubela, Christian Barrèrea, Scott E. Jarviscd, Stéphanie C. Stotzce, Renée L. Spaetgenscf, John D. Scottg, Véronique Corneth, Michel De Waardi, Gerald W. Zamponicj, Joël Nargeota, and Emmanuel Bourinetak

From the a Physiopathologie des Canaux Ioniques, Institut de Génétique Humaine CNRS UPR1142, 141 Rue de la Cardonille, 34396 Montpellier Cedex 5, France, the c Department of Physiology and Biophysics, Neuroscience Research Group, University of Calgary, Calgary, Alberta T2N 4N1, Canada, the g Howard Hughes Medical Institute, Vollum Institute, Oregon Health & Science University, Portland, Oregon 97201, h INSERM U464, Faculté de Médecine Nord, Boulevard Pierre Dramard, 13916 Marseille, France, and i INSERM EMI99-31, 17 Rue des Martyrs, 38054 Grenoble Cedex 9, France

Accurate calcium signaling requires spatial and temporal coordination of voltage-gated calcium channels (VGCCs) and a variety of signal transduction proteins. Accordingly, regulation of L-type VGCCs involves the assembly of complexes that include the channel subunits, protein kinase A (PKA), protein kinase A anchoring proteins (AKAPs), and beta 2-adrenergic receptors, although the molecular details underlying these interactions remain enigmatic. We show here, by combining extracellular epitope splicing into the channel pore-forming subunit and immunoassays with whole cell and single channel electrophysiological recordings, that AKAP79 directly regulates cell surface expression of L-type calcium channels independently of PKA. This regulation involves a short polyproline sequence contained specifically within the II-III cytoplasmic loop of the channel. Thus we propose a novel mechanism whereby AKAP79 and L-type VGCCs function as components of a biosynthetic mechanism that favors membrane incorporation of organized molecular complexes in a manner that is independent of PKA phosphorylation events.

* This work was supported by a Fondation UPSA grant (to E. B.), by Association Francaise de lutte contre les Myopathies (AFM) and Association de la Recherche contre le Cancer grants (to J. N.), and by operating grants from the Heart and Stroke Foundation of Alberta and the Northwest Territories and Canadian Institutes of Health Research (CIHR) (to G. W. Z.).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.

b  Supported by a studentship award from the AFM.

d  Holds an Alberta Heritage Foundation for Medical Research (AHFMR) M.D./Ph.D. studentship.

e  Supported by studentship awards from the AHFMR and the CIHR.

f  Supported by the AHFMR.

j Holds salary awards from the AHFMR and the CIHR.

k  To whom correspondence should be addressed: Physiopathologie des Canaux Ioniques Institut de Génétique Humaine, CNRS UPR1142, 141 Rue de la Cardonille, 34396 Montpellier Cedex 5, France. Tel.: 33-499-61-99-36; Fax: 33-499-61-99-01; E-mail: emmanuel.bourinet@igh.cnrs.fr.

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