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Originally published In Press as doi:10.1074/jbc.M000899200 on May 12, 2000

J. Biol. Chem., Vol. 275, Issue 30, 23362-23367, July 28, 2000
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Phospholemman Is a Substrate for Myotonic Dystrophy Protein Kinase*

J. Paul MounseyDagger §, J. Edward John IIIDagger , Steve M. Helmke, Erik W. Bush, John Gilbert||, Allen D. Roses||, M. Benjamin Perryman, Larry R. Jones**, and J. Randall MoormanDagger

From the Dagger  Departments of Internal Medicine (Cardiovascular Division), Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia 22908,  Department of Medicine, Division of Cardiology, University of Colorado Health Science Center, Denver, Colorado 80262, || Departments of Internal Medicine (Neurology) and Neurobiology, Duke University Medical Center, Durham, North Carolina 27710, and the ** Departments of Internal Medicine and Pharmacology, Krannert Institute of Cardiology, Indiana University School of Medicine, Indianapolis, Indiana 46202

The genetic abnormality in myotonic muscular dystrophy, multiple CTG repeats lie upstream of a gene that encodes a novel protein kinase, myotonic dystrophy protein kinase (DMPK). Phospholemman (PLM), a major membrane substrate for phosphorylation by protein kinases A and C, induces Cl currents (ICl(PLM)) when expressed in Xenopus oocytes. To test the idea that PLM is a substrate for DMPK, we measured in vitro phosphorylation of purified PLM by DMPK. To assess the functional effects of PLM phosphorylation we compared ICl(PLM) in Xenopus oocytes expressing PLM alone to currents in oocytes co-expressing DMPK, and examined the effect of DMPK on oocyte membrane PLM expression. We found that PLM is indeed a good substrate for DMPK in vitro. Co-expression of DMPK with PLM in oocytes resulted in a reduction in ICl(PLM). This was most likely a specific effect of phosphorylation of PLM by DMPK, as the effect was not present in oocytes expressing a phos(-) PLM mutant in which all potential phosphorylation had been disabled by Ser right-arrow Ala substitution. The biophysical characteristics of ICl(PLM) were not changed by DMPK or by the phos(-) mutation. Co-expression of DMPK reduced the expression of PLM in oocyte membranes, suggesting a possible mechanism for the observed reduction in ICl(PLM) amplitude. These data show that PLM is a substrate for phosphorylation by DMPK and provide functional evidence for modulation of PLM function by phosphorylation.

* This work was supported by the National Institutes of Health (to A. D. R., L. R. J., and J. R. M.), the Muscular Dystrophy Association (to J. G., A. D. R., and J. R. M.), the Piton Foundation (to A. D. R.), the American Heart Association Virginia Affiliate (to J. P. M.), an American Heart Association Established Investigator Award (to J. R. M.), and the long term support of the Clinical Research Unit, M01-RR-30, National Center for Research Resources, General Clinical Research Centers Program, National Institutes of Health.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.

§ To whom correspondence should be addressed: Box 6012, MR4 Bldg., UVAHSC, Charlottesville, VA 22908. Tel.: 804-982-3367; Fax: 804-982-3162; E-mail: pmounsey@virginia.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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