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J. Biol. Chem., Vol. 275, Issue 49, 38938-38943, December 8, 2000
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From the Department of Pharmacology & Cell Biophysics, University
of Cincinnati College of Medicine, Cincinnati, Ohio 45267-0575
Phospholamban (PLB) can be phosphorylated at
Ser16 by cyclic AMP-dependent protein
kinase and at Thr17 by
Ca2+-calmodulin-dependent protein kinase during
A Single Site (Ser16) Phosphorylation in
Phospholamban Is Sufficient in Mediating Its Maximal Cardiac Responses
to
-Agonists*
-agonist stimulation. A previous study indicated that mutation of
S16A in PLB resulted in lack of Thr17 phosphorylation and
attenuation of the -agonist stimulatory effects in perfused mouse
hearts. To further delineate the functional interplay between dual-site
PLB phosphorylation, we generated transgenic mice expressing the T17A
mutant PLB in the cardiac compartment of the null background. Lines
expressing similar levels of T17A mutant, S16A mutant, or wild-type PLB
in the null background were characterized in parallel. Cardiac myocyte
basal mechanics and Ca2+ kinetics were similar among the
three groups. Isoproterenol stimulation was associated with
phosphorylation of both Ser16 and Thr17 in
wild-type PLB and Ser16 phosphorylation in T17A mutant PLB,
whereas there was no detectable phosphorylation of S16A mutant PLB.
Phosphorylation of Ser16 alone in T17A mutant PLB resulted
in responses of the mechanical and Ca2+ kinetic parameters
to isoproterenol similar to those in wild-type myocytes, which
exhibited dual-site PLB phosphorylation. However, those parameters were
significantly attenuated in the S16A mutant myocytes. Thus,
Ser16 in PLB can be phosphorylated independently of
Thr17 in vivo, and phosphorylation of
Ser16 is sufficient for mediating the maximal cardiac
responses to -adrenergic stimulation.
*
This study was supported by the National Institutes of
Health Grants HL26057, HL52318, HL07382, and P40RR12358.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: Dept. of Pharmacology
& Cell Biophysics, University of Cincinnati College of Medicine, 231 Bethesda Ave., Cincinnati, OH 45267-0575. Tel.: 513-558-2377; Fax:
513-558-2269; E-mail: kraniaeg@email.uc.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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