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J. Biol. Chem., Vol. 276, Issue 43, 39959-39967, October 26, 2001
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From the In skeletal muscle both insulin and
contractile activity are physiological stimuli for glycogen synthesis,
which is thought to result in part from the dephosphorylation and
activation of glycogen synthase (GS).
PP1G/RGL(GM) is a glycogen/sarcoplasmic reticulum-associated type 1 phosphatase that was originally postulated to mediate insulin control of glycogen metabolism. However, we recently
showed (Suzuki, Y., Lanner, C., Kim, J.-H., Vilardo, P. G., Zhang,
H., Jie Yang, J., Cooper, L. D., Steele, M., Kennedy, A., Bock,
C., Scrimgeour, A., Lawrence, J. C. Jr., L., and
DePaoli-Roach, A. A. (2001) Mol. Cell. Biol. 21, 2683-2694) that insulin activates GS in muscle of
RGL(GM) knockout (KO) mice similarly to the
wild type (WT). To determine whether PP1G is involved in glycogen
metabolism during muscle contractions, RGL KO and
overexpressors (OE) were subjected to two models of contraction,
in vivo treadmill running and in situ
electrical stimulation. Both procedures resulted in a 2-fold increase
in the GS
The Muscle-specific Protein Phosphatase
PP1G/RGL(GM) Is Essential for Activation of
Glycogen Synthase by Exercise*
§,
,,,,, and
Research Division, Joslin Diabetes Center
and Harvard Medical School, Boston, Massachusetts 02215 and the
¶ Department of Biochemistry and Molecular Biology and the
** Krannert Institute of Cardiology, Indiana University
School of Medicine, Indianapolis, Indiana 46202
/+ glucose-6-P activity ratio in WT mice, but this response
was completely absent in the KO mice. The KO mice, which also have a
reduced GS activity associated with significantly reduced basal
glycogen levels, exhibited impaired maximal exercise capacity, but
contraction-induced activation of glucose transport was unaffected. The
RGL OE mice are characterized by enhanced GS activity ratio
and an ~3-4-fold increase in glycogen content in skeletal muscle.
These animals were able to tolerate exercise normally. Stimulation of
GS and glucose uptake following muscle contraction was not
significantly different as compared with WT littermates. These results
indicate that although PP1G/RGL is not necessary for
activation of GS by insulin, it is essential for regulation of glycogen
metabolism under basal conditions and in response to contractile
activity, and may explain the reduced muscle glycogen content in the
RGL KO mice, despite the normal insulin activation of
GS.
*
This work was supported in part by National Institutes of
Health Grant DK36569, by a research grant from the American Diabetes Association (to A. D. P. R.), and by National Institutes of Health Grants AR45670 and AR42238 (to L. J. G.).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.
Present address: Dept. of Medical Genetics, Tohoku University
School of Medicine, 1-1 Seiryomachi Aoba-ku, Sendai 980-8574, Japan.
To whom correspondence should be addressed: Dept. of
Biochemistry and Molecular Biology, Indiana University School of
Medicine, 635 Barnhill Dr., Indianapolis, IN 46202-5122. Tel.:
317-274-1585; Fax: 317-274-4686; E-mail:
adepaoli@iupui.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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