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J Biol Chem, Vol. 275, Issue 8, 5431-5440, February 25, 2000

Loss of the Major Isoform of Phosphoglucomutase Results in Altered Calcium Homeostasis in Saccharomyces cerevisiae*

Lianwu FuDagger , Attila MisetaDagger §, Dacia Hunton, Richard B. Marchase, and David M. BedwellDagger ||

From the Departments of Dagger  Microbiology and  Cell Biology, University of Alabama at Birmingham, Birmingham, Alabama 35294

Phosphoglucomutase (PGM) is a key enzyme in glucose metabolism, where it catalyzes the interconversion of glucose 1-phosphate (Glc-1-P) and glucose 6-phosphate (Glc-6-P). In this study, we make the novel observation that PGM is also involved in the regulation of cellular Ca2+ homeostasis in Saccharomyces cerevisiae. When a strain lacking the major isoform of PGM (pgm2Delta ) was grown on media containing galactose as sole carbon source, its rate of Ca2+ uptake was 5-fold higher than an isogenic wild-type strain. This increased rate of Ca2+ uptake resulted in a 9-fold increase in the steady-state total cellular Ca2+ level. The fraction of cellular Ca2+ located in the exchangeable pool in the pgm2Delta strain was found to be as large as the exchangeable fraction observed in wild-type cells, suggesting that the depletion of Golgi Ca2+ stores is not responsible for the increased rate of Ca2+ uptake. We also found that growth of the pgm2Delta strain on galactose media is inhibited by 10 µM cyclosporin A, suggesting that activation of the calmodulin/calcineurin signaling pathway is required to activate the Ca2+ transporters that sequester the increased cytosolic Ca2+ load caused by this high rate of Ca2+ uptake. We propose that these Ca2+-related alterations are attributable to a reduced metabolic flux between Glc-1-P and Glc-6-P due to a limitation of PGM enzymatic activity in the pgm2Delta strain. Consistent with this hypothesis, we found that this "metabolic bottleneck" resulted in an 8-fold increase in the Glc-1-P level compared with the wild-type strain, while the Glc-6-P and ATP levels were normal. These results suggest that Glc-1-P (or a related metabolite) may participate in the control of Ca2+ uptake from the environment.

* This work was supported by Grant JDF 99502 from the Juvenile Diabetes Foundation International.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 Clinical Chemistry, University Medical School, 7624 Pecs, Hungary.

|| To whom correspondence should be addressed: Dept. of Microbiology, Bevill Biomedical Research Bldg., Rm. 432, 845 19th St. S., University of Alabama at Birmingham, Birmingham, AL 35294-2170. Tel.: 205-934-6593; Fax: 205-975-5482; E-mail: dbedwell@uab.edu.

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