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J. Biol. Chem., Vol. 279, Issue 47, 49138-49150, November 19, 2004

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Degradation of the Gluconeogenic Enzymes Fructose-1,6-bisphosphatase and Malate Dehydrogenase Is Mediated by Distinct Proteolytic Pathways and Signaling Events^*

Guo-Chiuan Hung, C. Randell Brown, Allison B. Wolfe, Jingjing Liu, and Hui-Ling Chiang

From the Department of Cellular and Molecular Physiology, Penn State University College of Medicine, Hershey, Pennsylvania 17033

The key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) is subjected to catabolite inactivation and degradation when glucose-starved cells are replenished with fresh glucose. In various studies, the proteasome and the vacuole have each been reported to be the major site of FBPase degradation. Because different growth conditions were used in these studies, we examined whether variations in growth conditions could alter the site of FBPase degradation. Here, we demonstrated that FBPase was degraded outside the vacuole (most likely in the proteasome), when glucose was added to cells that were grown in low glucose media for a short period of time. By contrast, cells that were grown in the same low glucose media for longer periods of time degraded FBPase in the vacuole in response to glucose. Another gluconeogenic enzyme malate dehydrogenase (MDH2) showed the same degradation characteristics as FBPase in that the short term starvation of cells led to a non-vacuolar degradation, whereas long term starvation resulted in the vacuolar degradation of this protein. The N-terminal proline is required for the degradation of FBPase and MDH2 for both the vacuolar and non-vacuolar proteolytic pathways. The cAMP signaling pathway and the phosphorylation of glucose were needed for the vacuolar-dependent degradation of FBPase and MDH2. By contrast, the cAMP-dependent signaling pathway was not involved in the non-vacuolar degradation of these proteins, although the phosphorylation of glucose was required.

Received for publication, April 23, 2004 , and in revised form, August 25, 2004.

^* This work was supported by Public Health Services Grant RO1GM59480 from the National Institutes of Health (NIH) (to H.-L. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: Bldg. 8, Rm. 403, Laboratory of Biochemistry and Genetics, NIDDK/NIH, Bethesda, MD 20892-0830.

To whom correspondence should be addressed: Dept. of Cellular and Molecular Physiology, Penn State University College of Medicine, 500 University Dr., Hershey, PA 17033. Tel.: 717-531-0859; Fax: 717-531-7667; E-mail: crb13{at}psu.edu.

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