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Originally published In Press as doi:10.1074/jbc.M105470200 on August 24, 2001

J. Biol. Chem., Vol. 276, Issue 47, 43915-43923, November 23, 2001
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Characterization of Glucokinase-binding Protein Epitopes by a Phage-displayed Peptide Library
IDENTIFICATION OF 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE AS A NOVEL INTERACTION PARTNER*

Simone BaltruschDagger , Sigurd LenzenDagger , David A. Okar§, Alex J. Lange§, and Markus TiedgeDagger **

From the Dagger  Institute of Clinical Biochemistry, Hannover Medical School, 30623 Hannover, Germany and the § Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455

The low affinity glucose-phosphorylating enzyme glucokinase shows the phenomenon of intracellular translocation in beta cells of the pancreas and the liver. To identify potential binding partners of glucokinase by a systematic strategy, human beta cell glucokinase was screened by a 12-mer random peptide library displayed by the M13 phage. This panning procedure revealed two consensus motifs with a high binding affinity for glucokinase. The first consensus motif, LSAXXVAG, corresponded to the glucokinase regulatory protein of the liver. The second consensus motif, SLKVWT, showed a complete homology to the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2), which acts as a key regulator of glucose metabolism. Through yeast two-hybrid analysis it became evident that the binding of glucokinase to PFK-2/FBPase-2 is conferred by the bisphosphatase domain, whereas the kinase domain is responsible for dimerization. 5'-Rapid amplification of cDNA ends analysis and Northern blot analysis revealed that rat pancreatic islets express the brain isoform of PFK-2/FBPase-2. A minor portion of the islet PFK-2/FBPase-2 cDNA clones comprised a novel splice variant with 8 additional amino acids in the kinase domain. The binding of the islet/brain PFK-2/ FBPase-2 isoform to glucokinase was comparable with that of the liver isoform. The interaction between glucokinase and PFK-2/FBPase-2 may provide the rationale for recent observations of a fructose-2,6-bisphosphate level-dependent partial channeling of glycolytic intermediates between glucokinase and glycolytic enzymes. In pancreatic beta cells this interaction may have a regulatory function for the metabolic stimulus-secretion coupling. Changes in fructose-2,6-bisphosphate levels and modulation of PFK-2/FBPase-2 activities may participate in the physiological regulation of glucokinase-mediated glucose-induced insulin secretion.

* This work was supported by a grant from the Deutsche Forschungsgemeinschaft (to S. L.), a Research Award from the American Diabetes Association (to D. A. O.), and Research Grant 198236 from the Juvenile Diabetes Research Foundation International and National Institutes of Health Grant DK-38354 (to A. J. L.).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.

Some of the results were obtained during thesis work by this author.

** To whom correspondence should be addressed: Inst. of Clinical Biochemistry, Hannover Medical School, D-30623 Hannover, Germany. E-mail: tiedge.markus@mh-hannover.de.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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