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(Received for publication, March 27, 1997)
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From the To understand the insulin-induced activation of
6-phosphofructo-2-kinase (PFK-2) of the bifunctional enzyme
PFK-2/fructose-2,6-bisphosphatase in heart, the effect of
phosphorylation by protein kinases of the insulin signaling pathways on
PFK-2 activity was studied. Purified PFK-2/fructose-2,6-bisphosphatase
from bovine heart is a mixture of two isoforms
(Mr 58,000 and 54,000 on SDS-polyacrylamide gels). The Mr 54,000 protein is an
alternatively spliced form, lacking phosphorylation sites for protein
kinases. Recombinant enzymes corresponding to the
Mr 58,000 (BH1) and Mr
54,000 (BH3) forms were expressed and used as substrates for
phosphorylation. The recombinant BH1 isoform was phosphorylated by p70
ribosomal S6 kinase (p70s6k), mitogen-activated protein
kinase-activated protein kinase-1, and protein kinase B (PKB), whereas
the recombinant BH3 isoform was a poor substrate for these protein
kinases. Treatment with all protein kinases activated PFK-2 in the
recombinant BH1 preparation. Phosphorylation of the recombinant BH1
isoform correlated with PFK-2 activation and was reversed by treatment
with protein phosphatase 2A. All the protein kinases phosphorylated
Ser-466 and Ser-483 in the BH1 isoform, but to different extents:
p70s6k preferentially phosphorylated Ser-466, whereas
mitogen-activated protein kinase-activated protein kinase-1 and PKB
phosphorylated Ser-466 and Ser-483 to a similar extent. We propose that
PKB is part of the insulin signaling cascade for PFK-2 activation in heart.
Hormone and Metabolic Research Unit,
Institute of Cellular and Molecular Pathology and the Louvain
University Medical School, Avenue Hippocrate, 75, 1200 Brussels,
Belgium and the ¶ Medical Research Council Protein Phosphorylation
Unit, Department of Biochemistry, University of Dundee,
Dundee, DD1 4HN, Scotland
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D. R. Plas, S. Talapatra, A. L. Edinger, J. C. Rathmell, and C. B. Thompson Akt and Bcl-xL Promote Growth Factor-independent Survival through Distinct Effects on Mitochondrial Physiology J. Biol. Chem., April 6, 2001; 276(15): 12041 - 12048. [Abstract] [Full Text] [PDF]
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G. G. Choudhury Akt Serine Threonine Kinase Regulates Platelet-derived Growth Factor-induced DNA Synthesis in Glomerular Mesangial Cells. REGULATION OF c-fos AND p27kip1 GENE EXPRESSION J. Biol. Chem., September 14, 2001; 276(38): 35636 - 35643. [Abstract] [Full Text] [PDF]
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D. Brodbeck, M. M. Hill, and B. A. Hemmings Two Splice Variants of Protein Kinase Bgamma Have Different Regulatory Capacity Depending on the Presence or Absence of the Regulatory Phosphorylation Site Serine 472 in the Carboxyl-terminal Hydrophobic Domain J. Biol. Chem., July 27, 2001; 276(31): 29550 - 29558. [Abstract] [Full Text] [PDF]
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