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Papers In Press, published online ahead of print March 7, 2001
Molecular Physiology & Biophysics, Vanderbilt University Medical School, Nashville, TN 37232
Corresponding Author: richard.obrien{at}mcmail.vanderbilt.edu
Glucose-6-phosphatase is a multi-component system that catalyzes the terminal step in gluconeogenesis. To examine the effect of the cAMP signal transduction pathway on expression of the gene encoding the mouse glucose-6-phosphatase catalytic subunit (G6Pase), the liver-derived HepG2 cell line was transiently cotransfected with a series of G6Pase-chloramphenicol acetyltransferase (CAT) fusion genes and an expression vector encoding the catalytic subunit of cAMP-dependent protein kinase (PKA). PKA markedly stimulated G6Pase-CAT fusion gene expression, and mutational analysis of the G6Pase promoter revealed that multiple cis-acting elements were required for this response. One of these elements was mapped to the G6Pase promoter region between ?114 and ?99, and this sequence was shown to bind hepatocyte nuclear factor (HNF-6). This HNF-6 binding site was able to confer a stimulatory effect of PKA on the expression of a heterologous fusion gene; a mutation that abolished HNF-6 binding also abolished the stimulatory effect of PKA. Further investigation revealed that PKA phosphorylated HNF-6 in vitro. Site-directed mutation of three consensus PKA phosphorylation sites in the HNF-6 carboxy-terminus markedly reduced this phosphorylation. These results suggest that the stimulatory effect of PKA on G6Pase fusion gene transcription in HepG2 cells may be mediated, in part, by phosphorylation of HNF-6.
J. Biol. Chem, 10.1074/jbc.M101442200
Submitted on February 14, 2001
Revised on March 2, 2001
Accepted on March 6, 2001
Protein kinase A phosphorylates hepatocyte nuclear factor-6 and stimulates glucose-6-phosphatase catalytic subunit gene transcription
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