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J. Biol. Chem., Vol. 268, Issue 24, 17811-17819, Aug, 1993
K Park and KH Kim
Insulin induction of acetyl-CoA carboxylase (ACC) and differentiation of
30A5 preadipocytes into adipocytes requires a brief exposure of the cells
to cAMP. Using the techniques of DNase I footprinting, DNA band shift, and
analysis of the point and deletion mutations, a region from - 113 to -95
has been identified as the site through which cAMP sensitizes the cell for
the response to insulin. One sequence-specific DNA-protein complex, b3, is
formed in the DNA-mobility shift assay when nuclear extract from 30A5 cells
is mixed with the oligonucleotide representing this region. Purified human
AP-2 also generates the complex corresponding to b3 with the same ACC PII
probe or with the AP- 2 consensus sequence probe from SV40 promoter.
Substitution of A for G in the sequence GGGGCTGGG abolishes the formation
of b3 sequence- specific complex. Stably transfected 30A5 cells with the
same mutations in the plasmid no longer respond to insulin in spite of
their exposure to cAMP. These results establish that the 21 base pair
region in ACC promoter II and the binding of AP-2 protein to this sequence
are required for cAMP action. cAMP-dependent protein kinase phosphorylates
AP-2 both in vitro and in vivo and the phosphorylation of AP-2 does not
affect its binding activity.
The site of cAMP action in the insulin induction of gene expression of acetyl-CoA carboxylase is AP-2
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907-1153.
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