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J Biol Chem, Vol. 273, Issue 32, 20175-20179, August 7, 1998
From Institut Cochin de Génétique Moléculaire,
USF1 and USF2 are ubiquitous transcription
factors of the basic helix-loop-helix leucine zipper family. They form
homo- and heterodimers and recognize a CACGTG motif termed E box. In
the liver, USF binding activity is mainly accounted for by the
USF1/USF2 heterodimer, which binds in vitro the
glucose/carbohydrate response elements (GlRE/ChoRE) of
glucose-responsive genes. To assign a physiological role of USFs
in vivo, we have undertaken the disruption of USF1 and USF2
genes in mice. We present here the generation of USF1-deficient mice.
In the liver of these mice, we demonstrate that USF2 remaining dimers
can compensate for glucose responsiveness, even though the level of
total USF binding activity is reduced by half as compared with wild
type mice. The residual USF1 binding activity was similarly reduced in
the previously reported USF2
Differential Roles of Upstream Stimulatory Factors 1 and 2 in the
Transcriptional Response of Liver Genes to Glucose
,
,
,
,
, and
U.129 INSERM Unité de Recherches en Physiologie et
Pathologie Génétiques et Moléculaires, and

U.257 INSERM Laboratoire de
Génétique Cellulaire et Moléculaire Université
René Descartes, 24 rue du Faubourg Saint-Jacques,
75014 Paris, France
/
mice in which an impaired glucose
responsiveness was observed (Vallet, V. S., Henrion, A. A.,
Bucchini, D., Casado, M., Raymondjean, M., Kahn, A., and Vaulont, S. (1997) J. Biol. Chem. 272, 21944-21949). Taken
together, these results clearly suggest differential transactivating efficiencies of USF1 and USF2 in promoting the glucose response. Furthermore, they support the view that USF2 is the functional transactivator of the glucose-responsive complex.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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