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J Biol Chem, Vol. 274, Issue 3, 1207-1215, January 15, 1999
From the Department of Pharmacology and Therapeutics, Roswell Park
Cancer Institute, Buffalo, New York 14263
Sp1 sites can mediate growth/cell cycle induction
of dihydrofolate reductase in late G1 (Jensen,
D. E., Black, A. R. Swick, A. G., and Azizkhan, J. C. (1997) J. Cell. Biochem. 67, 24-31). To
investigate mechanisms underlying this induction, effects of serum
stimulation on regulation of Sp1 were examined. In Balb/c 3T3 cells,
serum stimulation did not affect Sp1 synthesis or the relative binding
of Sp1 family members to DNA; however, it did result in a rapid,
~2-fold increase in Sp1 levels and an ~3-fold increase in specific
Sp1 phosphorylation in mid-G1. In normal human diploid
fibroblasts, serum stimulation also increased Sp1 phosphorylation in
mid-G1 but did not affect Sp1 levels. Therefore, Sp1
phosphorylation is regulated in a growth/cell
cycle-dependent manner which correlates temporally with
induction of dihydrofolate reductase transcription. Further studies
revealed a kinase activity specifically associated with Sp1 in a
growth-regulated manner. This activity is distinct from purified
kinases previously shown to phosphorylate Sp1 in vitro and
phosphorylates Sp1 between amino acids 612 and 678 in its C terminus, a
region also phosphorylated in mid-G1 in vivo.
Therefore, this study indicates that phosphorylation of the C terminus
of Sp1 may play a role in the cell cycle regulation of its
transcriptional activity.
Growth/Cell Cycle Regulation of Sp1 Phosphorylation
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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