GC box binding induces phosphorylation of Sp1 by a DNA-dependent protein kinase

Jackson, Stephen; MacDonald, Judy J.; Lees‐Miller, Susan P.; Tjian, Robert

doi:10.1016/0092-8674(90)90296-q

Cited by 647 publications

(443 citation statements)

References 34 publications

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“…The Sp1 antibody detected two polypeptide species with apparent molecular masses of 95 kD and 105 kD, which is most probably due to di erential phosphorylation (Jackson et al, 1990). During the time course of PDGF-BB treatment of the cells, we observed no signi®cant change in Sp1 expression level suggesting that Sp1 is constitutively expressed in NIH3T3 cells (Figure 3a).…”

Section: Identi®cation Of Sequences From the 5'-¯anking Region Of Thementioning

confidence: 87%

“…Recently it was shown that ternary complex factor Sap-1a interacts with the coactivator CBP, which functionally coactivates Sap-1a-dependent transcription upon Sap1a phosphorylation by mitogen-activated kinase . Although Sp1 becomes phosphorylated by a nuclear DNA-dependent protein kinase within its transcriptional activation domains upon SV40 infection of cells (Jackson et al, 1990), the involvement of Sp1 phosphorylation in transactivation of target genes upon PDGF-stimulation remains to be elucidated.…”

Section: Discussionmentioning

confidence: 99%

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Sp1 recognition sites in the proximal promoter of the human vascular endothelial growth factor gene are essential for platelet-derived growth factor-induced gene expression

Finkenzeller

Sparacio

Technau³

et al. 1997

Oncogene

182

170

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Stimulation of NIH3T3 cells with platelet-derived growth factor (PDGF)-BB enhances expression of vascular endothelial growth factor (VEGF), an endothelial cell-speci®c mitogen and a key mediator of tumor angiogenesis. Here, we identi®ed cis-acting VEGF promoter elements and trans-acting factors which are involved in PDGF-stimulated VEGF expression. By 5'-deletion and transient transfection analysis, a G+C-rich region at 785 to 750 of the human VEGF promoter was shown to be necessary and su cient for both PDGF inducible and basal expression. The region contains three potential recognition sites for Sp1 transcription factors, which overlap with two Egr-1 sites. Mutations that abolish the ability of Sp1 to interact with the VEGF promoter element also abrogate expression induced by PDGF. Mutations of the potential Egr-1 binding sites did not a ect PDGF responsiveness. Gel shift and antibody supershift analyses showed that Sp1 and Sp3 interact constitutively with the VEGF promoter element. Our data strongly suggest that enhanced VEGF gene expression in PDGF-induced NIH3T3 cells is mediated by Sp1 and/or Sp3 transcription factors bound to the 785 to 750 promoter region of the VEGF gene.

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Section: Identi®cation Of Sequences From the 5'-¯anking Region Of Thementioning

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Sp1 recognition sites in the proximal promoter of the human vascular endothelial growth factor gene are essential for platelet-derived growth factor-induced gene expression

Finkenzeller

Sparacio

Technau³

et al. 1997

Oncogene

182

170

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“…The mechanism for increased stability of Sp1 is not clear. Sp1 undergoes post-translational modi®cations such as phosphorylation and glycosylation (Jackson et al, 1990;Jackson and Tjian, 1988). Glycosylation may aid in nuclear localization and DNA binding while phosphorylation may assist in stabilizing the Sp1-DNA complex.…”

Section: Discussionmentioning

confidence: 99%

Repression of transforming growth factor-β receptor type I promoter expression by Sp1 deficiency

Periyasamy

Ammanamanchi²,

Tillekeratne

et al. 2000

Oncogene

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In this report, we describe the mechanism of TGF-b receptor type I (RI) repression in the GEO human colon carcinoma cells. Treatment of GEO cells with the DNA methyltransferase inhibitor, 5 azacytidine induced RI expression and restored TGF-b response. A stably transfected RI promoter-reporter construct (RI-Luc) expressed higher activity in the 5 aza C treated GEO cells, suggesting the activation of a transactivator for RI transcription. Gel shift analysis indicated enhanced binding of proteins from the 5 aza C treated nuclear extracts to radiolabeled Sp1 oligonucleotides speci®cally contained in the RI promoter. Protein stability studies after cyclohexamide treatment suggested an increase in the Sp1 protein stability from the 5 aza C treated GEO cells. Further, transfection of Sp1 cDNA into untreated GEO control cells increased RI promoter activity and thus induced RI expression. 5 aza C mediated Sp1 expression in Sp1 de®cient GEO colon and MCF-7 breast cancer cells also enhanced the activity of several other Sp1 dependent promoters such as TGFb receptor type II (RII), Cyclin A and p21/waf1/cip1. These results indicate that restoration of Sp1 in several di erent types of Sp1 de®cient cells leads to enhanced activation of a wide range of Sp1 dependent promoters. Oncogene (2000) 19, 4660 ± 4667.

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“…Furthermore, little is known about the regulation of Sp1-related factors. Sp1 has been shown to be the substrate for a double-stranded DNA-dependent protein kinase (Jackson et al, 1990). In addition, Sp1 is phosphorylated in T lymphocytes stimulated with okadaic acid (Vlach et al, 1995) and in vitro by the cAMP-dependent protein kinase (PKA) (Rohl et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Cooperation of Sp1 and p300 in the induction of the CDK inhibitor p21WAF1/CIP1 during NGF-mediated neuronal differentiation

et al. 1999

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Addition of nerve growth factor (NGF) to PC12 cells promotes neuronal di erentiation while inhibiting cell proliferation. In order to understand how NGF exerts its antimitogenic e ect during di erentiation, we have studied the mechanism by which this factor activates the promoter of the CDK inhibitor p21 WAF1/CIP1 . The minimal region of the p21 promoter required for the NGF-induction was mapped to a contiguous stretch of 10 bp located 83 bases upstream of the transcription initiation site. This GC-rich region was shown to interact speci®cally with the transcription factor Sp1 and the related protein Sp3, in either exponentiallygrowing or NGF-treated PC12 cells. The addition of NGF resulted in an accumulation of the transcriptional co-activator p300 in complexes associated with the NGF-responsive region. Transcriptional activity of Sp1, Sp3 and p300 was speci®cally induced by NGF in a Gal4-fusion assay, indicating that induction of p21 during neuronal di erentiation may involve regulation of the activity of these factors by NGF. Furthermore, p300 was able to act as a co-activator for Sp1-mediated transcriptional activation in PC12 cells, suggesting that p300 and Sp1 may cooperate in activating p21 transcription during the withdrawal of neuronal precursors from the cell cycle. This hypothesis is supported by experiments showing that p300 and Sp1 form complexes in PC12 cells.

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GC box binding induces phosphorylation of Sp1 by a DNA-dependent protein kinase

Cited by 647 publications

References 34 publications

Sp1 recognition sites in the proximal promoter of the human vascular endothelial growth factor gene are essential for platelet-derived growth factor-induced gene expression

Sp1 recognition sites in the proximal promoter of the human vascular endothelial growth factor gene are essential for platelet-derived growth factor-induced gene expression

Repression of transforming growth factor-β receptor type I promoter expression by Sp1 deficiency

Cooperation of Sp1 and p300 in the induction of the CDK inhibitor p21WAF1/CIP1 during NGF-mediated neuronal differentiation

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