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ESR1 — SP1

Pathways - manually collected, often from reviews:

• FastForward regulation: SP1 → ESR1 (transcriptional regulation, unknown)
  Evidence: DNABINDING, PROMACTIVITY, REG
• FastForward regulation: SP1 → ESR1 (transcriptional regulation, increase) Huang et al., J Biol Chem 2006*
  Evidence: DNABINDING, PROMACTIVITY, REG
• FastForward regulation: SP1 → ESR1 (transcriptional regulation, increase) deGraffenried et al., J Steroid Biochem Mol Biol 2002*
  Evidence: DNABINDING, PROMACTIVITY, REG
• NCI Pathway Database Regulation of nuclear SMAD2/3 signaling: SMAD3/SMAD4/ER alpha complex (SMAD3-SMAD4-ESR1) → SMAD3/SMAD4/SP1 complex (SMAD3-SMAD4-SP1) (transcription, inhibits)
  Poncelet et al., J Biol Chem 2001*, Matsuda et al., J Biol Chem 2001
  Evidence: mutant phenotype, reporter gene, physical interaction
• NCI Pathway Database FOXA1 transcription factor network: E2/ERA complex (ESR1) → SP1 (SP1) (transcription, activates) Eeckhoute et al., Genes Dev 2006
  Evidence: mutant phenotype, reporter gene, physical interaction

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: ESR1 — SP1 (direct interaction, pull down) Saville et al., J Biol Chem 2000*
• IRef Biogrid Interaction: ESR1 — SP1 (physical association, affinity chromatography technology) Li et al., Endocrinology 2007*
• IRef Biogrid Interaction: ESR1 — SP1 (physical association, affinity chromatography technology) Itoh et al., J Immunol 2007*
• IRef Biogrid Interaction: ESR1 — SP1 (colocalization, imaging technique) Koslowski et al., J Biol Chem 2009*
• IRef Biogrid Interaction: ESR1 — SP1 (physical association, affinity chromatography technology) Jin et al., J Biol Chem 2008
• IRef Biogrid Interaction: ESR1 — SP1 (physical association, affinity chromatography technology) Dong et al., J Biol Chem 2006*
• IRef Biogrid Interaction: ESR1 — SP1 (direct interaction, pull down) Castet et al., Mol Endocrinol 2006*
• IRef Biogrid Interaction: ESR1 — SP1 (colocalization, imaging technique) He et al., Mol Biol Cell 2005*
• IRef Biogrid Interaction: ESR1 — SP1 (physical association, affinity chromatography technology) He et al., Mol Biol Cell 2005*
• IRef Biogrid Interaction: ESR1 — SP1 (physical association, affinity chromatography technology) Varshochi et al., J Biol Chem 2005*
• IRef Biogrid Interaction: ESR1 — SP1 (direct interaction, pull down) Petz et al., J Steroid Biochem Mol Biol 2004*
• MIPS CORUM ESR1-SP1 complex: ESR1-SP1 complex complex (ESR1-SP1) Saville et al., J Biol Chem 2000*
• IRef Hprd Interaction: ESR1 — SP1 (in vivo) Wang et al., Mol Endocrinol 1999*, Kim et al., Mol Endocrinol 2005*
• IRef Hprd Interaction: ESR1 — SP1 (in vitro) Wang et al., Mol Endocrinol 1999*, Kim et al., Mol Endocrinol 2005*
• IRef Intact Interaction: ESR1 — SP1 (direct interaction, pull down) Porter et al., Mol Endocrinol 1997*
• IRef Intact Interaction: ESR1 — SP1 (direct interaction, cross-linking study) Porter et al., Mol Endocrinol 1997*

Text-mined interactions from Literome

Qin et al., Endocrinology 1999 : Wild-type human estrogen receptor did not bind directly to the IGFBP-4 oligonucleotides ; however, human estrogen receptor enhanced Sp1-DNA binding in a concentration dependent manner
Wang et al., Mol Endocrinol 1999 (Breast Neoplasms) : The estrogen receptor ( ER ) protein enhanced Sp1 interactions with upstream GC-rich sites, and interactions of ER, Sp1, and ER/Sp1 with downstream DNA bound-NF-Y was investigated by kinetic analysis for protein-DNA binding ( on- and off-rates ), coimmunoprecipitation, and pulldown assays using wild-type and truncated glutathione S-transferase (GST)-Sp1 chimeric proteins
Salvatori et al., Endocrinology 2000 : ERalpha does not bind this imperfect thyroid hormone response element half-site but is able to enhance binding of Sp1 to its site, in gel mobility shift assays, suggesting that the mechanism by which the receptor stimulated the transcription involved protein-protein interactions that replaced DNA binding
Petz et al., Mol Endocrinol 2000 (Breast Neoplasms) : In vitro DNase I footprinting and gel mobility shift assays demonstrated that Sp1 present in MCF-7 nuclear extracts and purified Sp1 protein bound to the two Sp1 sites and that the estrogen receptor enhanced Sp1 binding
deGraffenried et al., J Steroid Biochem Mol Biol 2002 : Sp1 is essential for estrogen receptor alpha gene transcription
Schultz et al., Mol Cell Endocrinol 2003 (Breast Neoplasms) : Mutation of either Sp1 site decreases Sp1-DNA complex formation and ERalpha mediated transactivation ... ERalpha enhances Sp1 binding, but does not interact directly with the -80/-34 region
deGraffenried et al., Breast Cancer Res Treat 2004 (Breast Neoplasms) : Regulation of the estrogen receptor alpha minimal promoter by Sp1 , USF-1 and ERalpha
Mukherjee et al., Biochim Biophys Acta 2005 : We further demonstrated that ERalpha but not ERbeta was responsible for the estrogen mediated Sp1 activation
Dong et al., Mol Endocrinol 2007 (Breast Neoplasms) : Moreover, it was indicated that estrogen stimulated PADI4 expression through binding of estrogen receptor (ER)-alpha to the upstream of the PADI4 gene and ERalpha mediated enhancement of activator protein-1, Sp1 , and nuclear factor-Y levels
Jin et al., PloS one 2012 : We further found that estrogen receptor a ( ERa ) , a known Sp1 co-activator, could potentiate GC-boxes containing MGARP promoter activity and this effect is mediated by Sp1