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ESR1 — SMAD3

Pathways - manually collected, often from reviews:

• 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 Regulation of nuclear SMAD2/3 signaling: ER alpha (ESR1) → SMAD3/SMAD4 complex (SMAD3-SMAD4) (modification, collaborate)
  Matsuda et al., J Biol Chem 2001
  Evidence: mutant phenotype, reporter gene, physical interaction
• NCI Pathway Database Regulation of nuclear SMAD2/3 signaling: ER alpha (ESR1) → SMAD3/SMAD4/ER alpha complex (SMAD3-SMAD4-ESR1) (modification, collaborate)
  Matsuda et al., J Biol Chem 2001
  Evidence: mutant phenotype, reporter gene, physical interaction
• NCI Pathway Database Regulation of nuclear SMAD2/3 signaling: SMAD3/SMAD4 complex (SMAD3-SMAD4) → SMAD3/SMAD4/ER alpha complex (SMAD3-SMAD4-ESR1) (modification, collaborate)
  Matsuda et al., J Biol Chem 2001
  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 — SMAD3 (physical association, affinity chromatography technology) Ito et al., J Biol Chem 2010*
• IRef Hprd Interaction: ESR1 — SMAD3 (in vivo) Matsuda et al., J Biol Chem 2001
• IRef Hprd Interaction: ESR1 — SMAD3 (in vitro) Matsuda et al., J Biol Chem 2001

Text-mined interactions from Literome

Cherlet et al., Mol Cell Biochem 2007 (Breast Neoplasms) : Transient transfection of Cos1 cells with p3TP-lux, demonstrate that ERalpha and ERbeta ( 1 ) repress Smad3 transcriptional activity in an estradiol dependent manner and that this effect is inhibited by antiestrogen treatment
Ito et al., J Biol Chem 2010 (Breast Neoplasms...) : ERalpha mediated reductions in Smad levels did not require the DNA binding ability of ERalpha, implying that ERalpha opposes the effects of TGF-beta via a novel non-genomic mechanism ... Our analysis revealed that ERalpha formed a protein complex with Smad and the ubiquitin ligase Smurf, and enhanced Smad ubiquitination and subsequent degradation in an estrogen dependent manner