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ESR1 — SMAD2

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

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: ESR1 — SMAD2 (physical association, affinity chromatography technology) Matsuda et al., J Biol Chem 2001
• IRef Biogrid Interaction: ESR1 — SMAD2 (physical association, affinity chromatography technology) Ito et al., J Biol Chem 2010*
• IRef Biogrid Interaction: ESR1 — SMAD2 (direct interaction, pull down) Ito et al., J Biol Chem 2010*
• IRef Hprd Interaction: ESR1 — SMAD2 (in vitro) Matsuda et al., J Biol Chem 2001
• IRef Ophid Interaction: SMAD2 — ESR1 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Montague et al., Circ Res 2006 : ERalpha expression and activation reduced the phosphorylation of Smad2 , a signaling molecule important in differentiation of SMC and initiated cell death through cleavage of caspase-3
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