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AHR — HSP90AA1

Pathways - manually collected, often from reviews:

• WikiPathways Aryl Hydrocarbon Receptor Pathway: Complex of SRC-AIP-AHR-HSP90AA1-PTGES3 → AHR (activation)
• WikiPathways Aryl Hydrocarbon Receptor: Complex of AIP-AHR-AIP-HSP90AA1-HSP90AA1 → CCL1 (mim-transcription-translation)
• WikiPathways Aryl Hydrocarbon Receptor: Complex of AIP-AHR-AIP-HSP90AA1-HSP90AA1 → CDC37 (activation) Enan et al., Biochem Pharmacol 1996*, Blankenship et al., Mol Pharmacol 1997*
• WikiPathways Aryl Hydrocarbon Receptor: Complex of AIP-AHR-AIP-HSP90AA1-HSP90AA1 → VEGFA (activation)
• WikiPathways Aryl Hydrocarbon Receptor: Complex of AIP-AHR-AIP-HSP90AA1-HSP90AA1 → ARNT/AHR (activation)
• WikiPathways Aryl Hydrocarbon Receptor: Complex of AIP-AHR → Complex of AIP-AHR-AIP-HSP90AA1-HSP90AA1 (activation)
  

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

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: AHR — HSP90AA1 (physical association, affinity chromatography technology) Ma et al., J Biol Chem 1997*
• IRef Dip Interaction: AHR — HSP90AA1 (physical association, coimmunoprecipitation) Gradin et al., J Biol Chem 1994*
• IRef Hprd Interaction: AHR — HSP90AA1 (in vivo) Chen et al., J Biol Chem 1994*, Ma et al., J Biol Chem 1997*
• IRef Hprd Interaction: Complex of HSP90AA1-AIP-AHR-AHR-HSP90AA1-AIP-AIP-HSP90AA1-AHR (in vivo) Carver et al., J Biol Chem 1997*, Carver et al., J Biol Chem 1998*
• IRef Ophid Interaction: AHR — HSP90AA1 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Caruso et al., Biochem Pharmacol 1999 (Breast Neoplasms) : Taken together, these results demonstrate that HSP90 can regulate AhR activity in vivo, and that Ah-responsiveness is dependent upon cellular ER content through a mechanism that involves HSP90
Soshilov et al., J Biol Chem 2011 : Interestingly, whereas Hsp90 binding residues within the ligand binding domain were not involved in Hsp90 dependent AhR protein stability, several of these residues are important for ligand dependent AhR activation, and their mutation resulted in conversion of two AhR antagonists/partial agonists into full AhR agonists