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HSP90AA1 — STIP1

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

Studies that report less than 10 interactions are marked with *

• IRef Bind Interaction: STIP1 — HSP90AA1
• IRef Bind_translation Interaction: STIP1 — HSP90AA1 (surface plasmon resonance)
• IRef Bind_translation Interaction: STIP1 — HSP90AA1 (two hybrid)
• IRef Biogrid Interaction: STIP1 — HSP90AA1 (direct interaction, pull down) Horibe et al., Journal of translational medicine 2011*
• IRef Biogrid Interaction: STIP1 — HSP90AA1 (physical association, affinity chromatography technology) Mollapour et al., Mol Cell 2010*
• IRef Biogrid Interaction: STIP1 — HSP90AA1 (direct interaction, pull down) Scheufler et al., Cell 2000*
• IRef Biogrid Interaction: STIP1 — HSP90AA1 (physical association, affinity chromatography technology) Johnson et al., J Biol Chem 1998*
• IRef Biogrid Interaction: STIP1 — HSP90AA1 (direct interaction, pull down) Li et al., Nature structural & molecular biology 2011
• IRef Biogrid Interaction: STIP1 — HSP90AA1 (direct interaction, pull down) Kundrat et al., Biochemistry 2010*
• IRef Biogrid Interaction: STIP1 — HSP90AA1 (physical association, affinity chromatography technology) Tsutsumi et al., Proc Natl Acad Sci U S A 2012*
• IRef Biogrid Interaction: STIP1 — HSP90AA1 (physical association, affinity chromatography technology) Sarkar et al., Int J Cancer 2013*
• IRef Biogrid Interaction: STIP1 — HSP90AA1 (physical association, affinity chromatography technology) Gano et al., Mol Cell Proteomics 2010
• IRef Biogrid Interaction: STIP1 — HSP90AA1 (physical association, affinity chromatography technology) Skarra et al., Proteomics 2011
• IRef Biogrid Interaction: STIP1 — HSP90AA1 (direct interaction, pull down) Brinker et al., J Biol Chem 2002*
• IRef Hprd Interaction: STIP1 — HSP90AA1 (in vivo) Scheufler et al., Cell 2000*
• IRef Hprd Interaction: STIP1 — HSP90AA1 (in vitro) Scheufler et al., Cell 2000*
• IRef Hprd Interaction: Complex of 26 proteins (in vivo) Dittmar et al., J Biol Chem 1997*, Dittmar et al., J Biol Chem 1997*
• IRef Intact Interaction: Complex of 29 proteins (association, anti tag coimmunoprecipitation) Skarra et al., Proteomics 2011
• IRef Intact Interaction: Complex of HSP90AA1-PPP5C-STIP1 (association, anti tag coimmunoprecipitation) Skarra et al., Proteomics 2011
• IRef Intact Interaction: Complex of PPP5C-HSPA1A-STIP1-HSP90AA1-PPP5C-CDC37-HSP90AB1-HSPA8-CCT4 (association, anti tag coimmunoprecipitation) Skarra et al., Proteomics 2011
• IRef Intact Interaction: Complex of 120 proteins (association, anti bait coimmunoprecipitation) Brazão et al., FEBS Lett 2012
• IRef Intact Interaction: Complex of 306 proteins (association, pull down) Komarova et al., Mol Cell Proteomics 2011
• IRef Intact Interaction: Complex of 203 proteins (association, cross-linking study) Byron et al., Proteomics 2012
• IRef Intact Interaction: Complex of 156 proteins (association, anti tag coimmunoprecipitation) Lau et al., Cell 2012
• IRef Ophid Interaction: STIP1 — HSP90AA1 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005
• IRef Ophid Interaction: STIP1 — HSP90AA1 (aggregation, confirmational text mining) Scheufler et al., Cell 2000*

Text-mined interactions from Literome

Song et al., J Biol Chem 2005 : Thus, Sti1p regulated Hsp70 and Hsp90 separately, Hsp90 is implicated as a TPR2b ligand, and mutations separately affecting regulation of either chaperone impair a pathway that is dependent upon both
Flom et al., Biochem J 2007 : As evidence for the role of Sti1 in mediating the interaction between Hsp70 and Hsp90 in vivo, we identified Sti1 mutants that result in reduced recovery of Hsp70 in Hsp90 complexes
Reidy et al., Mol Cell Biol 2010 : Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [ PSI+ ] prions by Hsp104
Lee et al., EMBO J 2012 : Dynamics of the regulation of Hsp90 by the co-chaperone Sti1 ... Our data suggest that Sti1 inhibits Hsp90 's ATPase activity by preventing N-terminal dimerization and docking of the N-terminal domain with the middle domain
Prodromou et al., EMBO J 1999 : The inherent ATPase activity of Hsp90 is completely inhibited by binding of Sti1 , but is not affected by Cpr6, although Cpr6 can reactivate the ATPase activity by displacing Sti1 from Hsp90