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HSP90AA1 — LRRK2

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

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: LRRK2 — HSP90AA1 (physical association, affinity chromatography technology) Nichols et al., Biochem J 2010
• IRef Biogrid Interaction: LRRK2 — HSP90AA1 (physical association, affinity chromatography technology) Wang et al., J Neurosci 2008*
• IRef Biogrid Interaction: LRRK2 — HSP90AA1 (direct interaction, enzymatic study) Zach et al., PloS one 2010*
• IRef Biogrid Interaction: LRRK2 — HSP90AA1 (physical association, affinity chromatography technology) Dächsel et al., Parkinsonism Relat Disord 2007
• IRef Biogrid Interaction: LRRK2 — HSP90AA1 (physical association, affinity chromatography technology) Sen et al., J Biol Chem 2009*
• IRef Biogrid Interaction: LRRK2 — HSP90AA1 (physical association, affinity chromatography technology) Gloeckner et al., Hum Mol Genet 2006*
• IRef Biogrid Interaction: LRRK2 — HSP90AA1 (physical association, affinity chromatography technology) Rudenko et al., Biochem J 2012*
• IRef Biogrid Interaction: LRRK2 — HSP90AA1 (physical association, affinity chromatography technology) Ding et al., PloS one 2009*
• IRef Intact Interaction: Complex of YWHAG-YWHAB-CDC37-LRRK2-YWHAE-HSP90AA1-HSP90AB1-YWHAQ-YWHAZ (association, anti tag coimmunoprecipitation) Nichols et al., Biochem J 2010
• IRef Intact Interaction: Complex of LRRK2-HSP90AA1-HSP90AB1-CDC37-YWHAH-YWHAZ-YWHAQ-YWHAB-YWHAE (association, anti tag coimmunoprecipitation) Nichols et al., Biochem J 2010
• IRef Intact Interaction: Complex of 16 proteins (association, anti tag coimmunoprecipitation) Dächsel et al., Parkinsonism Relat Disord 2007
• IRef Intact Interaction: Complex of 39 proteins (association, anti tag coimmunoprecipitation) Liu et al., Nature 2012

Text-mined interactions from Literome

Wang et al., J Neurosci 2008 : Here we show that LRRK2 forms a complex with heat shock protein 90 (Hsp90) in vivo and that inhibition of Hsp90 disrupts the association of Hsp90 with LRRK2 and leads to proteasomal degradation of LRRK2
Rudenko et al., Biochem J 2012 (Parkinson Disease) : Hsp90 ( heat-shock protein of 90 kDa ) has an increased affinity for the G2385R variant compared with WT ( wild-type ) LRRK2, and inhibition of the chaperone binding combined with proteasome inhibition leads to association of mutant LRRK2 with high molecular mass native fractions that probably represent proteasome degradation pathways