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HSP90AA1 — MAPK15

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

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: MAPK15 — HSP90AA1 (physical association, affinity chromatography technology) Taipale et al., Cell 2012
• IRef Intact Interaction: Complex of 30 proteins (association, tandem affinity purification) Varjosalo et al., Nat Methods 2013

Text-mined interactions from Literome

Citri et al., J Biol Chem 2006 : Analyzing Hsp90 regulation of two major signaling cascades, the mitogen activated protein kinase and phosphatidylinositol 3-kinase, leads us to propose that the selectivity of the chaperone to specific kinases is functional, namely that Hsp90 controls kinases that function as hubs integrating multiple inputs
LaFayette et al., PLoS Pathog 2010 : We identified an additional level of regulatory control in the C. albicans circuitry linking PKC signaling, Hsp90, and calcineurin as genetic reduction of Hsp90 led to depletion of the terminal MAPK , Mkc1. Deletion of C. albicans PKC1 rendered fungistatic ergosterol biosynthesis inhibitors fungicidal and attenuated virulence in a murine model of systemic candidiasis
Antonopoulou et al., Comp Biochem Physiol A Mol Integr Physiol 2013 (MAP Kinase Signaling System) : In the white muscle, Hsp90 levels decreased and the phosphorylation of p38 MAPK increased in both feeding regimes compared to control