title: A proteomic snapshot of the human heat shock protein 90 interactome.
abstract: Heat shock protein 90 (Hsp90) is a molecular chaperone which modulates several signalling pathways within a cell. By applying co-immunoprecipitation with endogeneous Hsp90, we were able to identify 39 novel protein interaction partners of this chaperone in human embryonic kidney cells (HEK293). Interestingly, levels of DNA-activated protein kinase catalytic subunit, an Hsp90 interaction partner found in this study, were found to be sensitive to Hsp90 inhibitor treatment only in HeLa cells but not in HEK293 cells referring to the tumorgenicity of this chaperone.
authors.affiliation: Institute of Pharmaceutical Sciences, University of Graz, Universitätsplatz 1, 8010 Graz, Austria.
authors.forename: S Fabio
authors.initials: SF
authors.lastname: Falsone
authors.forename: Bernd
authors.initials: B
authors.lastname: Gesslbauer
authors.forename: Florian
authors.initials: F
authors.lastname: Tirk
authors.forename: Anna-Maria
authors.initials: AM
authors.lastname: Piccinini
authors.forename: Andreas J
authors.initials: AJ
authors.lastname: Kungl
mesh_terms: D051747:DNA-Activated Protein Kinase / Q000378:metabolism*; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D047468:Immunoprecipitation; D021122:Protein Subunits / Q000378:metabolism; D040901:Proteomics
chemical_list: D018841:HSP90 Heat-Shock Proteins; D021122:Protein Subunits; D051747:DNA-Activated Protein Kinase