c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells

The ability of Heat Shock Protein 90 (Hsp90) to hydrolyze ATP is essential for its chaperone function. The co-chaperone Aha1 stimulates Hsp90 ATPase activity, tailoring the chaperone function to specific “client” proteins. The intracellular signaling mechanisms directly regulating Aha1 association w...

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Bibliographic Details
Main Authors: Dunn, Diana M., Woodford, Mark R., Truman, Andrew W., Jensen, Sandra M., Schulman, Jacqualyn, Caza, Tiffany, Remillard, Taylor C., Loiselle, David, Wolfgeher, Donald, Blagg, Brian S.J., Franco, Lucas, Haystead, Timothy A., Daturpalli, Soumya, Mayer, Matthias P., Trepel, Jane B., Morgan, Rhodri M.L., Prodromou, Chrisostomos, Kron, Stephen J., Panaretou, Barry, Stetler-Stevenson, William G., Landas, Steve K., Neckers, Len, Bratslavsky, Gennady, Bourboulia, Dimitra, Mollapour, Mehdi
Format: Online
Language:English
Published: 2015
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4778718/