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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Detalles Bibliográficos
Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4778718/
https://www.ncbi.nlm.nih.gov/pubmed/26235616
http://dx.doi.org/10.1016/j.celrep.2015.07.004

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4778718/
https://www.ncbi.nlm.nih.gov/pubmed/26235616
http://dx.doi.org/10.1016/j.celrep.2015.07.004

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