Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function.

@article{Basso2002AktFA,
  title={Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function.},
  author={Andrea D. Basso and David B. Solit and Gabriela Chiosis and Banabihari B Giri and Philip N Tsichlis and Neal Rosen},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 42},
  pages={39858-66}
}
Hsp90 is a chaperone required for the conformational maturation of certain signaling proteins including Raf, cdk4, and steroid receptors. Natural products and synthetic small molecules that bind to the ATP-binding pocket in the amino-terminal domain of Hsp90 inhibit its function and cause the degradation of these client proteins. Inhibition of Hsp90 function in cells causes down-regulation of an Akt kinase-dependent pathway required for D-cyclin expression and retinoblastoma protein-dependent G… CONTINUE READING
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