The role of Hsp90N, a new member of the Hsp90 family, in signal transduction and neoplastic transformation.

@article{Grammatikakis2002TheRO,
  title={The role of Hsp90N, a new member of the Hsp90 family, in signal transduction and neoplastic transformation.},
  author={Nicholas Grammatikakis and Adina Vultur and Chilakamarti V. Ramana and Aliki Siganou and Clifford W. Schweinfest and Dennis K. Watson and Leda Raptis},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 10},
  pages={8312-20}
}
The 90-kDa heat shock protein (Hsp90), the target of the ansamycin class of anti-cancer drugs, is required for the conformational activation of a specific group of signal transducers, including Raf-1. In this report we have identified a 75-kDa Raf-associated protein as Hsp90N, a novel member of the Hsp90 family. Intriguingly, the ansamycin-binding domain is replaced in Hsp90N by a much shorter, hydrophobic sequence, preceded by a putative myristylation signal. We demonstrate that, although much… CONTINUE READING

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