An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells.

@article{Ostrovsky2009AnER,
  title={An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells.},
  author={Olga Ostrovsky and Catherine A. Makarewich and Erik Lee Snapp and Yair Argon},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2009},
  volume={106 28},
  pages={11600-5}
}
Glucose-regulated protein 94 (GRP94) is an endoplasmic reticulum (ER) chaperone for which only few client proteins and no cofactors are known and whose mode of action is unclear. To decipher the mode of GRP94 action in vivo, we exploited our finding that GRP94 is necessary for the production of insulin-like growth factor (IGF)-II and developed a cell-based functional assay. Grp94(-/-) cells are hypersensitive to serum withdrawal and die. This phenotype can be complemented either with exogenous… CONTINUE READING

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References

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Showing 1-10 of 47 references

GRP 94 protects cells grown without serum from apoptosisby regulatingthesecretionof insulin - likegrowthfactor II

  • JJ Wassenberg, RC Reed, CV Nicchitta
  • MolBiolCell
  • 2009

GRP94 protects cells grown without serum from apoptosisby regulatingthesecretionof insulin-likegrowthfactor II.MolBiolCell20:1855– 1864

  • O Ostrovsky, NT Ahmed, Y Argon
  • 2009

Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages

  • Y Yang
  • Immunity
  • 2007

Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex

  • MM Ali
  • Nature
  • 2006

Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94

  • F Chu
  • Protein Sci 15:1260–1269
  • 2006

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