The Hsp90 inhibitor geldanamycin abrogates colocalization of eIF4E and eIF4E-transporter into stress granules and association of eIF4E with eIF4G.

@article{Suzuki2009TheHI,
  title={The Hsp90 inhibitor geldanamycin abrogates colocalization of eIF4E and eIF4E-transporter into stress granules and association of eIF4E with eIF4G.},
  author={Yukari Suzuki and Michiko Minami and Miho Suzuki and Keiko Abe and Shuhei Zenno and Masafumi Tsujimoto and Ken Matsumoto and Yasufumi Minami},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 51},
  pages={35597-604}
}
The eukaryotic translation initiation factor eIF4E plays a critical role in the control of translation initiation through binding to the mRNA 5' cap structure. eIF4E is also a component of processing bodies and stress granules, which are two types of cytoplasmic RNA granule in which translationally inactivated mRNAs accumulate. We found that treatment with the Hsp90 inhibitor geldanamycin leads to a substantial reduction in the number of HeLa cells that contain processing bodies. In contrast… CONTINUE READING

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An Hsp90 Inhibitor Abrogates eIF4E Activities 35604 JOURNAL OF BIOLOGICAL CHEMISTRY

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