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Phosphorylation of the Translational Repressor PHAS-I by the Mammalian Target of Rapamycin

Brunn, Gregory J., Hudson, Christine C., Sekulić, Aleksandar, Williams, Josie M., Hosoi, Hajime, Houghton, Peter J., Lawrence, John C., Abraham, Robert T.·1997·Science
DOI 10.1126/science.277.5322.99
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Abstract

The immunosuppressant rapamycin interferes with G 1 -phase progression in lymphoid and other cell types by inhibiting the function of the mammalian target of rapamycin (mTOR). mTOR was determined to be a terminal kinase in a signaling pathway that couples mitogenic stimulation to the phosphorylation of the eukaryotic initiation factor (eIF)-4E–binding protein, PHAS-I. The rapamycin-sensitive protein kinase activity of mTOR was required for phosphorylation of PHAS-I in insulin-stimulated human embryonic kidney cells. mTOR phosphorylated PHAS-I on serine and threonine residues in vitro, and these modifications inhibited the binding of PHAS-I to eIF-4E. These studies define a role for mTOR in translational control and offer further insights into the mechanism whereby rapamycin inhibits G 1 -phase progression in mammalian cells.

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Research works printed but not linked: 33

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Metadata

Authors
Brunn, G. J., Hudson, C. C., Sekulić, A., Williams, J. M., Hosoi, H., Houghton, P. J., Lawrence, J. C., & Abraham, R. T.
Affiliations
G. J. Brunn and J. C. Lawrence Jr., Departments of Pharmacology and Medicine, University of Virginia School of Medicine, Charlottesville, VA 22908, USA.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1997-07-04
Volume
277
Issue
5322
Pages
99-101
ISSN
  • 0036-8075
  • 1095-9203
DOI
10.1126/science.277.5322.99
Cited by
846
References
1
Language
en

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