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PHAS-I as a Link Between Mitogen-Activated Protein Kinase and Translation Initiation
Abstract
PHAS-I is a heat-stable protein (relative molecular mass ≈ 12,400) found in many tissues. It is rapidly phosphorylated in rat adipocytes incubated with insulin or growth factors. Nonphosphorylated PHAS-I bound to initiation factor 4E (eIF-4E) and inhibited protein synthesis. Serine-64 in PHAS-I was rapidly phosphorylated by mitogen-activated (MAP) kinase, the major insulin-stimulated PHAS-I kinase in adipocyte extracts. Results obtained with antibodies, immobilized PHAS-I, and a messenger RNA cap affinity resin indicated that PHAS-I did not bind eIF-4E when serine-64 was phosphorylated. Thus, PHAS-I may be a key mediator of the stimulation of protein synthesis by the diverse group of agents and stimuli that activate MAP kinase.
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Self-citationeIF4 Initiation Factors: Effectors of mRNA Recruitment to Ribosomes and Regulators of Translation
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Metadata
- Authors
- Lin, T.-A., Kong, X., Haystead, T. A. J., Pause, A., Belsham, G., Sonenberg, N., & Lawrence, J. C.
- Venue
- Science
- Published
- 1994-10-28
- Volume
- 266
- Issue
- 5185
- Pages
- 653-656
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2069652470
- Cited by
- 671
- References
- 2
- FWCI
- 18.63
- Type
- journal article
- Language
- en
- Open access
- closed
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- Lin, T.-A., Kong, X., Haystead, T. A. J., Pause, A., Belsham, G., Sonenberg, N., & Lawrence, J. C. (1994). PHAS-I as a Link Between Mitogen-Activated Protein Kinase and Translation Initiation. Science. https://doi.org/10.1126/science.7939721
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