PHAS-1 as a link between mitogen-activated protein kinase and translation initiation

T.-A. Lin, X. Kong, T. A. J. Haystead, A. Pause, Graham Belsham, N. Sonenberg, J. C. Lawrence

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

PHAS-I is a heat-stable protein (relative molecular mass approximate to 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.
Original languageEnglish
JournalScience
Volume266
Issue number5185
Pages (from-to)653-656
ISSN0036-8075
DOIs
Publication statusPublished - 1994
Externally publishedYes

Cite this

Lin, T-A., Kong, X., Haystead, T. A. J., Pause, A., Belsham, G., Sonenberg, N., & Lawrence, J. C. (1994). PHAS-1 as a link between mitogen-activated protein kinase and translation initiation. Science, 266(5185), 653-656. https://doi.org/10.1126/science.7939721