PHAS-I as a link between mitogen-activated protein kinase and translation initiation - PubMed (original) (raw)
. 1994 Oct 28;266(5185):653-6.
doi: 10.1126/science.7939721.
Affiliations
- PMID: 7939721
- DOI: 10.1126/science.7939721
PHAS-I as a link between mitogen-activated protein kinase and translation initiation
T A Lin et al. Science. 1994.
Abstract
PHAS-I is a heat-stable protein (relative molecular mass approximately 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.
Comment in
- Missing link in insulin's path to protein production.
O'Brien C. O'Brien C. Science. 1994 Oct 28;266(5185):542-3. doi: 10.1126/science.7939699. Science. 1994. PMID: 7939699 No abstract available.
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