| pubmed-article:2122455 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2122455 | lifeskim:mentions | umls-concept:C0332437 | lld:lifeskim |
| pubmed-article:2122455 | lifeskim:mentions | umls-concept:C0018873 | lld:lifeskim |
| pubmed-article:2122455 | lifeskim:mentions | umls-concept:C1514559 | lld:lifeskim |
| pubmed-article:2122455 | lifeskim:mentions | umls-concept:C0030943 | lld:lifeskim |
| pubmed-article:2122455 | lifeskim:mentions | umls-concept:C1274040 | lld:lifeskim |
| pubmed-article:2122455 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
| pubmed-article:2122455 | lifeskim:mentions | umls-concept:C1157563 | lld:lifeskim |
| pubmed-article:2122455 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:2122455 | pubmed:dateCreated | 1990-12-7 | lld:pubmed |
| pubmed-article:2122455 | pubmed:abstractText | Eukaryotic protein synthesis initiation factor 4E (eIF-4E) is a 25-kDa polypeptide that binds to the 7-methylguanosine-containing cap of mRNA and participates in the transfer of mRNA to the 40S ribosomal subunit, a step that is rate-limiting for protein synthesis under most cellular conditions. eIF-4E is the least abundant of the initiation factors, is present at approximately 10% of molar concentration of mRNA, and thus may serve as a site of regulation for the recruitment of mRNA into polysomes. Previous studies have indicated that phosphorylation of eIF-4E at Ser-53 is correlated with an increased rate of protein synthesis in a variety of systems in vivo and is required for eIF-4E to become bound to the 48S initiation complex. In this study we show that overexpression of eIF-4E in HeLa cells using an episomally replicating, BK virus-based vector leads to an unusual phenotype: cells grow rapidly, forming densely packed, multilayered foci. They progressively form syncytia, some containing as many as six nuclei, and ultimately lyse 1 month after transfection. Some of these properties are reminiscent of oncogenically transformed cells. Cells transfected with the identical vector expressing a variant of eIF-4E, which contains alanine at position 53 and thus cannot be phosphorylated at the major in vivo site, grow normally. Estimations using the Ala-53 variant or a bacterial chloramphenicol acetyltransferase reporter gene in the same vector indicate that the degree of eIF-4E overexpression is 3- to 9-fold more than the endogenous level. These results suggest that eIF-4E may play a key role in cell cycle progression. | lld:pubmed |
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| pubmed-article:2122455 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2122455 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2122455 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2122455 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:2122455 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2122455 | pubmed:author | pubmed-author:RhoadsR ERE | lld:pubmed |
| pubmed-article:2122455 | pubmed:author | pubmed-author:De... | lld:pubmed |
| pubmed-article:2122455 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2122455 | pubmed:volume | 87 | lld:pubmed |
| pubmed-article:2122455 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2122455 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2122455 | pubmed:pagination | 8212-6 | lld:pubmed |
| pubmed-article:2122455 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2122455 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2122455 | pubmed:articleTitle | Overexpression of eukaryotic protein synthesis initiation factor 4E in HeLa cells results in aberrant growth and morphology. | lld:pubmed |
| pubmed-article:2122455 | pubmed:affiliation | Department of Biochemistry, University of Kentucky College of Medicine, Lexington 40536. | lld:pubmed |
| pubmed-article:2122455 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2122455 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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