Linked Life Data

1980214

Source:http://linkedlifedata.com/resource/pubmed/id/1980214

Statements in which the resource exists.
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pubmed-article:1980214pubmed:abstractTextEukaryotic initiation factor 4F (eIF-4F) is a multisubunit protein that functions in the first step of the binding of capped mRNAs to the small ribosomal subunit. Its largest polypeptide component, p220, is cleaved following poliovirus infection. This is thought to inactivate eIF-4F function, thereby preventing cap-dependent initiation of translation of cellular mRNAs. In this report, we show that p220 in extracts of uninfected HeLa cells is specifically lost in the presence of calcium. The responsible activities have been partially purified and identified as the calcium-dependent, neutral, cysteine proteases calpains I and II. In addition, a third calcium-dependent activity was resolved from the calpains and also results in the loss of p220. This activity has properties similar to a transglutaminase and copurifies with tissue transglutaminase through several chromatographic steps. None of these calcium-dependent activities appears to mediate p220 cleavage in poliovirus-infected cells.lld:pubmed
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pubmed-article:1980214pubmed:authorpubmed-author:CroallD EDElld:pubmed
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pubmed-article:1980214pubmed:pagination10055-61lld:pubmed
pubmed-article:1980214pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:1980214pubmed:articleTitleThe p220 component of eukaryotic initiation factor 4F is a substrate for multiple calcium-dependent enzymes.lld:pubmed
pubmed-article:1980214pubmed:affiliationDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City 84132.lld:pubmed
pubmed-article:1980214pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1980214pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:1980214pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
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