pubmed-article:12192037 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12192037 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:12192037 | lifeskim:mentions | umls-concept:C0040711 | lld:lifeskim |
pubmed-article:12192037 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:12192037 | lifeskim:mentions | umls-concept:C1442498 | lld:lifeskim |
pubmed-article:12192037 | lifeskim:mentions | umls-concept:C1823882 | lld:lifeskim |
pubmed-article:12192037 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
pubmed-article:12192037 | lifeskim:mentions | umls-concept:C0013879 | lld:lifeskim |
pubmed-article:12192037 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:12192037 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:12192037 | pubmed:issue | 18 | lld:pubmed |
pubmed-article:12192037 | pubmed:dateCreated | 2002-8-22 | lld:pubmed |
pubmed-article:12192037 | pubmed:abstractText | The eukaryotic Y-box-binding protein YB-1 functions in various biological processes, including DNA repair, cell proliferation, and transcriptional and translational controls. To gain further insight into how human YB-1 plays its role in pleiotropic functions, we here used two-hybrid screenings to identify partners of this protein; the results showed that YB-1 itself, iron-regulatory protein 2 (IRP2), and five ribosomal proteins each served as partners to YB-1. We then examined the biological effect of the interaction of YB-1 and IRP2 on translational regulation. Both in vitro binding and coimmunoprecipitation assays showed the direct interaction of YB-1 and IRP2 in the presence of a high concentration of iron. RNA gel shift assays showed that YB-1 reduced the formation of the IRP2-mRNA complex when the iron-responsive element of the ferritin mRNA 5' untranslated region (UTR) was used as a probe. By using an in vitro translation assay using luciferase mRNA ligated to the ferritin mRNA 5'UTR as a reporter construct, we showed that both YB-1 and IRP2 inhibited the translation of the mRNA. However, coadministration of YB-1 and IRP2 proteins abrogated the inhibition of protein synthesis by each protein. An In vivo coimmunoprecipitation assay showed that IRP2 bound to YB-1 in the presence of iron and a proteasome inhibitor. The direct interaction of YB-1 and IRP2 provides the first evidence of the involvement of YB-1 in the translational regulation of an iron-related protein. | lld:pubmed |
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pubmed-article:12192037 | pubmed:language | eng | lld:pubmed |
pubmed-article:12192037 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12192037 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12192037 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12192037 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12192037 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12192037 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12192037 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12192037 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12192037 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12192037 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12192037 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12192037 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12192037 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12192037 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12192037 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12192037 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12192037 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12192037 | pubmed:month | Sep | lld:pubmed |
pubmed-article:12192037 | pubmed:issn | 0270-7306 | lld:pubmed |
pubmed-article:12192037 | pubmed:author | pubmed-author:ShirasunaKane... | lld:pubmed |
pubmed-article:12192037 | pubmed:author | pubmed-author:NakamuraTakan... | lld:pubmed |
pubmed-article:12192037 | pubmed:author | pubmed-author:KohnoKimitosh... | lld:pubmed |
pubmed-article:12192037 | pubmed:author | pubmed-author:KuwanoMichihi... | lld:pubmed |
pubmed-article:12192037 | pubmed:author | pubmed-author:IzumiHirotoH | lld:pubmed |
pubmed-article:12192037 | pubmed:author | pubmed-author:IwaiKazuhiroK | lld:pubmed |
pubmed-article:12192037 | pubmed:author | pubmed-author:UchiumiTakesh... | lld:pubmed |
pubmed-article:12192037 | pubmed:author | pubmed-author:AshizukaMegum... | lld:pubmed |
pubmed-article:12192037 | pubmed:author | pubmed-author:FukudaTakaoT | lld:pubmed |
pubmed-article:12192037 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12192037 | pubmed:volume | 22 | lld:pubmed |
pubmed-article:12192037 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12192037 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12192037 | pubmed:pagination | 6375-83 | lld:pubmed |
pubmed-article:12192037 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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