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Article: Latent membrane protein 1 of Epstein-Barr virus regulates p53 phosphorylation through MAP kinases

TitleLatent membrane protein 1 of Epstein-Barr virus regulates p53 phosphorylation through MAP kinases
Authors
Issue Date2007
PublisherElsevier Ireland Ltd. The Journal's web site is located at http://www.elsevier.com/locate/canlet
Citation
Cancer Letters, 2007, v. 255 n. 2, p. 219-231 How to Cite?
AbstractThe Epstein-Barr virus (EBV) encoded latent membrane protein 1 (LMP1), an oncogenic protein, plays an important role in the carcinogenesis of nasopharyngeal carcinoma (NPC). Phosphorylation of p53 protein is likely to play the key role in regulating its activity. p53 protein accumulates but mutation of p53 gene is not common in NPC. The molecular mechanisms of p53 augmentation have not been completely elucidated. Here, the role of MAP kinases in the phosphorylation of p53 modulated by LMP1 was determined. p53 could be activated and phosphorylated clearly at Ser15, Ser20, Ser392, and Thr81 modulated by LMP1. Furthermore, LMP1-induced phosphorylation of p53 at Ser15 was directly by ERKs; at Ser20 and Thr81 by JNK, at Ser 15 and Ser392 by p38 kinase. The phosphorylation of p53 was associated with its transcriptional activity and stability modulated by LMP1. These results strongly suggest that MAP kinases have a direct role in LMP1-induced phosphorylation of p53 at multiple sites, which provide a novel view for us to understand the mechanism of the activation of p53 in the carcinogenesis of nasopharyngeal carcinoma. © 2007 Elsevier Ireland Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/149674
ISSN
2014 Impact Factor: 5.621
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLi, Len_US
dc.contributor.authorGuo, Len_US
dc.contributor.authorTao, Yen_US
dc.contributor.authorZhou, Sen_US
dc.contributor.authorWang, Zen_US
dc.contributor.authorLuo, Wen_US
dc.contributor.authorHu, Den_US
dc.contributor.authorLi, Zen_US
dc.contributor.authorXiao, Len_US
dc.contributor.authorTang, Men_US
dc.contributor.authorYi, Wen_US
dc.contributor.authorTsao, SWen_US
dc.contributor.authorCao, Yen_US
dc.date.accessioned2012-06-26T05:56:54Z-
dc.date.available2012-06-26T05:56:54Z-
dc.date.issued2007en_US
dc.identifier.citationCancer Letters, 2007, v. 255 n. 2, p. 219-231en_US
dc.identifier.issn0304-3835en_US
dc.identifier.urihttp://hdl.handle.net/10722/149674-
dc.description.abstractThe Epstein-Barr virus (EBV) encoded latent membrane protein 1 (LMP1), an oncogenic protein, plays an important role in the carcinogenesis of nasopharyngeal carcinoma (NPC). Phosphorylation of p53 protein is likely to play the key role in regulating its activity. p53 protein accumulates but mutation of p53 gene is not common in NPC. The molecular mechanisms of p53 augmentation have not been completely elucidated. Here, the role of MAP kinases in the phosphorylation of p53 modulated by LMP1 was determined. p53 could be activated and phosphorylated clearly at Ser15, Ser20, Ser392, and Thr81 modulated by LMP1. Furthermore, LMP1-induced phosphorylation of p53 at Ser15 was directly by ERKs; at Ser20 and Thr81 by JNK, at Ser 15 and Ser392 by p38 kinase. The phosphorylation of p53 was associated with its transcriptional activity and stability modulated by LMP1. These results strongly suggest that MAP kinases have a direct role in LMP1-induced phosphorylation of p53 at multiple sites, which provide a novel view for us to understand the mechanism of the activation of p53 in the carcinogenesis of nasopharyngeal carcinoma. © 2007 Elsevier Ireland Ltd. All rights reserved.en_US
dc.languageengen_US
dc.publisherElsevier Ireland Ltd. The Journal's web site is located at http://www.elsevier.com/locate/canleten_US
dc.relation.ispartofCancer Lettersen_US
dc.subject.meshCell Line, Tumoren_US
dc.subject.meshEpstein-Barr Virus Infections - Metabolismen_US
dc.subject.meshHerpesvirus 4, Human - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshMitogen-Activated Protein Kinases - Physiologyen_US
dc.subject.meshNasopharyngeal Neoplasms - Virologyen_US
dc.subject.meshPhosphorylationen_US
dc.subject.meshSerine - Metabolismen_US
dc.subject.meshThreonine - Metabolismen_US
dc.subject.meshTumor Suppressor Protein P53 - Metabolismen_US
dc.subject.meshViral Matrix Proteins - Metabolismen_US
dc.titleLatent membrane protein 1 of Epstein-Barr virus regulates p53 phosphorylation through MAP kinasesen_US
dc.typeArticleen_US
dc.identifier.emailTsao, SW:gswtsao@hkucc.hku.hken_US
dc.identifier.authorityTsao, SW=rp00399en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.canlet.2007.04.014en_US
dc.identifier.pmid17582679en_US
dc.identifier.scopuseid_2-s2.0-34547965826en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34547965826&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume255en_US
dc.identifier.issue2en_US
dc.identifier.spage219en_US
dc.identifier.epage231en_US
dc.identifier.isiWOS:000249676700006-
dc.publisher.placeIrelanden_US
dc.identifier.scopusauthoridLi, L=26662260500en_US
dc.identifier.scopusauthoridGuo, L=35083512700en_US
dc.identifier.scopusauthoridTao, Y=7402420317en_US
dc.identifier.scopusauthoridZhou, S=16687258000en_US
dc.identifier.scopusauthoridWang, Z=18937718400en_US
dc.identifier.scopusauthoridLuo, W=36114068500en_US
dc.identifier.scopusauthoridHu, D=15764988700en_US
dc.identifier.scopusauthoridLi, Z=8219788700en_US
dc.identifier.scopusauthoridXiao, L=18938029700en_US
dc.identifier.scopusauthoridTang, M=54409388100en_US
dc.identifier.scopusauthoridYi, W=36115760400en_US
dc.identifier.scopusauthoridTsao, SW=7102813116en_US
dc.identifier.scopusauthoridCao, Y=7404524499en_US

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