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Transglutaminase 2 inhibits Rb binding of human papillomavirus E7 by incorporating polyamine
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Jeon, Ju Hong | - |
dc.contributor.author | Choi, Kyung Ho | - |
dc.contributor.author | Cho, Sung Yup | - |
dc.contributor.author | Kim, Chai Wan | - |
dc.contributor.author | Shin, Dong Myung | - |
dc.contributor.author | Kwon, Joon Cheo | - |
dc.contributor.author | Song, Kye Yong | - |
dc.contributor.author | Park, Sang Chul | - |
dc.contributor.author | Kim, In Gyu | - |
dc.date.accessioned | 2024-05-16T01:41:05Z | - |
dc.date.available | 2024-05-16T01:41:05Z | - |
dc.date.created | 2024-04-23 | - |
dc.date.created | 2024-04-23 | - |
dc.date.created | 2024-04-23 | - |
dc.date.issued | 2003-10 | - |
dc.identifier.citation | The EMBO Journal, Vol.22 No.19, pp.5273-5282 | - |
dc.identifier.issn | 0261-4189 | - |
dc.identifier.uri | https://hdl.handle.net/10371/202787 | - |
dc.description.abstract | Transglutaminase 2 (TGase 2) is one of a family of enzymes that catalyze protein modification through the incorporation of polyamines into substrates or the formation of protein crosslinks. However, the physiological roles of TGase 2 are largely unknown. To elucidate the functions of TGase 2, we have searched for its interacting proteins. Here we show that TGase 2 interacts with E7 oncoprotein of human papillomavirus type 18 (HPV18) in vitro and in vivo. TGase 2 incorporates polyamines into a conserved glutamine residue in the zinc-binding domain of HPV18 E7 protein. This modification mediates the inhibition of E7's Rb binding ability. In contrast, TGase 2 does not affect HPV16 E7, due to absence of a glutamine residue at this polyamination site. Using E7 mutants, we demonstrate that TGase 2-dependent inhibition of HPV E7 function correlates with the presence of the polyamination site. Our results indicate that TGase 2 is an important cellular interfering factor and define a novel host-virus interaction, suggesting that the inability of TGase 2 to inactivate HPV16 E7 could explain the high prevalence of HPV16 in cervical cancer. | - |
dc.language | 영어 | - |
dc.publisher | Nature Publishing Group | - |
dc.title | Transglutaminase 2 inhibits Rb binding of human papillomavirus E7 by incorporating polyamine | - |
dc.type | Article | - |
dc.identifier.doi | 10.1093/emboj/cdg495 | - |
dc.citation.journaltitle | The EMBO Journal | - |
dc.identifier.wosid | 000185731300037 | - |
dc.identifier.scopusid | 2-s2.0-0141864664 | - |
dc.citation.endpage | 5282 | - |
dc.citation.number | 19 | - |
dc.citation.startpage | 5273 | - |
dc.citation.volume | 22 | - |
dc.description.isOpenAccess | Y | - |
dc.contributor.affiliatedAuthor | Jeon, Ju Hong | - |
dc.contributor.affiliatedAuthor | Cho, Sung Yup | - |
dc.contributor.affiliatedAuthor | Park, Sang Chul | - |
dc.contributor.affiliatedAuthor | Kim, In Gyu | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | TUMOR-SUPPRESSOR PROTEIN | - |
dc.subject.keywordPlus | TISSUE TRANSGLUTAMINASE | - |
dc.subject.keywordPlus | HPV E7 | - |
dc.subject.keywordPlus | TRANSAMIDATION ACTIVITY | - |
dc.subject.keywordPlus | TRANSFORMING ACTIVITY | - |
dc.subject.keywordPlus | NUCLEAR-LOCALIZATION | - |
dc.subject.keywordPlus | ONCOPROTEIN | - |
dc.subject.keywordPlus | GENE | - |
dc.subject.keywordPlus | IMMORTALIZATION | - |
dc.subject.keywordPlus | REQUIREMENTS | - |
dc.subject.keywordAuthor | host-virus interaction | - |
dc.subject.keywordAuthor | human papillomavirus E7 oncoprotein | - |
dc.subject.keywordAuthor | polyamination | - |
dc.subject.keywordAuthor | transglutaminase 2 | - |
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