Ubiquitin-specific protease 11 functions as a tumor suppressor by modulating Mgl-1 protein to regulate cancer cell growth
DC Field | Value | Language |
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dc.contributor.author | Lim, Key-Hwan | - |
dc.contributor.author | Suresh, Bharathi | - |
dc.contributor.author | Park, Jung-Hyun | - |
dc.contributor.author | Kim, Young-Soo | - |
dc.contributor.author | Ramakrishna, Suresh | - |
dc.contributor.author | Baek, Kwang-Hyun | - |
dc.date.accessioned | 2022-07-15T18:03:45Z | - |
dc.date.available | 2022-07-15T18:03:45Z | - |
dc.date.created | 2021-05-14 | - |
dc.date.issued | 2016-03 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/154910 | - |
dc.description.abstract | The Lethal giant larvae (Lgl) gene encodes a cortical cytoskeleton protein, Lgl, and is involved in maintaining cell polarity and epithelial integrity. Previously, we observed that Mgl-1, a mammalian homologue of the Drosophila tumor suppressor protein Lgl, is subjected to degradation via ubiquitin-proteasome pathway, and scaffolding protein RanBPM prevents the turnover of the Mgl-1 protein. Consequently, overexpression of RanBPM enhances Mgl-1-mediated cell proliferation and migration. Here, we analyzed the ability of ubiquitin-specific protease 11 (USP11) as a novel regulator of Mgl-1 and it requires RanBPM to regulate proteasomal degradation of Mgl-1. USP11 showed deubiquitinating activity and stabilized Mgl-1 protein. However, USP11-mediated Mgl-1 stabilization was inhibited in RanBPMknockdown cells. Furthermore, in the cancer cell migration, the regulation of Mgl-1 by USP11 required RanBPM expression. In addition, an in vivo study revealed that depletion of USP11 leads to tumor formation. Taken together, the results indicated that USP11 functions as a tumor suppressor through the regulation of Mgl-1 protein degradation via RanBPM. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | IMPACT JOURNALS LLC | - |
dc.title | Ubiquitin-specific protease 11 functions as a tumor suppressor by modulating Mgl-1 protein to regulate cancer cell growth | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Ramakrishna, Suresh | - |
dc.identifier.doi | 10.18632/oncotarget.7581 | - |
dc.identifier.scopusid | 2-s2.0-84971612117 | - |
dc.identifier.wosid | 000375687200088 | - |
dc.identifier.bibliographicCitation | ONCOTARGET, v.7, no.12, pp.14441 - 14457 | - |
dc.relation.isPartOf | ONCOTARGET | - |
dc.citation.title | ONCOTARGET | - |
dc.citation.volume | 7 | - |
dc.citation.number | 12 | - |
dc.citation.startPage | 14441 | - |
dc.citation.endPage | 14457 | - |
dc.type.rims | ART | - |
dc.type.docType | 정기학술지(Article(Perspective Article포함)) | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | Y | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Oncology | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.relation.journalWebOfScienceCategory | Oncology | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.subject.keywordPlus | DEUBIQUITINATING ENZYME | - |
dc.subject.keywordPlus | GIANT-LARVAE | - |
dc.subject.keywordPlus | SCAFFOLDING PROTEIN | - |
dc.subject.keywordPlus | ANDROGEN RECEPTOR | - |
dc.subject.keywordPlus | DROSOPHILA | - |
dc.subject.keywordPlus | RANBPM | - |
dc.subject.keywordPlus | COMPLEX | - |
dc.subject.keywordPlus | LGL | - |
dc.subject.keywordPlus | POLARITY | - |
dc.subject.keywordPlus | MECHANISMS | - |
dc.subject.keywordAuthor | deubiquitinating enzyme | - |
dc.subject.keywordAuthor | RanBPM | - |
dc.subject.keywordAuthor | UAF1 | - |
dc.subject.keywordAuthor | ubiquitin | - |
dc.subject.keywordAuthor | USP11 | - |
dc.identifier.url | https://www.oncotarget.com/article/7581/text/ | - |
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