Full metadata record
DC Field | Value | Language |
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dc.contributor.author | Ramakrishna, Suresh | - |
dc.date.accessioned | 2018-01-30T04:56:22Z | - |
dc.date.available | 2018-01-30T04:56:22Z | - |
dc.date.issued | 2016-03 | - |
dc.identifier.citation | ONCOTARGET, v. 7, NO 12, Page. 14441-14457 | en_US |
dc.identifier.issn | 1949-2553 | - |
dc.identifier.uri | http://www.oncotarget.com/index.php?journal=oncotarget&page=article&op=view&path[]=7581&path[]=21906 | - |
dc.identifier.uri | http://hdl.handle.net/20.500.11754/34408 | - |
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. | en_US |
dc.description.sponsorship | We thank our lab members for their critical comments and discussions. We would like to thank Jang-Joon Park for immunoprecipitation assays. We also thank Drs. Yoshiaki Ishigatsubo at Yokohama City University School of Medicine for Flag-tagged RanBPM plasmid and Patrick J. Brennwald at University of North Carolina for Mgl-1 antibody, respectively. This study was supported by a grant from the National Research and Development for Cancer Control, Ministry for Health, Welfare and Family Affairs, Republic of Korea (0820330). | en_US |
dc.language.iso | en | en_US |
dc.publisher | IMPACT JOURNALS LLC | en_US |
dc.subject | deubiquitinating enzyme | en_US |
dc.subject | RanBPM | en_US |
dc.subject | UAF1 | en_US |
dc.subject | ubiquitin | en_US |
dc.subject | USP11 | en_US |
dc.title | Ubiquitin-specific protease 11 functions as a tumor suppressor by modulating Mgl-1 protein to regulate cancer cell growth | en_US |
dc.type | Article | en_US |
dc.relation.no | 12 | - |
dc.relation.volume | 7 | - |
dc.identifier.doi | 10.18632/oncotarget.7581 | - |
dc.relation.page | 14441-14457 | - |
dc.relation.journal | ONCOTARGET | - |
dc.contributor.googleauthor | Lim, Key-Hwan | - |
dc.contributor.googleauthor | Suresh, Bharathi | - |
dc.contributor.googleauthor | Park, Jung-Hyun | - |
dc.contributor.googleauthor | Kim, Young-Soo | - |
dc.contributor.googleauthor | Ramakrishna, Suresh | - |
dc.contributor.googleauthor | Baek, Kwang-Hyun | - |
dc.relation.code | 2016010107 | - |
dc.sector.campus | S | - |
dc.sector.daehak | Graduate School of Biomedical Science & Engineering[S] | - |
dc.identifier.pid | suri28 | - |
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