103 0

Full metadata record

DC FieldValueLanguage
dc.contributor.author김계성-
dc.date.accessioned2019-09-05T05:07:41Z-
dc.date.available2019-09-05T05:07:41Z-
dc.date.issued2019-03-
dc.identifier.citationBIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE, v. 1865, NO 3, Page. 599-610en_US
dc.identifier.issn0925-4439-
dc.identifier.issn1879-260X-
dc.identifier.urihttps://www.sciencedirect.com/science/article/pii/S0925443918304927?via%3Dihub-
dc.identifier.urihttps://repository.hanyang.ac.kr/handle/20.500.11754/110282-
dc.description.abstractRNA-binding protein LIN28A is often highly expressed in human malignant tumors and is involved in tumor metastasis and poor prognosis. Knowledge about post-translational regulatory mechanisms governing LIN28A protein stability and function is scarce. Here, we investigated the role of ubiquitination and deubiquitination on LIN28A protein stability and report that LIN28A protein undergoes ubiquitination. Ubiquitin-specific protease 28 (USP28), a deubiquitinating enzyme, interacts with and stabilizes LIN28A protein to extend its half-life. USP28, through its deubiquitinating activity, antagonizes LIN28A protein turnover by reversing its proteasomal degradation. Our study describes the consequential impacts of USP28-mediated stabilization of LIN28A protein on enhancing cancer cell viability, migration and ultimately augmenting LIN28A-mediated tumor progression. Overall, our data suggest that a synergistic, combinatorial approach of targeting LIN28A with USP28 would contribute to effective cancer therapeutics.en_US
dc.description.sponsorshipThis work was supported by a grant from the Korea Health Technology R&D Project through the Korea Health Industry Development Institute (KHIDI), funded by the Ministry of Health and Welfare, Republic of Korea (HI16C1009) and National Research Foundation of Korea (NRF) grants (2018M3A9H3022412).en_US
dc.language.isoenen_US
dc.publisherELSEVIER SCIENCE BVen_US
dc.subjectCell viabilityen_US
dc.subjectCRISPR/Cas9en_US
dc.subjectKnockout cell linesen_US
dc.subjectLet-7en_US
dc.subjectProtein degradationen_US
dc.titleThe stability and oncogenic function of LIN28A are regulated by USP28en_US
dc.typeArticleen_US
dc.relation.no3-
dc.relation.volume1865-
dc.identifier.doi10.1016/j.bbadis.2018.12.006-
dc.relation.page599-610-
dc.relation.journalBIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE-
dc.contributor.googleauthorHaq, Saba-
dc.contributor.googleauthorDas, Soumyadip-
dc.contributor.googleauthorKim, Dong-Ho-
dc.contributor.googleauthorChandrasekaran, Arun Pandian-
dc.contributor.googleauthorHong, Seok-Ho-
dc.contributor.googleauthorKim, Kye-Seong-
dc.contributor.googleauthorRamakrishna, Suresh-
dc.relation.code2019000012-
dc.sector.campusS-
dc.sector.daehakCOLLEGE OF MEDICINE[S]-
dc.sector.departmentDEPARTMENT OF MEDICINE-
dc.identifier.pidks66kim-
Appears in Collections:
COLLEGE OF MEDICINE[S](의과대학) > MEDICINE(의학과) > Articles
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE