Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 김계성 | - |
dc.date.accessioned | 2019-09-05T05:07:41Z | - |
dc.date.available | 2019-09-05T05:07:41Z | - |
dc.date.issued | 2019-03 | - |
dc.identifier.citation | BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE, v. 1865, NO 3, Page. 599-610 | en_US |
dc.identifier.issn | 0925-4439 | - |
dc.identifier.issn | 1879-260X | - |
dc.identifier.uri | https://www.sciencedirect.com/science/article/pii/S0925443918304927?via%3Dihub | - |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/110282 | - |
dc.description.abstract | RNA-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.sponsorship | This 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.iso | en | en_US |
dc.publisher | ELSEVIER SCIENCE BV | en_US |
dc.subject | Cell viability | en_US |
dc.subject | CRISPR/Cas9 | en_US |
dc.subject | Knockout cell lines | en_US |
dc.subject | Let-7 | en_US |
dc.subject | Protein degradation | en_US |
dc.title | The stability and oncogenic function of LIN28A are regulated by USP28 | en_US |
dc.type | Article | en_US |
dc.relation.no | 3 | - |
dc.relation.volume | 1865 | - |
dc.identifier.doi | 10.1016/j.bbadis.2018.12.006 | - |
dc.relation.page | 599-610 | - |
dc.relation.journal | BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE | - |
dc.contributor.googleauthor | Haq, Saba | - |
dc.contributor.googleauthor | Das, Soumyadip | - |
dc.contributor.googleauthor | Kim, Dong-Ho | - |
dc.contributor.googleauthor | Chandrasekaran, Arun Pandian | - |
dc.contributor.googleauthor | Hong, Seok-Ho | - |
dc.contributor.googleauthor | Kim, Kye-Seong | - |
dc.contributor.googleauthor | Ramakrishna, Suresh | - |
dc.relation.code | 2019000012 | - |
dc.sector.campus | S | - |
dc.sector.daehak | COLLEGE OF MEDICINE[S] | - |
dc.sector.department | DEPARTMENT OF MEDICINE | - |
dc.identifier.pid | ks66kim | - |
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