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The stability and oncogenic function of LIN28A are regulated by USP28

Title
The stability and oncogenic function of LIN28A are regulated by USP28
Author
김계성
Keywords
Cell viability; CRISPR/Cas9; Knockout cell lines; Let-7; Protein degradation
Issue Date
2019-03
Publisher
ELSEVIER SCIENCE BV
Citation
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE, v. 1865, NO 3, Page. 599-610
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.
URI
https://www.sciencedirect.com/science/article/pii/S0925443918304927?via%3Dihubhttps://repository.hanyang.ac.kr/handle/20.500.11754/110282
ISSN
0925-4439; 1879-260X
DOI
10.1016/j.bbadis.2018.12.006
Appears in Collections:
COLLEGE OF MEDICINE[S](의과대학) > MEDICINE(의학과) > Articles
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