Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 김계성 | - |
dc.date.accessioned | 2022-08-30T01:33:28Z | - |
dc.date.available | 2022-08-30T01:33:28Z | - |
dc.date.issued | 2020-11 | - |
dc.identifier.citation | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, v. 21, no. 22, article no. 8719, page. 8719-8735 | en_US |
dc.identifier.issn | 1422-0067 | - |
dc.identifier.uri | https://www.mdpi.com/1422-0067/21/22/8719 | - |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/172631 | - |
dc.description.abstract | Fumarylacetoacetate hydrolase (FAH) is the last enzyme in the degradation pathway of the amino acids tyrosine and phenylalanine in mammals that catalyzes the hydrolysis of 4-fumarylacetoacetate into acetoacetate and fumarate. Mutations of the FAH gene are associated with hereditary tyrosinemia type I (HT1), resulting in reduced protein stability, misfolding, accelerated degradation and deficiency in functional proteins. Identifying E3 ligases, which are necessary for FAH protein stability and degradation, is essential. In this study, we demonstrated that the FAH protein level is elevated in liver cancer tissues compared to that in normal tissues. Further, we showed that the FAH protein undergoes 26S proteasomal degradation and its protein turnover is regulated by the anaphase-promoting complex/cyclosome-Cdh1 (APC/C)(Cdh1) E3 ubiquitin ligase complex. APC/C-Cdh1 acts as a negative stabilizer of FAH protein by promoting FAH polyubiquitination and decreases the half-life of FAH protein. Thus, we envision that Cdh1 might be a key factor in the maintenance of FAH protein level to regulate FAH-mediated physiological functions. | en_US |
dc.description.sponsorship | This research was supported by the National Research Foundation (2017M3A9B3061830 and 2018M3A9H3022412). | en_US |
dc.language.iso | en | en_US |
dc.publisher | MDPI | en_US |
dc.subject | CRISPR/Cas9 knockout | en_US |
dc.subject | in silico analysis | en_US |
dc.subject | liver cancer | en_US |
dc.subject | post-translational modifications | en_US |
dc.subject | ubiquitin-proteasome system | en_US |
dc.title | E3 Ubiquitin Ligase APC/CCdh1 Negatively Regulates FAH Protein Stability by Promoting Its Polyubiquitination | en_US |
dc.type | Article | en_US |
dc.relation.no | 1 | - |
dc.relation.volume | 21 | - |
dc.identifier.doi | 10.3390/ijms21228719 | - |
dc.relation.page | 8719-8735 | - |
dc.relation.journal | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | - |
dc.contributor.googleauthor | Kaushal, Kamini | - |
dc.contributor.googleauthor | Woo, Sang Hyeon | - |
dc.contributor.googleauthor | Tyagi, Apoorvi | - |
dc.contributor.googleauthor | Kim, Dong Ha | - |
dc.contributor.googleauthor | Suresh, Bharathi | - |
dc.contributor.googleauthor | Kim, Kye-Seong | - |
dc.contributor.googleauthor | Ramakrishna, Suresh | - |
dc.relation.code | 2020050347 | - |
dc.sector.campus | S | - |
dc.sector.daehak | GRADUATE SCHOOL OF BIOMEDICAL SCIENCE AND ENGINEERING[S] | - |
dc.sector.department | DEPARTMENT OF BIOMEDICAL SCIENCE | - |
dc.identifier.pid | ks66kim | - |
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