E3 Ubiquitin Ligase APC/C-Cdh1 Negatively Regulates FAH Protein Stability by Promoting Its Polyubiquitination
DC Field | Value | Language |
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dc.contributor.author | Kaushal, Kamini | - |
dc.contributor.author | Woo, Sang Hyeon | - |
dc.contributor.author | Tyagi, Apoorvi | - |
dc.contributor.author | Kim, Dong Ha | - |
dc.contributor.author | Suresh, Bharathi | - |
dc.contributor.author | Kim, Kye-Seong | - |
dc.contributor.author | Ramakrishna, Suresh | - |
dc.date.accessioned | 2022-07-07T11:20:04Z | - |
dc.date.available | 2022-07-07T11:20:04Z | - |
dc.date.issued | 2020-11 | - |
dc.identifier.issn | 1661-6596 | - |
dc.identifier.issn | 1422-0067 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/144461 | - |
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. | - |
dc.format.extent | 17 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | MDPI | - |
dc.title | E3 Ubiquitin Ligase APC/C-Cdh1 Negatively Regulates FAH Protein Stability by Promoting Its Polyubiquitination | - |
dc.type | Article | - |
dc.publisher.location | 스위스 | - |
dc.identifier.doi | 10.3390/ijms21228719 | - |
dc.identifier.scopusid | 2-s2.0-85096536004 | - |
dc.identifier.wosid | 000594186500001 | - |
dc.identifier.bibliographicCitation | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, v.21, no.22, pp 1 - 17 | - |
dc.citation.title | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | - |
dc.citation.volume | 21 | - |
dc.citation.number | 22 | - |
dc.citation.startPage | 1 | - |
dc.citation.endPage | 17 | - |
dc.type.docType | Article | - |
dc.description.isOpenAccess | Y | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Multidisciplinary | - |
dc.subject.keywordPlus | HUMAN FUMARYLACETOACETATE HYDROLASE | - |
dc.subject.keywordPlus | HEREDITARY TYROSINEMIA | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | GENE | - |
dc.subject.keywordPlus | DEFICIENCY | - |
dc.subject.keywordPlus | METABOLITE | - |
dc.subject.keywordPlus | DELIVERY | - |
dc.subject.keywordPlus | NETWORK | - |
dc.subject.keywordPlus | TYPE-1 | - |
dc.subject.keywordPlus | CDH1 | - |
dc.subject.keywordAuthor | CRISPR | - |
dc.subject.keywordAuthor | Cas9 knockout | - |
dc.subject.keywordAuthor | in silico analysis | - |
dc.subject.keywordAuthor | liver cancer | - |
dc.subject.keywordAuthor | post-translational modifications | - |
dc.subject.keywordAuthor | ubiquitin-proteasome system | - |
dc.identifier.url | https://www.mdpi.com/1422-0067/21/22/8719 | - |
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