DC Field | Value | Language |
---|---|---|
dc.contributor.author | Li, Zidong | ko |
dc.contributor.author | Kim, Hyoungmin | ko |
dc.contributor.author | Kim, Jaehoon | ko |
dc.contributor.author | Park, Jeong Hyeon | ko |
dc.date.accessioned | 2022-12-12T03:00:10Z | - |
dc.date.available | 2022-12-12T03:00:10Z | - |
dc.date.created | 2022-12-12 | - |
dc.date.created | 2022-12-12 | - |
dc.date.issued | 2023-03 | - |
dc.identifier.citation | BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS, v.1866, no.1 | - |
dc.identifier.issn | 1874-9399 | - |
dc.identifier.uri | http://hdl.handle.net/10203/302748 | - |
dc.description.abstract | EP400 is an ATP-dependent chromatin remodelling enzyme that regulates DNA double-strand break repair and transcription, including cMyc-dependent gene expression. We previously showed that the N-terminal domain of EP400 increases the efficacy of chemotherapeutic drugs against cancer cells. As the EP400 N-terminal-Like (EP400NL) gene resides next to the EP400 gene locus, this prompted us to investigate whether EP400NL plays a similar role in transcriptional regulation to the full-length EP400 protein. We found that EP400NL forms a human NuA4-like chromatin remodelling complex that lacks both the TIP60 histone acetyltransferase and EP400 ATPase. However, this EP400NL complex displays H2A.Z deposition activity on a chromatin template compa-rable to the human NuA4 complex, suggesting another associated ATPase such as BRG1 or RuvBL1/RuvBL2 catalyses the reaction. We demonstrated that the transcriptional coactivator function of EP400NL is required for serum and IFN gamma-induced PD-L1 gene activation. Furthermore, transcriptome analysis indicates that EP400NL contributes to cMyc-responsive mitochondrial biogenesis. Taken together, our studies show that EP400NL plays a role as a transcription coactivator of PD-L1 gene regulation and provides a potential target to modulate cMyc functions in cancer therapy. | - |
dc.language | English | - |
dc.publisher | ELSEVIER | - |
dc.title | EP400NL is involved in PD-L1 gene activation by forming a transcriptional coactivator complex | - |
dc.type | Article | - |
dc.identifier.wosid | 000889987700003 | - |
dc.identifier.scopusid | 2-s2.0-85141806686 | - |
dc.type.rims | ART | - |
dc.citation.volume | 1866 | - |
dc.citation.issue | 1 | - |
dc.citation.publicationname | BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS | - |
dc.identifier.doi | 10.1016/j.bbagrm.2022.194889 | - |
dc.contributor.localauthor | Kim, Jaehoon | - |
dc.contributor.nonIdAuthor | Li, Zidong | - |
dc.contributor.nonIdAuthor | Park, Jeong Hyeon | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | Cancer | - |
dc.subject.keywordAuthor | Chromatin remodelling | - |
dc.subject.keywordAuthor | cMyc | - |
dc.subject.keywordAuthor | PD-L1 | - |
dc.subject.keywordAuthor | H2A | - |
dc.subject.keywordAuthor | Z | - |
dc.subject.keywordAuthor | Epigenetic | - |
dc.subject.keywordPlus | HISTONE ACETYLTRANSFERASE COMPLEX | - |
dc.subject.keywordPlus | PD-L1 EXPRESSION | - |
dc.subject.keywordPlus | C-MYC | - |
dc.subject.keywordPlus | TRRAP | - |
dc.subject.keywordPlus | NUA4 | - |
dc.subject.keywordPlus | ASSOCIATION | - |
dc.subject.keywordPlus | ONCOPROTEIN | - |
dc.subject.keywordPlus | COFACTOR | - |
dc.subject.keywordPlus | RECRUITS | - |
dc.subject.keywordPlus | PATHWAY | - |
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