EP400NL is involved in PD-L1 gene activation by forming a transcriptional coactivator complex

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dc.citation.issue1
dc.citation.volume1866
dc.contributor.authorLi Z
dc.contributor.authorKim H
dc.contributor.authorKim J
dc.contributor.authorPark JH
dc.coverage.spatialNetherlands
dc.date.accessioned2024-09-12T03:06:11Z
dc.date.available2024-09-12T03:06:11Z
dc.date.issued2023-03
dc.description.abstractEP400 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 comparable 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 IFNγ-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.description.confidentialfalse
dc.edition.editionMarch 2023
dc.format.pagination194889-
dc.identifier.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/36328277
dc.identifier.citationLi Z, Kim H, Kim J, Park JH. (2023). EP400NL is involved in PD-L1 gene activation by forming a transcriptional coactivator complex.. Biochim Biophys Acta Gene Regul Mech. 1866. 1. (pp. 194889-).
dc.identifier.doi10.1016/j.bbagrm.2022.194889
dc.identifier.eissn1876-4320
dc.identifier.elements-typejournal-article
dc.identifier.issn1874-9399
dc.identifier.number194889
dc.identifier.piiS1874-9399(22)00104-3
dc.identifier.urihttps://mro.massey.ac.nz/handle/10179/71449
dc.languageeng
dc.publisherElsevier B V
dc.publisher.urihttps://www.sciencedirect.com/science/article/pii/S1874939922001043
dc.relation.isPartOfBiochim Biophys Acta Gene Regul Mech
dc.rights(c) 2022 The Author/s
dc.rightsCC BY 4.0
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectCancer
dc.subjectChromatin remodelling
dc.subjectEpigenetic
dc.subjectH2A.Z
dc.subjectPD-L1
dc.subjectcMyc
dc.subjectHumans
dc.subjectAdenosine Triphosphatases
dc.subjectATPases Associated with Diverse Cellular Activities
dc.subjectB7-H1 Antigen
dc.subjectCarrier Proteins
dc.subjectDNA Helicases
dc.subjectHistones
dc.subjectTranscription Factors
dc.subjectTranscriptional Activation
dc.titleEP400NL is involved in PD-L1 gene activation by forming a transcriptional coactivator complex
dc.typeJournal article
pubs.elements-id457982
pubs.organisational-groupOther
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