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Article: The Growing Complexity of UHRF1-Mediated Maintenance DNA Methylation

TitleThe Growing Complexity of UHRF1-Mediated Maintenance DNA Methylation
Authors
KeywordsDNA methylation
DNMT1
UHRF1
USP7
ubiquitination
Issue Date2018
PublisherMDPI AG. The Journal's web site is located at http://www.mdpi.com/journal/genes
Citation
Genes, 2018, v. 9 n. 12, p. 600 How to Cite?
AbstractMammalian DNMT1 is mainly responsible for maintenance DNA methylation that is critical in maintaining stem cell pluripotency and controlling lineage specification during early embryonic development. A number of studies have demonstrated that DNMT1 is an auto-inhibited enzyme and its enzymatic activity is allosterically regulated by a number of interacting partners. UHRF1 has previously been reported to regulate DNMT1 in multiple ways, including control of substrate specificity and the proper genome targeting. In this review, we discuss the recent advances in our understanding of the regulation of DNMT1 enzymatic activity by UHRF1 and highlight a number of unresolved questions.
Persistent Identifierhttp://hdl.handle.net/10722/278062
ISSN
2021 Impact Factor: 4.141
2020 SCImago Journal Rankings: 1.337
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorXie, S-
dc.contributor.authorQian, C-
dc.date.accessioned2019-10-04T08:06:46Z-
dc.date.available2019-10-04T08:06:46Z-
dc.date.issued2018-
dc.identifier.citationGenes, 2018, v. 9 n. 12, p. 600-
dc.identifier.issn2073-4425-
dc.identifier.urihttp://hdl.handle.net/10722/278062-
dc.description.abstractMammalian DNMT1 is mainly responsible for maintenance DNA methylation that is critical in maintaining stem cell pluripotency and controlling lineage specification during early embryonic development. A number of studies have demonstrated that DNMT1 is an auto-inhibited enzyme and its enzymatic activity is allosterically regulated by a number of interacting partners. UHRF1 has previously been reported to regulate DNMT1 in multiple ways, including control of substrate specificity and the proper genome targeting. In this review, we discuss the recent advances in our understanding of the regulation of DNMT1 enzymatic activity by UHRF1 and highlight a number of unresolved questions.-
dc.languageeng-
dc.publisherMDPI AG. The Journal's web site is located at http://www.mdpi.com/journal/genes-
dc.relation.ispartofGenes-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.subjectDNA methylation-
dc.subjectDNMT1-
dc.subjectUHRF1-
dc.subjectUSP7-
dc.subjectubiquitination-
dc.titleThe Growing Complexity of UHRF1-Mediated Maintenance DNA Methylation-
dc.typeArticle-
dc.identifier.emailXie, S: xiesi@hku.hk-
dc.identifier.emailQian, C: cmqian@hku.hk-
dc.identifier.authorityQian, C=rp01371-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.3390/genes9120600-
dc.identifier.scopuseid_2-s2.0-85058512224-
dc.identifier.hkuros306092-
dc.identifier.volume9-
dc.identifier.issue12-
dc.identifier.spage600-
dc.identifier.epage600-
dc.identifier.isiWOS:000454717800034-
dc.publisher.placeSwitzerland-
dc.identifier.issnl2073-4425-

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