ArticleScientific reports2018
Elucidating the transactivation domain of the pleiotropic transcription factor Myrf.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Persistent Leukoencephalopathy Following H1N1 Infection Associated With a Novel MYRF Variant (p.Gly735Asp).Annals of clinical and translational neurology · 2026Article
- Immune regulation by the SUMO family.Nature reviews. Immunology · 2025Review
- Discovery of oligodendrocyte enhancers that regulate Sox10 expression.PLoS genetics · 2025Article
- Uncovering oligodendrocyte enhancers that control Cnp expression.Human molecular genetics · 2023Article
- A Glance at the Molecules That Regulate Oligodendrocyte Myelination.Current issues in molecular biology · 2022Review
- Identifying oligodendrocyte enhancers governing Plp1 expression.Human molecular genetics · 2021Article
- The LRR-TM protein PAN-1 interacts with MYRF to promote its nuclear translocation in synaptic remodeling.eLife · 2021Article
- Molecular mechanism for the multiple sclerosis risk variant rs17594362.Human molecular genetics · 2019Article
- A principled strategy for mapping enhancers to genes.Scientific reports · 2019Article
- Variants in myelin regulatory factor (MYRF) cause autosomal dominant and syndromic nanophthalmos in humans and retinal degeneration in mice.PLoS genetics · 2019Article
- Functional mechanisms of MYRF DNA-binding domain mutations implicated in birth defects.The Journal of biological chemistryArticle
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Myrf is a newly discovered membrane-bound transcription factor that plays an essential role in as diverse organisms as human, worm, and slime mold. Myrf is generated as a type-II membrane protein in the endoplasmic reticulum (ER). It forms homo-oligomers to undergo auto-cleavage that releases Myrf N-terminal fragment from the ER membrane as a homo-trimer. The homo-trimer of Myrf N-terminal fragments enters the nucleus and binds the Myrf motif to activate transcription. Despite its prominent role as a transcriptional activator, little is known about the transactivation domain of Myrf. Here, we report that the N-terminal-most (NTM) domain of Myrf is required for transcriptional activity and, when fused to a Gal4 fragment, enables it to activate transcription. The transactivation function of the NTM domain did not require homo-trimerization. We also discovered that the NTM domain can be sumoylated at three lysine residues (K123, K208, and K276), with K276 serving as the main acceptor. K276 sumoylation repressed the transactivation function of the NTM domain without affecting the stability or nuclear localization of Myrf N-terminal fragment. In sum, this study identifies the NTM domain as the transactivation domain of Myrf and the potential regulatory impact of its K276 sumoylation.
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