MYRF is a membrane-associated transcription factor that autoproteolytically cleaves to directly activate myelin genes
Open accessAbstract
The myelination of axons is a crucial step during vertebrate central nervous system (CNS) development, allowing for rapid and energy efficient saltatory conduction of nerve impulses. Accordingly, the differentiation of oligodendrocytes, the myelinating cells of the CNS, and their expression of myelin genes are under tight transcriptional control. We previously identified a putative transcription factor, Myelin Regulatory Factor (Myrf), as being vital for CNS myelination. Myrf is required for the generation of CNS myelination during development and also for its maintenance in the adult. It has been controversial, however, whether Myrf directly regulates transcription, with reports of a transmembrane domain and lack of nuclear localization. Here we show that Myrf is a membrane-associated transcription factor that undergoes an activating proteolytic cleavage to separate its transmembrane domain-containing C-terminal region from a nuclear-targeted N-terminal region. Unexpectedly, this cleavage event occurs via a protein domain related to the autoproteolytic intramolecular chaperone domain of the bacteriophage tail spike proteins, the first time this domain has been found to play a role in eukaryotic proteins. Using ChIP-Seq we show that the N-terminal cleavage product directly binds the enhancer regions of oligodendrocyte-specific and myelin genes. This binding occurs via a defined DNA-binding consensus sequence and strongly promotes the expression of target genes. These findings identify Myrf as a novel example of a membrane-associated transcription factor and provide a direct molecular mechanism for its regulation of oligodendrocyte differentiation and CNS myelination.
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The proximal 300 bp human MAG promoter fragment contains evolutionarily conserved binding sites for MRF and RNF10.
“Finally, we also selected the proximal 300 bp fragment for further characterization as it contains evolutionary conserved binding sites for myelin gene regulatory factor (MRF) and Ring Finger Protein 10 (RNF10), critical activators of myelination in oligodendrocytes or Schwann cells, respectively (Hoshikawa et al., 2008; Emery et al., 2009; Bujalka et al., 2013).”
From Recombinant Human Myelin-Associated Glycoprotein Promoter Drives Selective AAV-Mediated Transgene Expression in Oligodendrocytes (2016) · cites this paper as Bujalka et al., 2013
The Results section, “MYRF Binds DNA Via a Defined Consensus Sequence” (page not provided), identifies a MYRF-binding motif near Mag and reports that mutating it abolished MYRF-dependent reporter activity. The cited passages do not establish that this site lies within the proximal 300 bp of the human MAG promoter, that it is evolutionarily conserved, or that the fragment contains an RNF10-binding site. (LLM, conf=0.88)
Experimental — accuracy not yet measuredThis transition was accompanied by reduced activity of myelin-associated gene networks and diminished regulon activity of key transcriptional regulators, including MYRF and NKX6-2, which serve as central regulators of myelin gene expression programs.
“This transition was accompanied by reduced activity of myelin-associated gene networks and diminished regulon activity of key transcriptional regulators, including MYRF and NKX6-2, which serve as central regulators of myelin gene expression programs (53-55) (Fig. 5J).”
From Molecular and cellular processes disrupted in the early postnatal Down syndrome prefrontal cortex (2026) · cites this paper as [53]
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Experimental — accuracy not yet measuredThere is an early upregulation of a gamma-secretase component (NCSTN), the transcription factor MYRF, and a structural component of myelin (PLLP).
“Additionally, there is an early upregulation of a gamma-secretase component (NCSTN), the transcription factor MYRF, which regulates myelination76, and a structural component of myelin itself (PLLP) (Fig. 7e, left, and Fig. 7g).”
From Integrated multimodal cell atlas of Alzheimer’s disease (2024) · cites this paper as [76]
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Myelin gene regulatory factor is a critical transcriptional regulator required for CNS myelination
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“To further investigate the subcellular localization of the cleavage products we transfected the CG-4 oligodendroglial cell line [20] with the Myc-MYRF-FLAG construct.”
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Yu, Y., Chen, Y., Kim, B., Wang, H., Zhao, C., He, X., Liu, L., Liu, W., Wu, L. M. N., Mao, M., et al. (2013) · Cell · doi:10.1016/j.cell.2012.12.006 · Cited by 375 · cited 5× · see citing works
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BackgroundCrystal structure of the polysialic acid–degrading endosialidase of bacteriophage K1F
Stummeyer, K., Dickmanns, A., Mühlenhoff, M., Gerardy‐Schahn, R., & Ficner, R. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb874 · Cited by 215 · see citing works
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“We have previously demonstrated that Myrf is required for oligodendrocyte differentiation and the generation and maintenance of CNS myelin [13,14].”
BackgroundMapping accessible chromatin regions using Sono-Seq
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MethodInfluentialAscl1 is required for oligodendrocyte development in the spinal cord
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“Recent reports indicate that its expression may be influenced by the coordinated activity of Olig2 and Brg1 [3] and by posttranscriptional regulation by miRNAs [37].”
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“The UniProt mouse MYRF sequence (accession number Q3UR85) was submitted to several subcellular targeting motif and feature predictors including ELM [46], PSORTII [47], NucPred [48], TMPRED [49], HMMTOP [50], Das-TMfilter [51], Toppred II [52], Paircoil2 [53], and to the protein databases PFAM [54] and Prosite [55].”
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“MYRF [8,9,13], it is tempting to speculate the two factors may”
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“The second is the perfectly conserved GVIAQ sequence corresponding to the region required for trimerization of the phage proteins [21].”
BackgroundZFP191 is required by oligodendrocytes for CNS myelination.Preprint
Howng, S. B., Avila, R., Emery, B., Traka, M., Lin, W.-S., Watkins, T. A., Cook, S., Bronson, R., Davisson, M. L., Barres, B., et al. (2010) · Genes & Development · doi:10.1101/gad.1864510 · Cited by 81 · cited 1× · see citing works
“2 [5], Ascl1/Mash1 [6], Zfp191 [7], and Sox10 [8,9].”
Embryonic stem cell-based system for mapping developmental transcriptional programs
Mazzoni, E. O., Mahony, S., Iacovino, M., Morrison, C. A., Mountoufaris, G., Closser, M., Whyte, W. A., Young, R. A., Kyba, M., Gifford, D. K., et al. (2011) · Europe PMC (PubMed Central) · doi:10.1038/nmeth.1775 · Cited by 79 · cited 1× · see citing works
“between the peaks identified with each method [24,25].”
MethodCrystal structure of an intramolecular chaperone mediating triple–β-helix folding
Schulz, E. C., Dickmanns, A., Urlaub, H., Schmitt, A., Mühlenhoff, M., Stummeyer, K., Schwarzer, D., Gerardy‐Schahn, R., & Ficner, R. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1746 · Cited by 74 · see citing works
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“These results reconcile previous reports that propose transmembrane/endoplasmic reticulum localization and nontranscription factor function of the family [15,16] and reports that have proposed a family of transcription factors defined by yeast Ndt80 and including MrfA in Dictyostelium and MYRF in mice [11,13,32].”
BackgroundInfluentialRegulation of the C. elegans molt by pqn-47
Russel, S., Frand, A. R., & Ruvkun, G. (2011) · Developmental Biology · doi:10.1016/j.ydbio.2011.09.025 · Cited by 39 · cited 3× · see citing works
“[15] note, the overall degree of sequence homology between Ndt80 and MYRF is quite low, however a recent report found that the key residues required for DNA binding by Ndt80 are also required for DNA binding by dictostelium MrfA [32].”
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Yao, Z., Fong, A. P., Cao, Y., Ruzzo, W. L., Gentleman, R. C., & Tapscott, S. J. (2013) · Skeletal Muscle · doi:10.1186/2044-5040-3-8 · Cited by 25 · cited 1× · see citing works
“between the peaks identified with each method [24,25].”
MethodSenoo, H., Wang, H.-Y., Araki, T., Williams, J. G., & Fukuzawa, M. (2012) · The International Journal of Developmental Biology · doi:10.1387/ijdb.120030jw · Cited by 21 · cited 6× · see citing works
“[15] note, the overall degree of sequence homology between Ndt80 and MYRF is quite low, however a recent report found that the key residues required for DNA binding by Ndt80 are also required for DNA binding by dictostelium MrfA [32].”
BackgroundResultInfluentialFingerman, I. M. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh625 · Cited by 18 · cited 9× · see citing works
“These results reconcile previous reports that propose transmembrane/endoplasmic reticulum localization and nontranscription factor function of the family [15,16] and reports that have proposed a family of transcription factors defined by yeast Ndt80 and including MrfA in Dictyostelium and MYRF in mice [11,13,32].”
BackgroundResultInfluentialStöhr, H., Marquardt, A., White, K., & Weber, B. H. F. (2000) · Cytogenetic and Genome Research · doi:10.1159/000015552 · Cited by 17 · cited 3× · see citing works
“[16], a transmembrane region was predicted by a number of programs at residues 767–789.”
BackgroundResult
Flagged first, then by citations
Cited by
Sorted by citations
Motor skill learning requires active central myelination
McKenzie, I. A., Ohayon, D., Li, H., Paes de Faria, J., Emery, B., Tohyama, K., & Richardson, W. D. (2014) · Science · doi:10.1126/science.1254960 · Cited by 1,177 · see citing works
Self-citationOligodendrocytes: Myelination and Axonal SupportPreprint
Simons, M., & Nave, K. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a020479 · Cited by 862 · see citing works
“2, Olig1, Sox10, YY1, and Zfp191, are turned on (He et al. 2007; Wegner 2008; Emery et al. 2009; Howng et al. 2010; Meijer et al. 2012; Bujalka et al. 2013).”
Integrated multimodal cell atlas of Alzheimer’s disease
Gabitto, M. I., Travaglini, K. J., Rachleff, V. M., Kaplan, E. S., Long, B., Ariza, J., Ding, Y., Mahoney, J. T., Dee, N., Goldy, J., et al. (2024) · Nature Neuroscience · doi:10.1038/s41593-024-01774-5 · Cited by 397 · see citing works
“Additionally, there is an early upregulation of a gamma-secretase component ( NCSTN ), the transcription factor MYRF, which regulates myelination 76 , and a structural component of myelin itself (PLLP) (Fig.”
Induction of myelinating oligodendrocytes in human cortical spheroids
Madhavan, M., Nevin, Z. S., Shick, H. E., Garrison, E., Clarkson-Paredes, C., Karl, M., Clayton, B. L. L., Factor, D. C., Allan, K. C., Barbar, L., et al. (2018) · Nature Methods · doi:10.1038/s41592-018-0081-4 · Cited by 353 · see citing works
Myelin plasticity: sculpting circuits in learning and memory
Xin, W., & Chan, J. R. (2020) · Nature Reviews Neuroscience · doi:10.1038/s41583-020-00379-8 · Cited by 329 · see citing works
Emery, B., & Lu, Q. R. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a020461 · Cited by 293 · see citing works
“Genome-wide binding studies (ChIP-Seq) found that Myrf directly targets a wide range of genes underpinning the morphological development and myelination by OLs, including cytoskeletal genes, lipid metabolism genes, other transcription factors, such as Smad7 (see above) and Nkx6-2 (see below), and the more well-studied…”
BackgroundInfluentialvan Tilborg, E., de Theije, C. G. M., van Hal, M., Wagenaar, N., de Vries, L. S., Benders, M. J. N. L., Rowitch, D. H., & Nijboer, C. H. A. (2017) · Glia · doi:10.1002/glia.23256 · Cited by 292 · see citing works
“The disinhibition allows OPCs to differentiate into pre-OLs and finally into mature, myelinating OLs under the influence of differentiation promoting transcription factors like myelin regulatory factor (Myrf) (Bujalka et al., 2013).”
Molecular Control of Oligodendrocyte Development
Elbaz, B., & Popko, B. (2019) · Trends in Neurosciences · doi:10.1016/j.tins.2019.01.002 · Cited by 286 · see citing works
“Its activity is controlled by complex post-translational processing – MYRF activation requires self-cleavage, which results in the release of its N-terminal fragment [19].”
BackgroundTranscriptional Convergence of Oligodendrocyte Lineage Progenitors during Development
Marques, S., van Bruggen, D., Vanichkina, D. P., Floriddia, E. M., Munguba, H., Väremo, L., Giacomello, S., Falcão, A. M., Meijer, M., Björklund, Å. K., et al. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.07.005 · Cited by 290 · see citing works
Metabolism and functions of lipids in myelin
Schmitt, S., Cantuti‐Castelvetri, L., & Simons, M. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.12.016 · Cited by 259 · see citing works
Mechanisms regulating the development of oligodendrocytes and central nervous system myelin.
Mitew, S., Hay, C., Peckham, H., Xiao, J., Koenning, M., & Emery, B. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2013.11.029 · Cited by 259 · see citing works
“…with a continued role in the regulation of myelin genes in the mature cells, ChIP-Seq experiments demonstrate that binding of MYRF to DNA is enriched in the vicinity of known myelin genes and other transcripts highly expressed by oligodendrocytes (Cahoy et al., 2008, Bujalka et al., 2013).”
BackgroundInfluentialHerring, C. A., Simmons, R. K., Freytag, S., Poppe, D., Moffet, J. J. D., Pflueger, J., Buckberry, S., Vargas-Landín, D. B., Clément, O., Goñi, E., et al. (2022) · Cell · doi:10.1016/j.cell.2022.09.039 · Cited by 226 · see citing works
“For example, MYRF, encoding a TF required for myelination, has a promoter OCR with high accessibility in ODCs starting in childhood, coinciding with myelination and MYRF expression (Figures 5C and S5G; Bujalka et al., 2013).”
Zhao, J., Liu, Y., Zhang, W., Zhou, Z., Wu, J., Cui, P., Zhang, Y., & Huang, G. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1078034 · Cited by 232 · see citing works
“Among our validated 3 down-regulated lncRNAs, Linc00261 is intergenic and transcribed from the minus strand of chr20; DKFZP434K028 is located at the intronic antisense of MYRF gene, and MYRF encodes a membrane-bound transcription factor that autoproteolytically cleaves to activate myelin genes.(32) RPL34AS1 is a bidir…”
BackgroundHornig, J., Fröb, F., Vogl, M. R., Hermans-Borgmeyer, I., Tamm, E. R., & Wegner, M. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003907 · Cited by 228 · see citing works
“Myrf has a DNA-binding domain of its own, and its preferential binding site has recently been determined bioinformatically, but not yet confirmed by EMSA [34].”
BackgroundInfluentialSelf-citationHuang, B., Wei, W., Wang, G., Gaertig, M. A., Feng, Y., Wang, W., Li, X., & Li, S. (2015) · Neuron · doi:10.1016/j.neuron.2015.02.026 · Cited by 181 · see citing works
CNS myelination and remyelination depend on fatty acid synthesis by oligodendrocytes
Dimas, P., Montani, L., Pereira, J. A., Moreno, D., Trötzmüller, M., Gerber, J., Semenkovich, C. F., Köfeler, H. C., & Suter, U. (2019) · eLife · doi:10.7554/elife.44702 · Cited by 178 · see citing works
Figlia, G., Gerber, D., & Suter, U. (2018) · Glia · doi:10.1002/glia.23273 · Cited by 165 · see citing works
“First, Myrf and Krox20, the master transcription factors for CNS and PNS myelination, respectively, bind to regulatory regions of genes involved in lipid synthesis (Bujalka et al., 2013; Jang et al., 2010).”
Backgroundm6A mRNA methylation is essential for oligodendrocyte maturation and CNS myelination
Xu, H., Dzhashiashvili, Y., Shah, A., Kunjamma, R. B., Weng, Y.-L., Elbaz, B., Fei, Q., Jones, J., Li, Y. I., Zhuang, X., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.12.013 · Cited by 142 · see citing works
Yang, H., Vainshtein, A., Maik-Rachline, G., & Peles, E. (2016) · Nature Communications · doi:10.1038/ncomms10884 · Cited by 150 · see citing works
Impaired oligodendrocyte maturation in preterm infants: Potential therapeutic targets
van Tilborg, E., Heijnen, C. J., Benders, M. J. N. L., van Bel, F., Fleiss, B., Gressèns, P., & Nijboer, C. H. A. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.11.002 · Cited by 148 · see citing works
“Furthermore, miRNA-199a is thought to interact with transcription factor MYRF, an important transcription factor regulating the expression of myelin-associated genes (Bujalka et al., 2013; Emery et al., 2009; Letzen et al., 2010).”
Myelinogenic Plasticity of Oligodendrocyte Precursor Cells following Spinal Cord Contusion Injury
Assinck, P., Duncan, G. J., Plemel, J. R., Lee, M. J., Stratton, J. A., Manesh, S. B., Liu, J., Ramer, L. M., Kang, S. H., Bergles, D. E., et al. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.2409-16.2017 · Cited by 151 · see citing works
Glial Cell Development and Function in ZebrafishPreprint
Lyons, D. A., & Talbot, W. S. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a020586 · Cited by 143 · see citing works
“Studies in mammals have shown that Sox10 acts together with Olig1 and Myrf to control myelin gene expression (Park et al. 2002; Li et al. 2007, 2011a; Bujalka et al. 2013; Hornig et al. 2013).”
BackgroundOsipovitch, M., Asenjo Martinez, A., Mariani, J. N., Cornwell, A., Dhaliwal, S., Zou, L., Chandler-Militello, D., Wang, S., Li, X., Benraiss, S.-J., et al. (2019) · Cell Stem Cell · doi:10.1016/j.stem.2018.11.010 · Cited by 120 · see citing works
“This results in the suppression of myelination, which requires the MYRF-dependent transcription of critical mRNAs associated with myelin biogenesis, such as MAG and MBP (Bujalka et al., 2013; Emery et al., 2009).”
BackgroundChromatin Landscape Defined by Repressive Histone Methylation during Oligodendrocyte Differentiation
Liu, J., Magri, L., Zhang, F., Marsh, N. O., Albrecht, S., Huynh, J. L., Kaur, J., Kuhlmann, T., Zhang, W., Slesinger, P. A., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.2606-14.2015 · Cited by 123 · see citing works
“Although several studies have characterized the molecular events occurring in the initiation stage of OPC differentiation to activate the lineage progression program (Bujalka et al., 2013; Yu et al., 2013), the precise molecular mechanisms de4”
BackgroundQi, H., Yu, L., Zhou, X., Wynn, J., Zhao, H., Guo, Y., Zhu, N., Kitaygorodsky, A., Hernan, R., Aspelund, G., et al. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007822 · Cited by 119 · see citing works
The fate and function of oligodendrocyte progenitor cells after traumatic spinal cord injury
Duncan, G. J., Manesh, S. B., Hilton, B. J., Assinck, P., Plemel, J. R., & Tetzlaff, W. (2019) · Glia · doi:10.1002/glia.23706 · Cited by 117 · see citing works
Myelin regulatory factor drives remyelination in multiple sclerosis
Duncan, G. J., Plemel, J. R., Assinck, P., Manesh, S. B., Muir, F. G. W., Hirata, R., Berson, M., Liu, J., Wegner, M., Emery, B., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1741-7 · Cited by 115 · see citing works
“MYRF can directly bind putative enhancer sequences of myelin genes, such as Mbp and Plp, to induce their expression [5] and together with the transcription factor Sox10, synergistically promote myelin gene expression [11, 25].”
BackgroundDNA damage in the oligodendrocyte lineage and its role in brain aging
Tse, K.-H., & Herrup, K. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.05.006 · Cited by 108 · see citing works
“To induce differentiation, MyRF partners with SOX10 to induce transcription of myelin-related genes including myelin basic protein (MBP), proteolipid protein (PLP), myelin associated glycoprotein (MAG) and myelin OL glycoprotein (MOG) (Bujalka et al., 2013; Koenning et al., 2012), all of which contain MyRF binding mot…”
BackgroundInfluentialSoxE factors: Transcriptional regulators of neural differentiation and nervous system development
Weider, M., & Wegner, M. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.08.013 · Cited by 107 · see citing works
Oligodendroglia Are Particularly Vulnerable to Oxidative Damage after Neurotrauma In Vivo
Giacci, M. K., Bartlett, C. A., Smith, N. M., Iyer, K. S., Toomey, L. M., Jiang, H., Guagliardo, P. R., Kilburn, M. R., & Fitzgerald, M. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1898-17.2018 · Cited by 111 · see citing works
“However, these newly differentiated oligodendrocytes may not be able to generate myelin due to their substantially reduced levels of MYRF (Emery et al., 2009; Koenning et al., 2012; Bujalka et al., 2013; Hornig et al., 2013).”
Transcriptional control of myelination and remyelination
Sock, E., & Wegner, M. (2019) · Glia · doi:10.1002/glia.23636 · Cited by 109 · see citing works
“In case of Sox10, it has been shown that jointly bound regulatory regions are synergistically activated (Bujalka et al., 2013; Hornig et al., 2013).”
BackgroundInfluentialDifferential Sox10 genomic occupancy in myelinating glia
Lopez‐Anido, C., Sun, G., Koenning, M., Srinivasan, R., Hung, H. A., Emery, B., Keleş, S., & Svaren, J. P. (2015) · Glia · doi:10.1002/glia.22855 · Cited by 100 · see citing works
“Sox10 binding sites overlap with binding of the bHLH factor, Olig2, and Myrf sites obtained by ChIP-Seq in cultured oligodendrocytes (Bujalka et al., 2013); so, we next determined if the overlap is correlated with H3K27ac status.”
BackgroundMethodInfluentialSock, E., & Wegner, M. (2021) · Developmental Neurobiology · doi:10.1002/dneu.22849 · Cited by 85 · see citing works
“Olig2 is for instance also expressed during development in motoneurons, Purkinje cell precursors, and subgroups of astrocyte precursors, where it counteracts astrocytic maturation (Cai et al., 2007; Fukuda et al., 2004; Ju et al., 2016; Q. R. Lu et al., 2000; Q. Zhou et al., 2000).”
BackgroundRole of ERK1/2 MAPK Signaling in the Maintenance of Myelin and Axonal Integrity in the Adult CNS
Ishii, A., Furusho, M., Dupree, J. L., & Bansal, R. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.3360-14.2014 · Cited by 100 · see citing works
“2 reverse primer, 5 -GAGTTCTATCCTCTCC AAAAGTTCAAA-3 ; Olig1 forward primer, 5 -GACCTCAGC CAATCTTCC-3 ; Olig1 reverse primer, 5 -TAACACCCTTGA TGTTTGTACC-3 ; Olig2 forward primer, 5 -TTATTA CAGACCGAGCCAACACC-3 ; Olig2 reverse primer, 5 - GTCGTGCATGCGCTTGCGTT-3 ; Sox10 forward primer, 5 - AGCCCAGGTGAAGACAGAGA-3 ; Sox10 r…”
BackgroundInfluentialImmunological Markers for Central Nervous System Glia
Huang, H., He, W., Tang, T., & Qiu, M.-S. (2022) · Neuroscience Bulletin · doi:10.1007/s12264-022-00938-2 · Cited by 86 · see citing works
“Once cleaved on the ER membrane, the N-terminal trimers of MYRF are released and translocate into the nucleus to function as a transcriptional activator [73, 74].”
BackgroundThe Degradome database: expanding roles of mammalian proteases in life and disease
Pérez-Silva, J. G., Español, Y., Velasco, G., & Quesada, V. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1201 · Cited by 97 · see citing works
Development of myelinating glia: an overview
Cristobal, C. D. D., & Lee, H. K. (2022) · Glia · doi:10.1002/glia.24238 · Cited by 71 · see citing works
“In addition, there is significant overlap between Olig2, Myrf, and Sox10 binding sites, suggesting that myelin gene expression is regulated by all three proteins in mice (Bujalka et al., 2013; Hornig et al., 2013; Yu et al., 2013).”
BackgroundCentral Nervous System Remyelination: Roles of Glia and Innate Immune Cells
Baaklini, C. S., Rawji, K. S., Duncan, G. J., Ho, M. F. S., & Plemel, J. R. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00225 · Cited by 80 · see citing works
“MyRF binds to enhancer sequences and directly drives the expression of myelin genes (Bujalka et al., 2013); it is necessary for remyelination after chemical and traumatic demyelinating injuries (Duncan et al.”
BackgroundThe nuclear transportation routes of membrane-bound transcription factors
Liu, Y., Li, P., Fan, L., & Wu, M. (2018) · Cell Communication and Signaling · doi:10.1186/s12964-018-0224-3 · Cited by 77 · see citing works
Myelin architecture: zippering membranes tightly together
Bakhti, M., Aggarwal, S., & Simons, M. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1492-0 · Cited by 77 · see citing works
Tanga, N., Kuboyama, K., Kishimoto, A., Kiyonari, H., Shiraishi, A., Suzuki, R., Watanabe, T., Fujikawa, A., & Noda, M. (2019) · Glia · doi:10.1002/glia.23583 · Cited by 77 · see citing works
“MYRF proteins exist as the full-length (~150 kDa) and a truncated cleavage product (~80 kDa) (Bujalka et al., 2013), and, thus, all MYRF bands detected were quantified in total.”
BackgroundFrom CNS stem cells to neurons and glia: Sox for everyone
Reiprich, S., & Wegner, M. (2014) · Cell and Tissue Research · doi:10.1007/s00441-014-1909-6 · Cited by 83 · see citing works
“A comparison of ChIP-Seq data sets has revealed that more than 30 % of regions bound by Myrf are simultaneously enriched in Sox10 precipitates arguing for common regulatory functions of both transcription factors (Bujalka et al. 2013).”
BackgroundGarnai, S. J., Brinkmeier, M. L., Emery, B., Alemán, T. S., Pyle, L. C., Veleva-Rotse, B. O., Sisk, R. A., Rozsa, F. W., Ozel, A. B., Li, J. Z., et al. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008130 · Cited by 76 · see citing works
Marin, M. A., & Carmichael, S. T. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.07.023 · Cited by 72 · see citing works
Current Insights Into Oligodendrocyte Metabolism and Its Power to Sculpt the Myelin Landscape
Narine, M., & Colognato, H. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.892968 · Cited by 71 · see citing works
“…factor (Myrf ) are essential for CNS myelination such that when the membrane-bound Myrf protein undergoes an activating cleavage event, its cleavage product can localize into the nucleus to bind and enhance the expression of pro-myelin genes such as Plp1, Mbp, Mag, and Trf (Bujalka et al., 2013).”
BackgroundInfluentialDuncan, I. D., Bugiani, M., Radcliff, A., Moran, J. J., Lopez-Anido, C., Duong, P. C., August, B. K., Wolf, N. I., van der Knaap, M. S., & Svaren, J. (2017) · Annals of Neurology · doi:10.1002/ana.24930 · Cited by 57 · see citing works
Huang, H., Teng, P., Du, J., Meng, J., Hu, X., Tang, T., Zhang, Z., Qi, Y. B., & Qiu, M. S. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.0154-18.2018 · Cited by 66 · see citing works
“In spinal injuries and acute MS lesions, OPCs still exist but fail to differentiate effectively into myelinating oligodendrocytes (Raine and Wu, 1993; Wolswijk, 1998; Chang et al., 2002; Jennings and Carroll, 2010).”
BackgroundReview of the phenotypic spectrum associated with haploinsufficiency of MYRF
Rossetti, L. Z., Glinton, K. E., Yuan, B., Liu, P., Pillai, N. R., Mizerik, E. A., Magoulas, P. L., Rosenfeld, J. A., Karaviti, L. P., Sutton, V. R., et al. (2019) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.61182 · Cited by 66 · see citing works
“The myelin regulatory factor gene (MYRF; MIM# 608329) encodes an endoplasmic reticulummembrane protein that undergoes auto-processing to release its N-terminal fragment which enters the nucleus, forms a homotrimer, and functions as a transcription factor (Bujalka et al., 2013; Kim et al., 2017; Li, Park, & Marcotte, 2…”
BackgroundChen, C. Z.-Y., Neumann, B., Förster, S., & Franklin, R. J. M. (2021) · Open Biology · doi:10.1098/rsob.200352 · Cited by 66 · see citing works
“In turn, Myrf initiates core programs to drive oligodendrocyte differentiation and myelin gene expression, to allow myelination to proceed [39,40].”
BackgroundOlig1 Acetylation and Nuclear Export Mediate Oligodendrocyte Development
Dai, J., Bercury, K., Jin, W.-L., & Macklin, W. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.0882-15.2015 · Cited by 56 · see citing works
“DNA pulldown assays were performed as described previously (Bujalka et al., 2013) with slight modifications.”
Ferrer, I. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.07.004 · Cited by 62 · see citing works
“This is accompanied by increased expression of MBP, MAG, PLP1, MOG and CNP which have MYRF binding motivs in their promoters (Emery et al., 2009; Koenning et al., 2012; Bujalka et al., 2013; McKenzie et al., 2014; Emery and Lu, 2015).”
BackgroundInterplay between exercise and dietary fat modulates myelinogenesis in the central nervous system
Yoon, H., Kleven, A. D., Paulsen, A. R., Kleppe, L. S., Wu, J., Ying, Z., Gómez‐Pinilla, F., & Scarisbrick, I. A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.01.019 · Cited by 61 · see citing works
“and maintaining the oligodendrocyte differentiation program, including the expression of MBP and PLP (Bujalka et al. 2013; Emery et al. 2009).”
Influentialvon Jonquieres, G., Fröhlich, D., Klugmann, C. B., Wen, X., Harasta, A. E., Ramkumar, R., Spencer, Z. H. T., Housley, G. D., & Klugmann, M. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00013 · Cited by 60 · see citing works
“Finally, we also selected the proximal 300 bp fragment for further characterization as it contains evolutionary conserved binding sites for myelin gene regulatory factor (MRF) and Ring Finger Protein 10 (RNF10), critical activators of myelination in oligodendrocytes or Schwann cells, respectively (Hoshikawa et al., 20…”
BackgroundMethodMyrf guides target gene selection of transcription factor Sox10 during oligodendroglial development
Aprato, J., Sock, E., Weider, M., Elsesser, O., Fröb, F., & Wegner, M. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz1158 · Cited by 60 · see citing works
“From ChIP-Seq experiments, 5′-CTGGYAC-3′ had been identified as consensus motif for Myrf binding in the genome (9).”
BackgroundMethodResultInfluentialMyelination induces axonal hotspots of synaptic vesicle fusion that promote sheath growth
Almeida, R., Williamson, J., Madden, M., Early, J. J., Voas, M. G., Talbot, W. S., Bianco, I. H., & Lyons, D. A. (2021) · Current Biology · doi:10.1016/j.cub.2021.06.036 · Cited by 57 · see citing works
Evolution of the CNS myelin gene regulatory program
Li, H., & Richardson, W. (2015) · Brain Research · doi:10.1016/j.brainres.2015.10.013 · Cited by 53 · see citing works
“…membrane-bound Myrf also forms trimers via a leucine zipper in the ICA domain; after self-cleavage, the detached N-terminal trimer of Myrf containing the DNA-binding domain translocates from ER into the nucleus to execute transcriptional regulation (Bujalka et al., 2013; Li et al., 2013).”
BackgroundPinz, H., Pyle, L. C., Li, D., Izumi, K., Skraban, C. M., Tarpinian, J. M., Braddock, S. R., Telegrafi, A. B., Monaghan, K. G., Zackai, E. H., et al. (2018) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.38620 · Cited by 58 · see citing works
“MYRF is a membrane-associated transcription factor that is activated through autocatalytic cleavage via the peptidase S74 domain to bind the enhancer region of target genes (Bujalka et al., 2013).”
BackgroundDNA Extraction and Purification
Dhaliwal, A. (2013) · Materials and Methods · doi:10.13070/mm.en.3.191 · Cited by 57 · see citing works
Oligodendrocytes in intracerebral hemorrhage
Kang, M., & Yao, Y. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13193 · Cited by 57 · see citing works
Castranio, E. L., Mounier, A., Wolfe, C. M., Nam, K. N., Fitz, N. F., Letronne, F., Schug, J., Koldamova, R. P., & Lefterov, I. M. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.05.006 · Cited by 55 · see citing works
Cantone, M., Küspert, M., Reiprich, S., Lai, X., Eberhardt, M., Göttle, P., Beyer, F., Azim, K., Küry, P., Wegner, M., et al. (2019) · Glia · doi:10.1002/glia.23569 · Cited by 56 · see citing works
“, 2016] for Tcf7l2, PMC3742440 [Bujalka et al., 2013] for Myrf, and GSE64703 [Lopez-Anido et al.”
BackgroundInfluentialKim, D., Choi, J., Fan, C., Shearer, R. S., Sharif, M. A., Busch, P., & Park, Y. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx080 · Cited by 55 · see citing works
“When expressed alone, the N-terminal fragment of Flag-hMyrf was localized to the nucleus while that of Myc-hMyrf-K583A was excluded from it (Figure 3A), as previously reported (14,15).”
BackgroundMethodResultInfluentialSomethiNG 2 talk about-Transcriptional regulation in embryonic and adult oligodendrocyte precursors.
Küspert, M., & Wegner, M. (2016) · Brain Research · doi:10.1016/j.brainres.2015.07.024 · Cited by 48 · see citing works
Laminin regulates oligodendrocyte development and myelination
Kang, M., & Yao, Y. (2021) · Glia · doi:10.1002/glia.24117 · Cited by 53 · see citing works
MYRF is associated with encephalopathy with reversible myelin vacuolization
Kurahashi, H., Azuma, Y., Masuda, A., Okuno, T., Nakahara, E., Imamura, T., Saitoh, M., Mizuguchi, M., Shimizu, T., Ohno, K., et al. (2017) · Annals of Neurology · doi:10.1002/ana.25125 · Cited by 53 · see citing works
“1208A>G Variant The N-terminal region of MYRF contains a DBD, which regulates the transcription of myelin genes.(16,22) The c.”
BackgroundDrug discovery for remyelination and treatment of MS
Marshall-Phelps, K. L., Early, J. J., & Lyons, D. A. (2017) · Glia · doi:10.1002/glia.23166 · Cited by 48 · see citing works
“also used the Oli-neu cell line, but in an attempt to overcome its limitations, overexpressed the transcription factor MyRF to drive myelin gene expression (Bujalka et al., 2013; Emery et al., 2009), prior to their screen (Porcu et al.”
MethodTeriflunomide promotes oligodendroglial differentiation and myelination
Göttle, P., Manousi, A., Kremer, D., Reiche, L., Hartung, H., & Küry, P. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1110-z · Cited by 47 · see citing works
“In the present study, we demonstrate that teriflunomide induces transcriptional regulators required for proper oligodendroglial cell differentiation such as Mash1/Ascl1, Sox 10, Myrf [23], Nkx2.”
InfluentialRemyelination protects neurons from DLK-mediated neurodegeneration
Duncan, G. J., Ingram, S. D., Emberley, K., Hill, J. E., Cordano, C., Abdelhak, A., McCane, M., Jenks, J. E., Jabassini, N., Ananth, K., et al. (2023) · bioRxiv · doi:10.1038/s41467-024-53429-5 · Cited by 28 · see citing works
MicroRNAs in oligodendrocyte development and remyelination
Ngo, C., & Kothary, R. (2022) · Journal of Neurochemistry · doi:10.1111/jnc.15618 · Cited by 42 · see citing works
“Lamin B1 over- expression leads to defective subcellular localization of MBP and PLP and decreased branching of maturing oligodendrocytes in vitro.”
BackgroundInfluentialGuo, C., Zhao, Z., Chen, D., He, S., Sun, N., Li, Z., Liu, J., Zhang, D., Zhang, J., Li, J., et al. (2019) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.18-26275 · Cited by 41 · see citing works
White matter alterations in Alzheimer’s disease without concomitant pathologies
Ferrer, I., & Andrés‐Benito, P. (2020) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12618 · Cited by 40 · see citing works
Meng, J., Ma, X., Tao, H., Jin, X. M., Witvliet, D. K., Mitchell, J. K., Zhu, M., Dong, M., Zhen, M., Jin, Y., et al. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.03.022 · Cited by 39 · see citing works
“elegans is consistent with the findings on mammalian MYRF, which have suggested that MYRF may undergo self-cleavage in the ER membrane, releasing its N-terminal fragment to the nucleus (Bujalka et al., 2013; Li et al., 2013).”
BackgroundMethodResultInfluentialExtrinsic Factors Driving Oligodendrocyte Lineage Cell Progression in CNS Development and Injury
Baydyuk, M., Morrison, V. E., Gross, P. S., & Huang, J. K. (2020) · Neurochemical Research · doi:10.1007/s11064-020-02967-7 · Cited by 41 · see citing works
Interplay between transcriptional control and chromatin regulation in the oligodendrocyte lineage
Hernandez, M., & Casaccia, P. (2015) · Glia · doi:10.1002/glia.22818 · Cited by 39 · see citing works
“MYRF is a membrane-bound transcription factor that undergoes an activating proteolytic cleavage, allowing the Nterminal domain to directly bind enhancer regions specific to oligodendrocyte and myelin genes to regulate transcription during differentiation (Bujalka et al., 2013).”
BackgroundThe function of contactin‐2/TAG‐1 in oligodendrocytes in health and demyelinating pathology
Zoupi, L., Savvaki, M., Kalemaki, K., Kalafatakis, I., Sidiropoulou, K., & Karagogeos, D. (2018) · Glia · doi:10.1002/glia.23266 · Cited by 29 · see citing works
“Interestingly, Myrf can directly target genes important in oligodendrocyte development like mag, plp1 and mbp while an active myrf binding region was identified for the Cntn2 gene (Bujalka et al., 2013).”
BackgroundPhosphorylation State of ZFP24 Controls Oligodendrocyte Differentiation
Elbaz, B., Aaker, J., Isaac, S., Kolarzyk, A., Brugarolas, P., Eden, A., & Popko, B. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.089 · Cited by 35 · see citing works
“A uthor M anuscript A uthor M anuscript A uthor M anuscript A uthor M anuscript for OLIG2 (Yu et al., 2013), SOX10 (Lopez-Anido et al., 2015), and MYRF (Bujalka et al., 2013) were converted to mm10 using UCSC liftover.”
BackgroundMethodInfluentialRamamurthy, E., Welch, G., Cheng, J., Yuan, Y., Gunsalus, L. M., Bennett, D. A., Tsai, L., & Pfenning, A. R. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.948456 · Cited by 39 · see citing works
“MYRF, a transcription factor which directly activates myelination (Bujalka et al., 2013) and has been previously linked to LOAD risk (Vardarajan et al.”
BackgroundIdentifying oligodendrocyte enhancers governing Plp1 expression
Kim, D., An, H., Fan, C., & Park, Y. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab184 · Cited by 35 · see citing works
Hamanaka, K., Takata, A., Uchiyama, Y., Miyatake, S., Miyake, N., Mitsuhashi, S., Iwama, K., Fujita, A., Imagawa, E., Alkanaq, A. N., et al. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz066 · Cited by 34 · see citing works
Cheng, G. W.-Y., Mok, K. K.-S., Yeung, S. H.-S., Kofler, J., Herrup, K., & Tse, K.-H. (2022) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlac054 · Cited by 36 · see citing works
Ulk4 deficiency leads to hypomyelination in mice
Liu, M., Xu, P., Guan, Z., Qian, X., Dockery, P., FitzGerald, U., O’Brien, T., & Shen, S. (2017) · Glia · doi:10.1002/glia.23236 · Cited by 35 · see citing works
“Myrf is a marker for post-mitotic oligodendrocytes and vital for generation and maintenance of myelination (Bujalka et al., 2013).”
BackgroundAge-dependent decline in remyelination capacity is mediated by apelin–APJ signaling
Ito, M., Muramatsu, R., Kato, Y., Sharma, B., Uyeda, A., Tanabe, S., Fujimura, H., Kidoya, H., Takakura, N., Kawahara, Y., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00041-7 · Cited by 34 · see citing works
Nicotinic acetylcholine receptors mediate donepezil‐induced oligodendrocyte differentiation
Imamura, O., Arai, M., Dateki, M., Ogata, T., Uchida, R., Tomoda, H., & Takishima, K. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13294 · Cited by 35 · see citing works
“(2015) 135, 1086--1098 found that the N-terminal cleavage product of MYRF directly binds to a wide range of genes involved in myelination (Bujalka et al. 2013).”
BackgroundBernhardt, C., Sock, E., Fröb, F., Hillgärtner, S., Nemer, M. J., & Wegner, M. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac953 · Cited by 34 · see citing works
“The triple combination of KLF9, SOX10 and MYRF elicited a massive 1408-fold activation (Figure 4J).”
BackgroundInfluentialSung, H.-Y., Chen, W., Huang, H., Wang, C., Chang, S., & Tzeng, S. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14788 · Cited by 34 · see citing works
“In addition, given that Myrf is vital for CNS myelination and mediates the production of myelin proteins (Emery et al. 2009; Bujalka et al. 2013), the inhibition of Myrf expression in the IL33KD OPCs coincided with the down-regulation of myelin proteins (MBP and PLP) in the IL33-KD OLGs.”
BackgroundRegulators of Oligodendrocyte DifferentiationPreprint
Emery, B., & Wood, T. L. (2024) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041358 · Cited by 35 · see citing works
MicroRNA and transcriptional crosstalk in myelinating glia
Svaren, J. P. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.06.010 · Cited by 33 · see citing works
“, 2010), and there is also Myrf binding in the miR219-2 locus (Bujalka et al., 2013) that would account for its induction during CNS myelination.”
BackgroundInfluentialSamudyata, S., Castelo‐Branco, G., & Liu, J. (2020) · Glia · doi:10.1002/glia.23820 · Cited by 31 · see citing works
“, 2018), whose expression is involved in a feed-forward transcriptional network that regulates lineage progression (Emery, 2013).”
BackgroundStroke in CNS white matter: Models and mechanisms
Marin, M. A., & Carmichael, S. T. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.07.039 · Cited by 33 · see citing works
“involved in OPC differentiation, was induced prior to the training (Bujalka et al., 2013; McKenzie et al., 2014).”
BackgroundHypoxia and myelination deficits in the developing brain
Singh, D. K., Ling, E., & Kaur, C. (2018) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2018.06.012 · Cited by 31 · see citing works
“Another transcription factor, the myelin regulatory factor (Myrf), promotes the OPCs differentiation into pre-oligodendrocytes and ultimately into mature oligodendrocyte (Bujalka et al., 2013).”
BackgroundCross, S. H., McKie, L., Hurd, T. W., Riley, S., Wills, J. C., Barnard, A. R., Young, F., MacLaren, R. E., & Jackson, I. J. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1008583 · Cited by 32 · see citing works
“MYC-MYRF-FLAG and MYC-MYRFΔ19FLAG have been described [39].”
Tong, L., Deng, Y.-B., Du, W., Zhou, W., Liao, X.-Y., & Jiang, X. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.914153 · Cited by 31 · see citing works
“Using chromatin-immunoprecipitation-sequencing (ChIP-Seq), the finding demonstrated that the N-terminal cleavage product directly binds the regulatory regions of several myelin-associated genes, such as Mbp, Plp, and Mag (Bujalka et al., 2013).”
BackgroundMuth, K. N., Piefke, S., Weider, M., Sock, E., Hermans‐Borgmeyer, I., Wegner, M., & Küspert, M. (2016) · Glia · doi:10.1002/glia.23044 · Cited by 32 · see citing works
“ChIP-Seq data furthermore mapped Myrf binding to the proximal Dusp15 promoter at 2148 bp relative to the transcriptional start site in differentiating oligodendrocytes (Bujalka et al., 2013).”
BackgroundMethodInfluentialDonkels, C., Peters, M., Núñez, M. T. F., Nakagawa, J. M., Kirsch, M., Vlachos, A., Scheiwe, C. F., Schulze‐Bonhage, A., Prinz, M., Beck, J., et al. (2019) · Epilepsia · doi:10.1111/epi.16415 · Cited by 30 · see citing works
Kornfeld, S. F., Cummings, S. E., Fathi, S., Bonin, S. R., & Kothary, R. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.29910 · Cited by 31 · see citing works
“moting protein (TPPP), and myelin basic protein (MBP), amongst others (Bujalka et al., 2013; Emery et al., 2009; Koenning et al., 2012).”
BackgroundInsights into White Matter Defect in Huntington’s Disease
Sun, Y., Tong, H., Yang, T., Liu, L., Li, X., & Li, S. (2022) · Cells · doi:10.3390/cells11213381 · Cited by 30 · see citing works
Novel truncation mutations in MYRF cause autosomal dominant high hyperopia mapped to 11p12–q13.3
Xiao, X., Sun, W., Ouyang, J., Li, S., Jia, X., Tan, Z., Hejtmancik, J. F., & Zhang, Q. (2019) · Human Genetics · doi:10.1007/s00439-019-02039-z · Cited by 30 · see citing works
Phosphorylation of myelin regulatory factor by PRKG2 mediates demyelination in Huntington's disease
Yin, P., Liu, Q., Pan, Y., Yang, W., Yang, S., Wei, W., Chen, X.-X., Hong, Y., Bai, D., Li, X., et al. (2020) · EMBO Reports · doi:10.15252/embr.201949783 · Cited by 28 · see citing works
“It is known that N-terminal fragment of MYRF (nMYRF) is generated by cleavage of full-length MYRF in the cytoplasm and then moves into nucleus to activate myelin gene transcription in oligodendrocytes [24,25].”
Ornelas, I. M., Khandker, L., Wahl, S., Hashimoto, H., Macklin, W. B., & Wood, T. L. (2020) · Glia · doi:10.1002/glia.23776 · Cited by 29 · see citing works
“Sox10 induce myelin gene expression (Bujalka et al., 2013; Stolt et al., 2002), while the transcription factors Tcf4 and Sox17 have stagespecific functions and are also required for oligodendrocyte differenti-”
BackgroundShaw, J. C., Crombie, G. K., Palliser, H. K., & Hirst, J. J. (2021) · Frontiers in Pediatrics · doi:10.3389/fped.2021.618052 · Cited by 28 · see citing works
“Once OPCs have matured into pre-oligodendrocytes (pre-OLs) they differentiate under the control of a number of transcription factors, but one of the most crucial is known as myelin regulatory factor (Myrf ) (16, 22).”
Background
- Authors
- Bujalka, H., Koenning, M., Jackson, S., Perreau, V. M., Pope, B., Hay, C. M., Mitew, S., Hill, A. F., Lu, Q. R., Wegner, M., Srinivasan, R., Svaren, J., Willingham, M., Barres, B. A., & Emery, B.
- Affiliations
- The University of Melbourne (AU)
- Friedrich-Alexander-Universität Erlangen-Nürnberg (DE)
- University of Wisconsin–Madison (US)
- Stanford University (US)
- Corresponding author
- Emery, Ben
- ORCID
- Venue
- PLoS Biology
- Publisher
- Public Library of Science (PLoS)
- Published
- 2013-08-13
- Volume
- 11
- Issue
- 8
- Pages
- e1001625
- ISSN
- 1544-9173 (ISSN-L)
- 1545-7885
- PMC
- PMC3742440
- OpenAlex
- W2085442517
- Cited by
- 271
- References
- 60
- Citations by year
- 2026: 18 · 2025: 20 · 2024: 24 · 2023: 23 · 2022: 24 · 2021: 26 · 2020: 19 · 2019: 26 · 2018: 23 · 2017: 22 · 2016: 11 · 2015: 17 · 2014: 7 · 2013: 7 · 2012: 4
- FWCI
- 5.19
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS Biology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Minerva Access (University of Melbourne) (submittedVersion, cc-by)
- Victoria University Research Repository (Victoria University) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- OPUS FAU (Kooperativer Bibliotheksverbund Berlin-Brandenburg (KOBV), on behalf of the Universitätsbibliothek Erlangen-Nürnberg) (submittedVersion, other-oa)
- Funders
- Myelin Repair Foundation
- Multiple Sclerosis Australia
- Trish Multiple Sclerosis Research Foundation
- National Institutes of Health (NIH-R01)
- Medical Research Council
- National Health and Medical Research Council (1009095)
- National Eye Institute (R01EY010257, R01 EY10257)
- National Institute of Neurological Disorders and Stroke (R01NS075243, R01NS078092)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (P30HD003352)
- Topics
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Health Sciences › Medicine › Pathology and Forensic Medicine › Multiple Sclerosis Research Studies
- Keywords
- MYRF, autoproteolytic cleavage, oligodendrocyte differentiation, CNS myelination, enhancer binding, nuclear localization
- MeSH terms
- Animals, Cell Line, Cells, Cultured, Gene Expression Regulation, Humans, Membrane Proteins, Myelin Sheath, Oligodendroglia, Transcription Factors, Mutagenesis, Site-Directed, Chromatin Immunoprecipitation, Mice
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