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Activity-dependent phosphorylation of MeCP2 threonine 308 regulates interaction with NCoR
Open accessAbstract
Rett syndrome (RTT) is an X-linked human neurodevelopmental disorder with features of autism and severe neurological dysfunction in females. RTT is caused by mutations in methyl-CpG-binding protein 2 (MeCP2), a nuclear protein that, in neurons, regulates transcription, is expressed at high levels similar to that of histones, and binds to methylated cytosines broadly across the genome. By phosphotryptic mapping, we identify three sites (S86, S274 and T308) of activity-dependent MeCP2 phosphorylation. Phosphorylation of these sites is differentially induced by neuronal activity, brain-derived neurotrophic factor, or agents that elevate the intracellular level of 3',5'-cyclic AMP (cAMP), indicating that MeCP2 may function as an epigenetic regulator of gene expression that integrates diverse signals from the environment. Here we show that the phosphorylation of T308 blocks the interaction of the repressor domain of MeCP2 with the nuclear receptor co-repressor (NCoR) complex and suppresses the ability of MeCP2 to repress transcription. In knock-in mice bearing the common human RTT missense mutation R306C, neuronal activity fails to induce MeCP2 T308 phosphorylation, suggesting that the loss of T308 phosphorylation might contribute to RTT. Consistent with this possibility, the mutation of MeCP2 T308A in mice leads to a decrease in the induction of a subset of activity-regulated genes and to RTT-like symptoms. These findings indicate that the activity-dependent phosphorylation of MeCP2 at T308 regulates the interaction of MeCP2 with the NCoR complex, and that RTT in humans may be due, in part, to the loss of activity-dependent MeCP2 T308 phosphorylation and a disruption of the phosphorylation-regulated interaction of MeCP2 with the NCoR complex.
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“Furthermore, this group found that the interaction between MeCP2 and the NCoR1/SMRT complex was facilitated by the NCoR1/SMRT interaction domain (NID) located at MeCP2 amino acids 285–309 [70,71].”
From Rett syndrome: a neurological disorder with metabolic components (2018) · cites this paper as [71]
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“suggest for the first time that RTT dysfunction is caused by a failure of MECP2 to anchor the HDAC3/NCoR/SMRT complex to chromatin53,54.”
From A suppressor screen in Mecp2 mutant mice implicates cholesterol metabolism in Rett syndrome (2013) · cites this paper as [54]
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“These findings have led to a model wherein MeCP2 serves as a bridge between methylated DNA and the corepressor complex, anchoring the NCoR1/SMRT complex to DNA via its NID and MBD, respectively.”
From Rett syndrome: a neurological disorder with metabolic components (2018) · cites this paper as [71]
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“A subset of MECP2 missense mutations abolish interactions with a transcriptional co-repressor complex containing HDAC3, NCoR1, SMRT, and TBLR1.”
From A suppressor screen in Mecp2 mutant mice implicates cholesterol metabolism in Rett syndrome (2013) · cites this paper as [54]
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“Such mutations recapitulate Rett Syndrome phenotypes in mice”
From A suppressor screen in Mecp2 mutant mice implicates cholesterol metabolism in Rett syndrome (2013) · cites this paper as [54]
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“M ECP2 is a methyl-CpG binding protein implicated in the regulation of neuronal chromatin architecture and gene transcription (1)(2)(3)(4), especially in response to neural activity and experience during postnatal life (5,6).”
From MeCP2 regulates the timing of critical period plasticity that shapes functional connectivity in primary visual cortex (2015) · cites this paper as [6]
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Rett syndrome is caused by mutations in X-linked MECP2, encoding methyl-CpG-binding protein 2
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Metadata
- Authors
- Ebert, D. H., Gabel, H. W., Robinson, N. D., Kastan, N. R., Hu, L. S., Cohen, S., Navarro, A. J., Lyst, M. J., Ekiert, R., Bird, A. P., & Greenberg, M. E.
- Affiliations
- Harvard University (US)
- Wellcome Centre for Cell Biology (GB)
- Corresponding author
- Greenberg, Michael E.
- ORCID
- Venue
- Nature
- Published
- 2013-07
- Volume
- 499
- Issue
- 7458
- Pages
- 341-345
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3922283
- OpenAlex
- W2081756408
- Cited by
- 227
- References
- 27
- Citations by year
- 2026: 8 · 2025: 12 · 2024: 9 · 2023: 12 · 2022: 14 · 2021: 14 · 2020: 12 · 2019: 10 · 2018: 23 · 2017: 21 · 2016: 25 · 2015: 19 · 2014: 33 · 2013: 14
- FWCI
- 20.10
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Wellcome Trust (092076)
- National Institutes of Health (5r01ns048276-15)
- National Institute of Mental Health (K08MH090306, K08MH90306)
- National Institute of General Medical Sciences (T32GM007753)
- National Institute of Neurological Disorders and Stroke (R01-NS-048276)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (P30HD018655, P30HD-18655)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- MeCP2, Rett syndrome, NCoR, nuclear receptor corepressor, transcriptional repression, neuronal activity, brain-derived neurotrophic factor, cyclic AMP, epigenetic regulation, knock-in mice, neurodevelopmental disorders
- MeSH terms
- Animals, Cells, Cultured, Humans, Mutation, Neurons, Phosphorylation, Threonine, Transcription, Genetic, Rett Syndrome, Mice, Methyl-CpG-Binding Protein 2, Co-Repressor Proteins
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