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MeCP2 heterochromatin organization is modulated by arginine methylation and serine phosphorylation

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dc.contributor.author Schmidt, Annika
dc.contributor.author Frei, Jana
dc.contributor.author Poetsch, Ansgar
dc.contributor.author Chittka, Alexandra
dc.contributor.author Aßmann, Chris
dc.contributor.author Lehmkuhl, Anne
dc.contributor.author Bauer, Uta-Maria
dc.contributor.author Nuber, Ulrike
dc.contributor.author Cardoso, Cristina
dc.contributor.author Zhang, Hui
dc.date.accessioned 2022-05-09T16:43:11Z
dc.date.available 2022-05-09T16:43:11Z
dc.date.created 2022
dc.date.issued 2022-05-09
dc.description Rett syndrome is a human intellectual disability disorder that is associated with mutations in the X-linked MECP2 gene. The epigenetic reader MeCP2 binds to methylated cytosines on the DNA and regulates chromatin organization. We have shown previously that MECP2 Rett syndrome missense mutations are impaired in chromatin binding and heterochromatin reorganization. Here, we performed a proteomics analysis of post-translational modifications of MeCP2 isolated from adult mouse brain. We show that MeCP2 carries various post-translational modifications, among them phosphorylation on S80 and S421, which lead to minor changes in either heterochromatin binding kinetics or clustering. We found that MeCP2 is (di)methylated on several arginines and that this modification alters heterochromatin organization. Interestingly, we identified the Rett syndrome mutation site R106 as a dimethylation site. In addition, co-expression of protein arginine methyltransferases 1 and 6 lead to a decrease of heterochromatin clustering. Altogether, we identified and validated novel modifications of MeCP2 in the brain and show that these can modulate its ability to bind as well as reorganize heterochromatin, which may play a role in the pathology of Rett syndrome. de_DE
dc.description.version Public access de_DE
dc.identifier.uri https://tudatalib.ulb.tu-darmstadt.de/handle/tudatalib/3455
dc.identifier.uri https://doi.org/10.48328/tudatalib-868
dc.language.iso en de_DE
dc.rights.licenseCC-BY-NC-4.0 (https://creativecommons.org/licenses/by-nc/4.0)
dc.subject Arginine (di)methylation de_DE
dc.subject Heterochromatin organization de_DE
dc.subject MeCP2 de_DE
dc.subject Protein arginine methyltransferases de_DE
dc.subject Rett syndrome de_DE
dc.subject.classification 2.11-03
dc.subject.ddc 570
dc.title MeCP2 heterochromatin organization is modulated by arginine methylation and serine phosphorylation de_DE
dc.type Software de_DE
dc.type Image de_DE
dcterms.accessRights openAccess
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person.identifier.orcid #PLACEHOLDER_PARENT_METADATA_VALUE#
person.identifier.orcid #PLACEHOLDER_PARENT_METADATA_VALUE#
person.identifier.orcid #PLACEHOLDER_PARENT_METADATA_VALUE#
person.identifier.orcid #PLACEHOLDER_PARENT_METADATA_VALUE#
person.identifier.orcid #PLACEHOLDER_PARENT_METADATA_VALUE#
person.identifier.orcid #PLACEHOLDER_PARENT_METADATA_VALUE#
person.identifier.orcid 0000-0002-7268-4136
person.identifier.orcid #PLACEHOLDER_PARENT_METADATA_VALUE#
person.identifier.orcid #PLACEHOLDER_PARENT_METADATA_VALUE#
tuda.history.classification Version=2020-2024;201-03 Zellbiologie
tuda.project DFG | CA198/10-1 | Interaktion zwischen
tuda.project DFG | CA198/16-1 | Rölle und Regulation
tuda.project DFG | NU119/3-1 | Interaktion zwischen
tuda.unit TUDa

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