{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T20:28:27Z","timestamp":1790713707371,"version":"4.1.0"},"reference-count":152,"publisher":"Oxford University Press (OUP)","issue":"1","license":[{"start":{"date-parts":[[2023,9,11]],"date-time":"2023-09-11T00:00:00Z","timestamp":1694390400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"funder":[{"DOI":"10.13039\/501100004381","name":"University of Western Ontario","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004381","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Center for Addition and Mental Health Foundation Discovery Fund"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2023,12,12]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>MeCP2 (Methyl CpG binding protein 2) is an intrinsically disordered protein that binds to methylated genome regions. The protein is a critical transcriptional regulator of the brain, and its mutations account for 95% of Rett syndrome (RTT) cases. Early studies of this neurodevelopmental disorder revealed a close connection with dysregulations of the ubiquitin system (UbS), notably as related to UBE3A, a ubiquitin ligase involved in the proteasome-mediated degradation of proteins. MeCP2 undergoes numerous post-translational modifications (PTMs), including ubiquitination and sumoylation, which, in addition to the potential functional outcomes of their monomeric forms in gene regulation and synaptic plasticity, in their polymeric organization, these modifications play a critical role in proteasomal degradation. UbS-mediated proteasomal degradation is crucial in maintaining MeCP2 homeostasis for proper function and is involved in decreasing MeCP2 in some RTT-causing mutations. However, regardless of all these connections to UbS, the molecular details involved in the signaling of MeCP2 for its targeting by the ubiquitin-proteasome system (UPS) and the functional roles of monomeric MeCP2 ubiquitination and sumoylation remain largely unexplored and are the focus of this review.<\/jats:p>","DOI":"10.1093\/hmg\/ddad150","type":"journal-article","created":{"date-parts":[[2023,9,11]],"date-time":"2023-09-11T11:28:34Z","timestamp":1694431714000},"page":"1-11","source":"Crossref","is-referenced-by-count":15,"title":["MeCP2 ubiquitination and sumoylation, in search of a function"],"prefix":"10.1093","volume":"33","author":[{"given":"Ladan","family":"Kalani","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Microbiology, University of Victoria , 3800 Finnerty Rd, Victoria, BC V8W 2Y2 , Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bo-Hyun","family":"Kim","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Microbiology, University of Victoria , 3800 Finnerty Rd, Victoria, BC V8W 2Y2 , Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John B","family":"Vincent","sequence":"additional","affiliation":[{"name":"Molecular Neuropsychiatry & Development (MiND) Lab, Campbell Family Mental Health Research Institute, Centre for Addiction and Mental Health , 250 College St, Toronto, ON M5T 1R8 , Canada"},{"name":"Institute of Medical Science, University of Toronto , 27 King\u2019s College Cir, Toronto, ON M5S 1A8 , Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juan","family":"Ausi\u00f3","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Microbiology, University of Victoria , 3800 Finnerty Rd, Victoria, BC V8W 2Y2 , Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2023,9,11]]},"reference":[{"key":"2023121917044416900_ref1","volume-title":"Chromatin","author":"Holde","year":"1988"},{"key":"2023121917044416900_ref2","doi-asserted-by":"crossref","first-page":"4059","DOI":"10.1182\/blood.V93.12.4059","article-title":"DNA methylation","volume":"93","author":"Singal","year":"1999","journal-title":"Blood"},{"key":"2023121917044416900_ref3","doi-asserted-by":"crossref","first-page":"786","DOI":"10.1073\/pnas.51.5.786","article-title":"Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis","volume":"51","author":"Allfrey","year":"1964","journal-title":"Proc Natl Acad Sci"},{"key":"2023121917044416900_ref4","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1016\/j.cell.2007.02.006","article-title":"Epigenetics: a landscape takes 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