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Emerging chromatin structural roles of the methyl-CpG binding protein MeCP2.

“ Irrespective of the precise underlying mechanisms, the novel studies clearly establish a role for MeCP2 in the architecture and compaction of heterochromatin, and reveal likely cooperation with HP1 proteins and major-satellite RNAs. ” DNA methylation is an essential epigenetic modiﬁcation, present in mammals predominantly at cytosine residues that are followed by guanines. In somatic cells, this so-called CpG methylation is found at high levels all along the genome. Different readers have evolved that bind to the methylated DNA and inﬂuence chromatin and gene expression. Methyl-CpG binding domain (MBD) proteins constitute the largest family of such proteins, and share a conserved MBD [1] . Extensive research has shown that their binding patterns evolved to facilitate appropriate gene expression levels in the context of highly methylated genomes [2] . Exciting recent studies on the best-studied MBD protein, MeCP2, evoke a new role besides transcriptional repression. They show that MeCP2 contributes to the 3D structuration and compaction of heterochromatin as well [3–6] . Below, we present these newly emerging insights and discuss their possible relevance for neurological disorders in humans that are caused by genetic mutations in the MeCP2 gene. The MeCP2 gene is positioned on the X chromosome and is mutated in almost all patients with Rett syndrome (RTT, OMIM 312750), a progressive and devastating autism-spectrum