The biological functions of the methyl-CpG-binding protein MeCP2 and its implication in Rett syndrome

2001 ◽  
Vol 23 ◽  
pp. S32-S37 ◽  
Author(s):  
Xinsheng Nan ◽  
Adrian Bird
Keyword(s):  
Rett Syndrome ◽  
Binding Protein ◽  
Biological Functions ◽  
Protein Mecp2

The methyl-CpG-binding protein MeCP2 and neurological disease

2008 ◽  
Vol 36 (4) ◽  
pp. 575-583 ◽  
Author(s):  
Adrian Bird
Keyword(s):  
Dna Methylation ◽  
Rett Syndrome ◽  
Dna Sequences ◽  
Neurological Disease ◽  
Binding Protein ◽  
Autism Spectrum ◽  
Model Systems ◽  
Mecp2 Gene ◽  
Methylated Dna ◽  
Protein Mecp2

The methyl-CpG-binding protein MeCP2 was discovered over 15 years ago as part of a search for proteins that selectively bind methylated DNA. It is a nuclear protein that is largely chromatin-bound and has a strong preference for binding to methylated DNA sequences in vivo. Evidence from model systems shows that MeCP2 can recruit the Sin3a co-repressor complex to promoters leading to transcriptional repression, therefore suggesting that MeCP2 can interpret the DNA methylation signal to bring about gene silencing. Mutations in the human MECP2 gene cause the autism spectrum disorder Rett Syndrome. MeCP2 is most highly expressed in neurons, and mice lacking this protein show symptoms that strikingly parallel those of Rett patients. Surprisingly, these symptoms are efficiently reversed by delayed activation of a ‘stopped’ Mecp2 gene, raising hopes that human Rett syndrome may also be reversible. Future studies of MeCP2 promise to shed light upon brain function, neurological disease and the biology of DNA methylation.

MeCP2 is a microsatellite binding protein that protects CA repeats from nucleosome invasion

Science ◽  
2021 ◽  
Vol 372 (6549) ◽  
pp. eabd5581 ◽  
Author(s):  
Abdulkhaleg Ibrahim ◽  
Christophe Papin ◽  
Kareem Mohideen-Abdul ◽  
Stéphanie Le Gras ◽  
Isabelle Stoll ◽  
...  
Keyword(s):  
Rett Syndrome ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Ca Repeat ◽  
Transcriptional Dysregulation ◽  
Genome Wide ◽  
Exact Function ◽  
Dna Shape ◽  
Syndrome Protein ◽  
Protein Mecp2

The Rett syndrome protein MeCP2 was described as a methyl-CpG-binding protein, but its exact function remains unknown. Here we show that mouse MeCP2 is a microsatellite binding protein that specifically recognizes hydroxymethylated CA repeats. Depletion of MeCP2 alters chromatin organization of CA repeats and lamina-associated domains and results in nucleosome accumulation on CA repeats and genome-wide transcriptional dysregulation. The structure of MeCP2 in complex with a hydroxymethylated CA repeat reveals a characteristic DNA shape, with considerably modified geometry at the 5-hydroxymethylcytosine, which is recognized specifically by Arg133, a key residue whose mutation causes Rett syndrome. Our work identifies MeCP2 as a microsatellite DNA binding protein that targets the 5hmC-modified CA-rich strand and maintains genome regions nucleosome-free, suggesting a role for MeCP2 dysfunction in Rett syndrome.

Dysfunction of the Methyl-CpG-Binding Protein MeCP2 in Rett Syndrome

2012 ◽  
pp. 43-69 ◽  
Author(s):  
Gaston Calfa ◽  
Alan K. Percy ◽  
Lucas Pozzo-Miller
Keyword(s):  
Rett Syndrome ◽  
Binding Protein ◽  
Protein Mecp2

Methyl-CpG-binding protein 2 (MECP2) mutation type is associated with bone disease severity in Rett syndrome

2019 ◽  
Author(s):  
Carla Caffarelli ◽  
Tomai Pitinca Maria Dea ◽  
Valentina Francolini ◽  
Roberto Canitano ◽  
felice Claudio De ◽  
...  
Keyword(s):  
Disease Severity ◽  
Rett Syndrome ◽  
Bone Disease ◽  
Binding Protein ◽  
Mecp2 Mutation ◽  
Mutation Type

scholarly journals Methyl-CpG-binding protein 2(MECP2) mutation type is associated with disease severity in Rett syndrome

2014 ◽  
Vol 51 (3) ◽  
pp. 152-158 ◽  
Author(s):  
Vishnu Anand Cuddapah ◽  
Rajesh B Pillai ◽  
Kiran V Shekar ◽  
Jane B Lane ◽  
Kathleen J Motil ◽  
...  
Keyword(s):  
Disease Severity ◽  
Rett Syndrome ◽  
Binding Protein ◽  
Mecp2 Mutation ◽  
Mutation Type

Vitamin D-binding protein: multifunctional component of blood serum

2021 ◽  
Vol 76 (1) ◽  
pp. 103-110
Author(s):  
Alexandra A. Povaliaeva ◽  
Ekaterina A. Pigarova ◽  
Anastasia A. Romanova ◽  
Larisa K. Dzeranova ◽  
Artem Y. Zhukov ◽  
...  
Keyword(s):  
Vitamin D ◽  
Binding Sites ◽  
Binding Protein ◽  
Vitamin D Metabolites ◽  
Biological Functions ◽  
Vitamin D Binding Protein ◽  
Fatty Acid Binding ◽  
Physiological Properties ◽  
Steroid Binding ◽  
Tumor Pathogenesis

Vitamin D-binding protein (DBP) was discovered more than half a century ago as a polymorphic serum protein and is currently characterized by a variety of physiological properties. First of all, DBP carries the bulk of vitamin D metabolites circulating in the bloodstream, while albumin is the second most important transport protein, especially in patients with a low concentration of DBP in serum. Since it was discovered that only 12% of the total circulating DBP have occupied steroid binding sites, a vigorous study of other potential biological roles of DBP was initiated: actin utilization, regulation of inflammation and innate immunity mechanisms, fatty acid binding, effects on bone metabolism and participation in the tumor pathogenesis. This review focuses on the main known biological functions of DBP.

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