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Histone Modification02:32

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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DNMT1 modulates interneuron morphology by regulating Pak6 expression through crosstalk with histone modifications.

Judit Symmank1, Cathrin Bayer1, Christiane Schmidt1

  • 1a Institute of Human Genetics , University Hospital Jena , Jena , Germany.

Epigenetics
|June 19, 2018
PubMed
Summary

DNA methyltransferase 1 (DNMT1) regulates gene transcription via histone modifications, impacting cortical interneuron migration. DNMT1 interacts with EZH2 to control Pak6 expression, crucial for neuronal development.

Keywords:
DNMT1EZH2H3K27me3InterneuronsPAK6morphology

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Area of Science:

  • Neuroscience
  • Epigenetics
  • Molecular Biology

Background:

  • Epigenetic mechanisms like DNA methylation and histone modifications are vital for development and health.
  • Epigenetic networks regulate neuronal circuit formation, including GABA-positive interneurons in the cerebral cortex.
  • DNA methyltransferase 1 (DNMT1) is crucial for cortical interneuron migration, regulating Pak6 expression.

Purpose of the Study:

  • To investigate the non-DNA methylation roles of DNMT1 in gene transcription.
  • To elucidate the mechanism by which DNMT1 regulates Pak6 expression in developing interneurons.
  • To explore the interaction between DNMT1 and histone modification pathways in cortical development.

Main Methods:

  • Analysis of DNMT1's role in modulating H3K4 and H3K27 trimethylation.
  • Investigating DNMT1 interactions with the Polycomb-repressor complex 2 (PCR2) enzyme EZH2.
  • Using Dnmt1 depletion and EZH2 inhibition to assess Pak6 expression and interneuron morphology.
  • Employing siRNA to downregulate Pak6 expression and rescue morphological defects.

Main Results:

  • DNMT1 modulates gene transcription through H3K4 and H3K27 trimethylation in developing interneurons.
  • DNMT1 interacts with EZH2 to mediate H3K27 trimethylation at the Pak6 gene locus.
  • Inhibition of EZH2 increased Pak6 expression and interneuron morphological complexity.
  • Pak6 downregulation rescued the morphological defects caused by EZH2 inhibition or Dnmt1 depletion.

Conclusions:

  • DNMT1's epigenetic regulation extends beyond DNA methylation to include histone modifications.
  • DNMT1-PCR2-EZH2 interaction is critical for the transcriptional control of Pak6 in cortical interneurons.
  • This crosstalk is essential for proper interneuron migration and cortical circuit development.