Protein methylation and demethylation are post-translational modifications that involve the addition or removal of a methyl group to specific amino acid residues in proteins. Methylation can occur on various amino acids, including lysine, arginine, histidine, and glutamate, among others. This modification is catalyzed by protein methyltransferases, which transfer a methyl group from the methyl donor, S-adenosylmethionine (SAM), to the target amino acid. The addition of a methyl group to a protein can have diverse functional consequences. It can regulate protein-protein interactions, enzymatic activity, subcellular localization, and stability, thereby modulating cellular processes such as signal transduction, gene expression, DNA repair, and protein turnover. On the other hand, protein demethylation is carried out by enzymes known as protein demethylases. These demethylases remove the methyl group from the methylated amino acid residue, thereby reversing the methylation modification. Demethylation processes can be accomplished through various mechanisms, depending on the specific amino acid being targeted and the demethylase involved. Protein methylation and demethylation play critical roles in numerous biological processes, including development, differentiation, epigenetic regulation, and disease. For example, histone methylation, as discussed earlier, is a well-known protein methylation event that orchestrates chromatin structure and gene expression. Similarly, methylation of non-histone proteins, such as transcription factors and signaling molecules, also contributes to their functional regulation. Overall, protein methylation and demethylation are dynamic and tightly regulated processes that govern protein function and cellular homeostasis. Understanding the mechanisms underlying these modifications is crucial for unraveling their roles in normal physiology and disease pathology and may offer potential therapeutic opportunities in the future.
This special issue aims to provide a comprehensive overview of recent advancements in the field of protein methylation/demethylation, with a focus on its role in disease and homeostasis. We welcome original research articles, reviews, and perspectives that cover a broad range of topics related to epigenetic modifications, including but not limited to:
(1) Molecular mechanisms of histone methylation and demethylation in disease and homeostasis.
(2) The role of histone methylation in gene regulation and chromatin remodeling.
(3) Advances in the development of small molecule inhibitors targeting protein methyltransferases and demethylases for disease therapy.
(4) Histone methylation in cancer initiation, progression, and therapy.
(5) The impact of environmental factors on protein methylation/demethylation.
(6) Identification of novel protein interaction networks affecting methyltransferase or demethylase activity."
Protein methylation and demethylation are post-translational modifications that involve the addition or removal of a methyl group to specific amino acid residues in proteins. Methylation can occur on various amino acids, including lysine, arginine, histidine, and glutamate, among others. This modification is catalyzed by protein methyltransferases, which transfer a methyl group from the methyl donor, S-adenosylmethionine (SAM), to the target amino acid. The addition of a methyl group to a protein can have diverse functional consequences. It can regulate protein-protein interactions, enzymatic activity, subcellular localization, and stability, thereby modulating cellular processes such as signal transduction, gene expression, DNA repair, and protein turnover. On the other hand, protein demethylation is carried out by enzymes known as protein demethylases. These demethylases remove the methyl group from the methylated amino acid residue, thereby reversing the methylation modification. Demethylation processes can be accomplished through various mechanisms, depending on the specific amino acid being targeted and the demethylase involved. Protein methylation and demethylation play critical roles in numerous biological processes, including development, differentiation, epigenetic regulation, and disease. For example, histone methylation, as discussed earlier, is a well-known protein methylation event that orchestrates chromatin structure and gene expression. Similarly, methylation of non-histone proteins, such as transcription factors and signaling molecules, also contributes to their functional regulation. Overall, protein methylation and demethylation are dynamic and tightly regulated processes that govern protein function and cellular homeostasis. Understanding the mechanisms underlying these modifications is crucial for unraveling their roles in normal physiology and disease pathology and may offer potential therapeutic opportunities in the future.
This special issue aims to provide a comprehensive overview of recent advancements in the field of protein methylation/demethylation, with a focus on its role in disease and homeostasis. We welcome original research articles, reviews, and perspectives that cover a broad range of topics related to epigenetic modifications, including but not limited to:
(1) Molecular mechanisms of histone methylation and demethylation in disease and homeostasis.
(2) The role of histone methylation in gene regulation and chromatin remodeling.
(3) Advances in the development of small molecule inhibitors targeting protein methyltransferases and demethylases for disease therapy.
(4) Histone methylation in cancer initiation, progression, and therapy.
(5) The impact of environmental factors on protein methylation/demethylation.
(6) Identification of novel protein interaction networks affecting methyltransferase or demethylase activity."