Introduction to the multi-author review on methylation in cellular physiology

Research output: Contribution to journalReview article

Abstract

Protein post-translational modifications (PTMs) have long been a topic of intensive investigation. Covalent additions to the 20 genetically encoded amino acids can alter protein interactions and can even change enzymatic function. In eukarya, PTMs can amplify both the complexity and functional paradigms of the cellular environment. Therefore, PTMs have been of substantial research interest, both for understanding fundamental mechanisms and to provide insight into drug design. Indeed, targeting proteins involved in writing, reading, and erasing PTMs important for human pathologies are some of the most fruitful avenues of drug discovery. In this multi-author review, we explore exciting new work on lysine and arginine methylation, molecular and structural understanding of some of the lysine and arginine methyltransferases (KMTs and PRMTs, respectively), novel insights into nucleic acid methylation, and how the enzymes responsible for writing these PTMs and readers responsible for recognizing these PTMs could be drugged. Here, we introduce the background and the topics covered in this issue.

Original languageEnglish (US)
JournalCellular and Molecular Life Sciences
DOIs
StatePublished - Jan 1 2019

Fingerprint

Post Translational Protein Processing
Methylation
Lysine
Drug Design
Protein Transport
Drug Discovery
Eukaryota
Nucleic Acids
Arginine
Reading
Pathology
Amino Acids
Enzymes
Research
Proteins

Keywords

  • Arginine methyltransferase
  • Histone
  • Lysine methyltransferase
  • Methylarginine
  • Methyllysine
  • MLL
  • N(6)-methyladenine
  • Post-translational modification
  • PRMT

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Cellular and Molecular Neuroscience
  • Cell Biology

Cite this

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title = "Introduction to the multi-author review on methylation in cellular physiology",
abstract = "Protein post-translational modifications (PTMs) have long been a topic of intensive investigation. Covalent additions to the 20 genetically encoded amino acids can alter protein interactions and can even change enzymatic function. In eukarya, PTMs can amplify both the complexity and functional paradigms of the cellular environment. Therefore, PTMs have been of substantial research interest, both for understanding fundamental mechanisms and to provide insight into drug design. Indeed, targeting proteins involved in writing, reading, and erasing PTMs important for human pathologies are some of the most fruitful avenues of drug discovery. In this multi-author review, we explore exciting new work on lysine and arginine methylation, molecular and structural understanding of some of the lysine and arginine methyltransferases (KMTs and PRMTs, respectively), novel insights into nucleic acid methylation, and how the enzymes responsible for writing these PTMs and readers responsible for recognizing these PTMs could be drugged. Here, we introduce the background and the topics covered in this issue.",
keywords = "Arginine methyltransferase, Histone, Lysine methyltransferase, Methylarginine, Methyllysine, MLL, N(6)-methyladenine, Post-translational modification, PRMT",
author = "David Shechter",
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KW - Arginine methyltransferase

KW - Histone

KW - Lysine methyltransferase

KW - Methylarginine

KW - Methyllysine

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KW - N(6)-methyladenine

KW - Post-translational modification

KW - PRMT

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