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Structure, Activity, and Function of Protein Methyltransferases

Structure, Activity, and Function of Protein Methyltransferases

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This collection of review articles describes the structure, function and mechanism of individual protein methyltransferase enzymes including protein lysine methyltransferases, protein arginine methyltransferases, and also the less abundant protein histidine methyltransferases and protein N-terminal end methyltransferases. The topics covered in the individual reviews include structural aspects (domain architecture, homologs and paralogs, and structure), biochemical properties (mechanism, sequence specificity, product specificity, regulation, and histone and non-histone substrates), cellular features (subcellular localization, expression patterns, cellular roles and function, biological effects of substrate protein methylation, connection to cell signaling pathways, and connection to chromatin regulation) and their role in diseases. This review book is a useful resource for scientists working on protein methylation and protein methyltransferases and those interested in joining this emerging research field.

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Keywords

  • Actin
  • actin cytoskeleton
  • AML
  • arginine methylation
  • Biochemistry
  • Biology, Life Sciences
  • Cancer
  • Cardiovascular Disease
  • cell proliferation
  • Cell signaling
  • chromatin regulation
  • Congenital Heart Diseases
  • Cytoskeleton
  • dendritic spine
  • diabetes
  • Disease
  • DNA damage repair
  • Dystonia
  • eEF1A
  • EHMT1
  • EHMT2
  • enteroviruses
  • enzyme regulation
  • enzyme specificity
  • epigenetics
  • G9a
  • GLP
  • GTPase
  • H3K36
  • H3K36me2
  • H3K4me3
  • H3K9 methylation
  • H3R2me2a
  • H4R3 methylation
  • heterochromatin
  • histone
  • Hsmar1
  • Huntington’s disease
  • Immunity
  • Inflammation
  • inflammatory bowel disease
  • lysine methylation
  • lysine-specific methyltransferase (PKMT)
  • Mathematics & science
  • methyltransferase
  • Metnase
  • METTL13
  • MLL2
  • N-terminal methylation
  • n/a
  • Neurodegenerative Diseases
  • Neuron
  • NHEJ
  • non-homologous end joining repair
  • NSD1
  • NSD3
  • NUP98-NSD1
  • Oncogenesis
  • PKMT
  • Pluripotency
  • Polymerization
  • post translational modification
  • Post-translational modification
  • post-translational protein modification
  • posttranslational modifications
  • Prader–Willi syndrome
  • PRMT1
  • PRMT2
  • PRMT5
  • PRMT6
  • PRMT7
  • protein arginine methylation
  • protein histidine methylation
  • protein lysine methylation
  • protein post-translational modification
  • Reference, information & interdisciplinary subjects
  • Research & information: general
  • Rett Syndrome
  • Schizophrenia
  • SET7/9
  • SETD3
  • SETD7
  • SETDB1
  • SETMAR
  • SH3
  • SOTOS
  • stress response
  • Structure
  • structure and function
  • synapse
  • transcriptional regulation
  • Translation
  • transposable elements
  • transposase
  • WHSC1L1

Links

DOI: 10.3390/books978-3-0365-4140-2

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