Protein Post-Translational Modifications in the Nervous System: from Development to Disease and Ageing

Protein Post-Translational Modifications in the Nervous System: from Development to Disease and Ageing

  • Beatriz Alvarez
  • Judit Symmank
  • Miguel Diaz-Hernandez
  • Geraldine Zimmer-Bensch
  • Patricia Franzka
Publisher:Frontiers Media SAISBN 13: 9782832556191ISBN 10: 2832556191

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Protein Post-Translational Modifications in the Nervous System: from Development to Disease and Ageing is written by Beatriz Alvarez and published by Frontiers Media SA. It's available with International Standard Book Number or ISBN identification 2832556191 (ISBN 10) and 9782832556191 (ISBN 13).

Post-translational modifications (PTMs) increase the functional diversity of the proteome by reversibly or irreversibly modifying proteins during or after their synthesis. Thereby, they contribute to the structural and functional variety of proteins, conveying a complexity to the proteome that is significantly higher than the coding capacity of the genome. Moreover, providing another level of epigenetic regulation, PTMs of histone proteins in particular contribute to the modulation of gene accessibility and specific cell expression profiles. PTMs include enzymatically controlled modifications such as phosphorylation, glycosylation, acetylation, methylation, ubiquitination, or proteolysis as well as non-enzymatic reactions such as nitrosation, oxidation, or glycation. They can occur at the same amino acid sites, interfering with each other in hierarchical orders and thereby adding another level of complexity. In this way, PTMs influence protein function, turnover, secretion, localization, and interactions with other cellular molecules such as proteins, nucleic acids, lipids, and cofactors. Thus, they influence almost all aspects of cell biology and pathogenesis as well as represent a basis for maintaining cellular homeostasis. In this regard, PTMs regulate several processes during neurodevelopment involving genes important for brain formation, the cytoskeleton and cytoskeleton-associating proteins as well as regulation of cell migration and axonal guidance.