Year: 2013
Type: editorial
Abstract: The Next Frontier of Post-Translational Modifications T he human genome encodes approximately 20,000 protein-encoding genes. 1 This complexity is increased by several orders of magnitude by including the number of splice variants and diverse posttranslational modifications (PTMs), which likely lead to millions of different functional members of the human proteome.Hundreds of unique PTMs have been described, although some are more thoroughly understood due to the availability of tools and reagents.The most commonly studied PTMs include phosphorylation, ubiquitylation, glycosylation, acetylation, lipidation, oxidation, and proteolysis.These distinct modifications function to rapidly switch proteins to different active or inactive conformations, change polarity or hydrophobicity to affect localization, recruit new interaction partners, or target degradation.Most PTMs occur at polar and charged amino acids, including serine, threonine, asparagine, cysteine, lysine, and arginine.Even after decades of studying phosphorlyation, our knowledge of the dynamics and diversity of PTM continues to expand with the development of new analytical methods and tools.PTMs are clearly required for the activation, inhibition, and degradation of nearly all proteins.Undoubtedly, the complexity of post-translational regulation makes the task of translating genomic information to the biological function of proteins daunting.In this issue, six reviews are presented that outline progress in understanding the diversity and regulation of distinct posttranslational events.Metabolic labeling with radioactive phosphate, acetate, sugars, and lipids provided the first evidence of the breadth of unique modifications in the proteome.Later, PTM-specific antibodies greatly enhanced the ability to rapidly analyze specific modifications, especially those that are sufficiently antigenic.Recent advances in mass spectrometry have provided the first proteome-wide view many PTMs.These experiments are massively more sensitive after selective enrichment, which reduces abundant unmodified peptides.Such studies have identified tens of thousands of phosphorylation sites. 2 Such studies
Source: Biopolymers
DOI: 10.1002/bip.22370
Author: Brent R. Martin
Institution: University of Michigan
Language: English
Subfield: Spectroscopy
Field: Chemistry
Domain: Physical Sciences
Open Access status: bronze
Funder: National Cancer Institute
OpenAlex ID: W1553632130