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Unveiling the human nitroproteome: Protein tyrosine nitration in cell signaling and cancer

Irene Griswold-Prenner1, Arun K Kashyap1, Sahar Mazhar1

  • 1Nitrase Therapeutics, Brisbane, California, USA.

The Journal of Biological Chemistry
|July 13, 2023
PubMed

Insights

Covalent modification of tyrosine residues, including nitration, impacts biological processes. This study details human nitrated proteins and reveals tyrosine nitration

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Covalent amino acid modification expands protein function.
  • Tyrosine residues undergo various posttranslational modifications (PTMs), including phosphorylation, sulfation, and nitration.
  • Aberrant tyrosine nitration is linked to human diseases.

Purpose of the Study:

  • To create an updated database of 908 human nitrated proteins.
  • To analyze the role of tyrosine nitration in cancer biology.
  • To investigate the interplay between tyrosine nitration and phosphorylation in cell signaling.

Main Methods:

  • Database curation of human nitrated proteins.
  • Bioinformatic analysis of protein modification sites.
  • Literature review and data synthesis.

Main Results:

  • A database of 908 human nitrated proteins was established.
  • Tyrosine nitration's role in cancer biology was analyzed.
  • 879 of 1971 tyrosine nitration sites are also phosphorylated, suggesting a significant role in cell signaling.

Conclusions:

  • Tyrosine nitration is a critical PTM with implications for human health and disease.
  • The extensive overlap between tyrosine nitration and phosphorylation sites highlights their interconnected roles in cell signaling.
  • Further research into tyrosine nitration in cancer biology is warranted.
Keywords:
3-nitrotyrosinecancer biologycell signalingposttranslational modificationstyrosine nitration

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