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post-translational proteic modifications

Sunday 30 November 2003

Post-translational modifications define the functional and structural plasticity of proteins in archaea, prokaryotes and eukaryotes.

Multi-site protein modification modulates protein activity and macromolecular interactions and is involved in a range of fundamental molecular processes.

Types

- proteic glycosylation

  • O-linked N-acetylglucosamine (GlcNAc) glycosylation

- proteic methylation
- proteic acetylation
- proteic nitration
- proteic ubiquitylation
- proteic farnesylation
- proteic palmitoylation
- proteic phosphorylation (PO4)
- proteic transglutamination
- proteic prenylation
- proteic carboxyl methylation by methyltransferase
- endoproteolytic processing by protease

References

- Jensen ON. Interpreting the protein language using proteomics. Nat Rev Mol Cell Biol. 2006 Jun;7(6):391-403. PMID: 16723975

- Seet BT, Dikic I, Zhou MM, Pawson T. Reading protein modifications with interaction domains. Nat Rev Mol Cell Biol. 2006 Jul;7(7):473-83. PMID: 16829979

- Drenth JP, Martina JA, van de Kerkhof R, Bonifacino JS, Jansen JB. Polycystic liver disease is a disorder of cotranslational protein processing. Trends Mol Med. 2005 Jan;11(1):37-42. PMID: 15649821

- Rehfeld JF, Goetze JP. The posttranslational phase of gene expression: new possibilities in molecular diagnosis. Curr Mol Med. 2003 Feb;3(1):25-38. PMID: 12558072