Amino Acids

, Volume 43, Issue 2, pp 505–517

Modulating protein activity and cellular function by methionine residue oxidation

Review Article

DOI: 10.1007/s00726-011-1175-9

Cite this article as:
Cui, Z.J., Han, Z.Q. & Li, Z.Y. Amino Acids (2012) 43: 505. doi:10.1007/s00726-011-1175-9

Abstract

The sulfur-containing amino acid residue methionine (Met) in a peptide/protein is readily oxidized to methionine sulfoxide [Met(O)] by reactive oxygen species both in vitro and in vivo. Methionine residue oxidation by oxidants is found in an accumulating number of important proteins. Met sulfoxidation activates calcium/calmodulin-dependent protein kinase II and the large conductance calcium-activated potassium channels, delays inactivation of the Shaker potassium channel ShC/B and L-type voltage-dependent calcium channels. Sulfoxidation at critical Met residues inhibits fibrillation of atherosclerosis-related apolipoproteins and multiple neurodegenerative disease-related proteins, such as amyloid beta, α-synuclein, prion, and others. Methionine residue oxidation is also correlated with marked changes in cellular activities. Controlled key methionine residue oxidation may be used as an oxi-genetics tool to dissect specific protein function in situ.

Keywords

Protein methionine oxidation Methionine sulfoxide Calcium/calmodulin-dependent protein kinase II BK potassium channel Protein fibrillation Neurodegenerative diseases Singlet oxygen 

Copyright information

© Springer-Verlag 2011

Authors and Affiliations

  1. 1.Institute of Cell BiologyBeijing Normal UniversityBeijingChina

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