Now at the Met: fine art of reversible sulfoxidation

Tal Ilani; Deborah Fass

doi:10.1016/j.molcel.2013.07.021

Now at the Met: fine art of reversible sulfoxidation

Mol Cell. 2013 Aug 8;51(3):281-2. doi: 10.1016/j.molcel.2013.07.021.

Authors

Tal Ilani¹, Deborah Fass

Affiliation

¹ Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel. Electronic address: tal.ilani@weizmann.ac.il.

PMID: 23932712
DOI: 10.1016/j.molcel.2013.07.021

Abstract

In this issue, Lee et al. (2013) exhibit methionine sulfoxidation in a new light. By bringing together two antagonistic enzymes affecting methionine redox state, the authors demonstrate that methionine oxidation constitutes a reversible, posttranslational regulatory mechanism, akin to protein phosphorylation.

Publication types

Comment

MeSH terms

Actins / metabolism*
Animals
Macrophages / metabolism*
Methionine / metabolism*
Methionine Sulfoxide Reductases / genetics*
Microfilament Proteins
Microtubule-Associated Proteins / metabolism*
Mixed Function Oxygenases / metabolism*
Oxidoreductases / metabolism*

Substances

Actins
Microfilament Proteins
Microtubule-Associated Proteins
Methionine
Mical1 protein, mouse
Mixed Function Oxygenases
Oxidoreductases
Methionine Sulfoxide Reductases
Msrb2 protein, mouse