Abstract
Posttranslational modification of proteins plays a fundamental role in cell biology. It provides cells a means to regulate the signaling, enzymatic or structural properties of proteins without continuous cycles of synthesis and degradation, offering multiple distinct functions to individual proteins in a rapid and reversible manner. Modifications can include phosphorylation, ubiquitination or methylation, which are widespread and simple to detect using current approaches. More challenging to identify, one modification of growing significance is the direct oxidation of cysteine and methionine side chains. Protein oxidation has long been known to occur spontaneously upon the accumulation of cellular reactive oxygen species (ROS), but new data are providing insight into the targeted oxidation of proteins by flavin-containing monooxygenases (FMOs). Here, we review how oxidation of cellular proteins can modulate their activity and consider potential roles for FMOs in the targeted modification of proteins shaping cell division, with a particular focus on two families of FMOs: MICAL and OSGIN.