Proteomic approaches to the characterization of protein thiol modification.
Protein cysteine residues are central to redox signaling and to protection against oxidative damage through their interactions with reactive oxygen and nitrogen species, and electrophiles. Although there is considerable evidence for a functional role for cysteine modifications, the identity and physiological significance of most protein thiol alterations are unknown. One way to identify candidate proteins involved in these processes is to utilize the proteomic methodologies that have been developed in recent years for the identification of proteins that undergo cysteine modification in response to redox signals or oxidative damage. These tools have proven effective in uncovering novel protein targets of redox modification and are important first steps that allow for a better understanding of how reactive molecules may contribute to signaling and damage. Here, we discuss a number of these approaches and their application to the identification of a variety of cysteine-centered redox modifications.
MRC Mitochondrial Biology Unit, Hills Road, Cambridge CB2 0XY, United Kingdom.
Edward T
ET
Chouchani
Andrew M
AM
James
Ian M
IM
Fearnley
Kathryn S
KS
Lilley
Michael P
MP
Murphy
D003545:Cysteine / Q000378:metabolism; D006801:Humans; D010084:Oxidation-Reduction; D011506:Proteins / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D040901:Proteomics / Q000379:methods*; D013438:Sulfhydryl Compounds / Q000737:chemistry / Q000378:metabolism*
D011506:Proteins; D013438:Sulfhydryl Compounds; D003545:Cysteine