Orphan PTMs: Rare, yet functionally important modifications of cysteine.

Abstract:

:The enhanced nucleophilicity and redox sensitivity of the thiol group renders cysteine residues susceptible to numerous electrophilic and oxidative post-translational modifications to form disulfides, sulfenic acids, nitrosothiols, and lipid-modified species. Outside of these well-characterized modifications of cysteine, there are reports of cysteine modification through phosphorylation, methylation, and ubiquitination. Although these post-translational modifications are highly abundant on other amino acids, they play a less pervasive role in cysteine biology. Despite the rarity of these modifications of cysteine, they have been shown to play critical roles in catalysis and regulation. Here we describe these rare post-translational modifications of cysteine in detail, by describing their discovery and functional characterization on diverse proteins. Furthermore, we highlight potential proteomic tools that may aid in globally identifying these modifications to fully elucidate their abundance in biological systems.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Shannon DA,Weerapana E

doi

10.1002/bip.22252

subject

Has Abstract

pub_date

2014-02-01 00:00:00

pages

156-64

issue

2

eissn

0006-3525

issn

1097-0282

journal_volume

101

pub_type

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