Thermal Proteome Profiling Reveals the O-GlcNAc-Dependent Meltome.

ABSTRACT: Posttranslational modifications alter the biophysical properties of proteins and thereby influence cellular physiology. One emerging manner by which such modifications regulate protein functions is through their ability to perturb protein stability. Despite the increasing interest in this phenomenon, there are few methods that enable global interrogation of the biophysical effects of posttranslational modifications on the proteome. Here, we describe an unbiased proteome-wide approach to explore the influence of protein modifications on the thermodynamic stability of thousands of proteins in parallel. We apply this profiling strategy to study the effects of O-linked N-acetylglucosamine (O-GlcNAc), an abundant modification found on hundreds of proteins in mammals that has been shown i

SUBMITTER: King DT 

PROVIDER: S-EPMC8969899 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature