Enhanced access to the human phosphoproteome with genetically encoded phosphothreonine

ABSTRACT: Protein phosphorylation is a ubiquitous post-translational modification used to regulate cellular processes and proteome architecture by modulating protein-protein interactions. The identification of phosphorylation events through proteomic surveillance has dramatically outpaced our capacity for functional assignment using traditional strategies, which often require knowledge of the upstream kinase a priori. The development of phospho-amino-acid-specific orthogonal translation systems, evolutionarily divergent aminoacyl-tRNA synthetase and tRNA pairs that enable co-translational insertion of a phospho-amino acids, has rapidly improved our ability to assess the physiological function of phosphorylation by providing kinase-independent methods of phosphoprotein production. Despite this utilit

SUBMITTER: Moen J 

PROVIDER: S-EPMC9700786 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature