Strong anion exchange-mediated phosphoproteomics reveals extensive human non-canonical phosphorylation.

ABSTRACT: Phosphorylation is a key regulator of protein function under (patho)physiological conditions, and defining site-specific phosphorylation is essential to understand basic and disease biology. In vertebrates, the investigative focus has primarily been on serine, threonine and tyrosine phosphorylation, but mounting evidence suggests that phosphorylation of other "non-canonical" amino acids also regulates critical aspects of cell biology. However, standard methods of phosphoprotein characterisation are largely unsuitable for the analysis of non-canonical phosphorylation due to their relative instability under acidic conditions and/or elevated temperature. Consequently, the complete landscape of phosphorylation remains unexplored. Here, we report an unbiased phosphopeptide enrichment strategy b

SUBMITTER: Hardman G 

PROVIDER: S-EPMC6826212 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature