Technologies and applications of high-throughput phosphoproteomics

SJ Humphrey1,2

  1. Charles Perkins Centre, The University of Sydney, NSW, Australia
  2. Max-Planck Institute of Biochemistry, Munich, Germany

Mass spectrometry-based proteomics has been used to study the dynamics of post-translational modifications for over a decade, and phosphoproteomics in particular has become a burgeoning field in its own right. Developments over the last few years have steadily increased the scope of phosphoproteomics studies in molecular biology, but major challenges remain, chief among these are practical limitations in scaling, performance and reproducibility, as well as large sample numbers due to complex workflows. However, these limitations are now falling away, with the development of robust and reproducible workflows aimed at simplifying phosphoproteomics experiments. The 'EasyPhos' method now allows acquiring large numbers of phosphoproteomes, enabling the analysis of dynamic and in vivo signaling (Humphrey et al., Nat. Biotech, 2015). These methods are currently being applied to diverse fields of biology ranging from embryonic stem cell differentiation to circadian rhythms. Combined with advances in instrumentation and bioinformatics analysis tools, such developments are making phosphoproteomics increasingly powerful, as I will discuss in this talk.