CETSA in integrated proteomics studies of cellular processes

Abstract

The Cellular Thermal Shift Assay (CETSA) has recently emerged as a promising method to directly monitor functional modulations of protein interaction states in intact cells and tissue samples. Recent data support that the mass spectrometry-coupled proteome-wide implementation of CETSA (MS-CETSA) generates stringent information on a wide range of different interaction classes and is uniquely well suited to study the modulation of protein interaction states in cellular processes and during drug action. To expand the mechanistic insight of CETSA shifts, and to complement information from CETSA experiments, we outline how the integration of MS-CETSA with other proteomics techniques can provide a new platform for detailed, comprehensive, and interactive studies of the functional modulations of proteomes in situ.

Keywords: Cell states; Cellular thermal shift assay (CETSA); Drug response; Mass spectrometry; Protein interaction states (PRINTS); Proteomics.