Proteomics-based identification of SIRT2 interaction partners

The NAD+ dependent deacetylase enzyme SIRT2 functions in diverse cellular processes including the cell cycle, metabolism and has recently been demonstrated to have important roles during tumorigenesis and bacterial infection. Though predominantly localised in the cytoplasm SIRT2 has been shown to continuously cycle in and out of the nucleus where it functions as a histone deacetylase. To investigate the varied and pleiotropic nature of SIRT2 we performed proteomic analyses using liquid chromatography-tandem mass spectrometry to identify novel interacting partners. Using this approach, we have generated a whole cell interactome consisting of over 500 proteins highlighting the distinct cellular processes in which SIRT2 functions.