Proteomics

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Proteomics-based identification of SIRT2 interaction partners


ABSTRACT: 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.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hela Cell

SUBMITTER: Impens Francis  

LAB HEAD: Mélanie Hamon

PROVIDER: PXD011523 | Pride | 2020-02-20

REPOSITORIES: Pride

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Publications

Active nuclear import of the deacetylase Sirtuin-2 is controlled by its C-terminus and importins.

Eldridge Matthew J G MJG   Pereira Jorge M JM   Impens Francis F   Hamon Mélanie A MA  

Scientific reports 20200210 1


The NAD-dependent deacetylase Sirtuin-2 (SIRT2) functions in diverse cellular processes including the cell cycle, metabolism, and has important roles in tumorigenesis and bacterial infection. SIRT2 predominantly resides in the cytoplasm but can also function in the nucleus. Consequently, SIRT2 localisation and its interacting partners may greatly impact its function and need to be defined more clearly. In this study we used mass spectrometry to determine the interactomes of SIRT2 in whole cells  ...[more]

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