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AP-MS analysis of sirtuin-2 interactions and whole-cell proteome analysis in human fibroblasts

ABSTRACT: Sirtuins are NAD+-dependent deacylases with diverse enzymatic activities and substrates. They were implicated in regulation of cancer progression, neurodegeneration, aging, and viral infection. Sirtuin-2 localizes to the cytoplasm and is known to deacetylate alpha-tubulin. Current knowledge on sirtuin-2 interactions and its effect on gene expression in normal cells is very limited. We used proteomics approach to define its interactions and its effect on global protein levels in human fibroblasts.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Primary Cell, Fibroblast

SUBMITTER: Hanna Budayeva

LAB HEAD: Ileana M. Cristea

PROVIDER: PXD004212 | Pride | 2016-08-12

REPOSITORIES: Pride

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Human Sirtuin 2 Localization, Transient Interactions, and Impact on the Proteome Point to Its Role in Intracellular Trafficking.

Budayeva Hanna G HG Cristea Ileana M IM

Molecular & cellular proteomics : MCP 20160808 10

Human sirtuin 2 (SIRT2) is an NAD<sup>+</sup>-dependent deacetylase that primarily functions in the cytoplasm, where it can regulate α-tubulin acetylation levels. SIRT2 is linked to cancer progression, neurodegeneration, and infection with bacteria or viruses. However, the current knowledge about its interactions and the means through which it exerts its functions has remained limited. Here, we aimed to gain a better understanding of its cellular functions by characterizing SIRT2 subcellular loc ...[more]

PMID: 27503897

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