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

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.

沉默信息调节蛋白家族（Sirtuins）是一类依赖烟酰胺腺嘌呤二核苷酸（NAD+）的去酰基化酶，具备多样的酶促活性与底物。该家族成员被证实参与调控肿瘤进展、神经退行性病变、衰老进程以及病毒感染过程。其中，沉默信息调节蛋白2（Sirtuin-2）定位于细胞质，且已知可对α-微管蛋白（alpha-tubulin）进行去乙酰化修饰。目前学界关于Sirtuin-2的相互作用蛋白，以及其在正常细胞中对基因表达的调控效应的认知仍十分有限。本研究采用蛋白质组学（proteomics）方法，明确了Sirtuin-2的相互作用蛋白谱，并解析了其对人成纤维细胞（human fibroblasts）中全局蛋白质水平的影响。