TP53 and autoimmune disease: SIRT1 deacetylates and thus inactivates the p53 protein. SIRT1 also stimulates autophagy by preventing the acetylation of proteins (via deacetylation) required for autophagy, as demonstrated in cultured cells and embryonic and neonatal tissues. This feature provides a link between sirtuin expression and the cellular response to nutrient constraints due to caloric restriction. SIRT1 inhibits NF-κB regulated gene expression by deacetylating the RelA/p65 subunit of NF-κB in lysine 310. SIRT1 plays a role in activating T17 helper cells that contribute to autoimmune disease.