Fig. 3. Post-translational modification of SIRT1 by intracellular signaling molecules. SIRT1 protein consists of 747 amino acids and is commonly divided into three functional domains, N-terminal domain, catalytic domain, and C-terminal domain. SIRT1 can be modified by various post-translational modifications, leading to alteration of its catalytic activity or expression. In general, cysteine residues are susceptible to oxidation/reduction, carbonylation, S-nitrosylation, and S-nitrosation. Likewise, serine/threonine residues are particularly sensitive to phosphorylation and O-linked glycosylation. Lysine residues are readily targeted by ubiquitination and SUMOylation. P, Phosphorylation; Ox, oxidation; Re, reduction; N, S-Nitrosylation or S-Nitrosation; C, carbonylation; G, O-GlcNacylation; Ub, ubiquitination; S, SUMOylation; JNK, c-Jun N-terminal kinase; GSNO, S-Nitrosoglutathione; GSH, glutathione; CK, casein kinase; JAK, Janus kinase; OGT, O-linked-β-N-acetylglucosamine (O-GlcNAc) transferase; MDM2, mouse double minute 2 homolog; AMPK, AMP-activated protein kinase; Ref-1, redox factor-1; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; PKA, protein kinase A; 4-HNE, 4-Hydroxy-2-nonenal; DYRK, dual-specificity tyrosine phosphorylation-regulated kinase; SMURF2, Smad ubiquitination regulatory Factor 2; CDK, Cyclin-dependent kinase; LKB1, liver kinase 1.

© J Cancer Prev