Molecular and cellular regulatory roles of sirtuin protein

Sirtuins (SIRT) are unique posttranslational modification enzymes that utilize NAD + as co-substrate to remove acyl groups from lysine residues. SIRT act on variety of substrates and impact major metabolic process. All seven members of SIRT family are unique and targets wide range of cellular proteins in nucleus, cytoplasm, and mitochondria for post-translational modification by acetylation (SIRT1, 2, 3, and 5) or ADP-ribosylation (SIRT4 and 6). Each member of SIRT family is distinct. SIRT2 was first to be discovered that incited research on mammalian SIRT. Enzymatic activities of SIRT 4 are yet to be elucidated while only SIRT7 is localized in nucleoli that govern the transcription of RNA polymerase I. SIRT 5 and 6 exhibit weakest deacetylase activity. Out of all SIRT analogs, SIRT1 is identified as nutrient sensor. Increased expression of only SIRT3 is linked with longevity in humans. Since SIRT is regulated by the bioenergetic state of the cell, nutrition impacts it but very few studies about diet-mediated effect on SIRT are reported. The present review elaborates distribution, specific biological role and prominent effect of all SIRT on vital human tissue along with highlighting need to trace molecular mechanisms and identifying foods that may augment it beneficially.

Automated summary

Sirtuins (SIRT) are a unique group of enzymes that can remove acyl groups from lysine residues using NAD+ as a co-substrate. The members of the SIRT family have distinct characteristics and biological functions, affecting various metabolic processes in different cellular locations. Understanding the distribution, specific biological roles, and effects of SIRT in human tissues is crucial for identifying molecular mechanisms and finding foods that can beneficially enhance SIRT activity.