Regulation of the NAD + -dependent deacetylase SIRT2 by CDK5

TL;DRAbstract

SIRT2 belongs to the protein family of sirtuins, which are homologs of the yeast silencing information regulator 2 (Sir2), an NAD+-dependent histone deacetylase. Seven different sirtuins, SIRT1-7, have been identified in mammals, which share a common catalytic core domain but possess distinct N- and C-terminal extensions. In the case of SIRT2 this core domain elicits an NAD+-dependent deacetylase activity. SIRT2 is the only sirtuin, which is predominantly localized in the cytoplasm. It is highly abundant in the brain, especially in myelin-forming oligodendrocytes. Cellular processes, in which SIRT2 is implicated, include differentiation, neurite outgrowth, autophagy, and spindle checkpoint activation. In addition, SIRT2 is associated with neurodegenerative diseases, such as Huntington's and Alzheimer's disease. These findings strongly suggest that SIRT2 is tightly controlled and potentially responsive to different signal transduction pathways. However, very little is known about how SI

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