Abstract
Although the benefit of sirtuin activation in age-related diseases is well-characterized, the benefit of sirtuin activation in acute diseases has been elusive. Here we discuss that, at least in yeast, Sir2 activation prevents programmed cell death induced by the sustained activation of the stress activated protein kinase (SAPK) Hog1, the yeast homologue of the p38 SAPK. Sir2 prevents ROS formation and maximize cell survival upon SAPK activation. The conserved function of Sir2 in age-related diseases and the conserved role of SAPKs open the possibility of a novel role for sirtuins in cell fate determination in eukaryotic cells.
Highlights
Activation of sirtuins has been proved to be positive in age-related diseases [1,2,3,4,5]
The transient activation of the stress activated protein kinase (SAPK) serves to control many aspects of the cell physiology ranging from control of metabolism, cell cycle progression and gene expression which are essential for cellular adaptation to stress [11,12,13,14,15]
Despite the essential role of Hog1 in cell survival upon stress, it has been known for a long time that sustained activation of the SAPK was deleterious for cell growth as it has been shown by other MAPKs [16,17,18]
Summary
Activation of sirtuins has been proved to be positive in age-related diseases [1,2,3,4,5]. Despite the essential role of Hog1 in cell survival upon stress, it has been known for a long time that sustained activation of the SAPK was deleterious for cell growth as it has been shown by other MAPKs [16,17,18]. The study by Vendrell et al shows that inhibition of cell growth by sustained activation of Hog1 is caused by the induction of apoptosis-like cell death in yeast.
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