Transient activation of fission yeast AMPK is required for cell proliferation during osmotic stress

• DOI: 10.1091/mbc.e17-04-0235
• Publication Date: 2017-05-18T00:50:18Z
• Authors: Katherine L. Schutt; James B. Moseley
• Keywords: Osmotic shock; AMP-Activated Protein Kinase

The heterotrimeric kinase AMPK acts as an energy sensor to coordinate cell metabolism with environmental status in species from yeast through humans. Low intracellular ATP leads activation phosphorylation of the loop within catalytic subunit. Other stresses also activate AMPK, but it is unclear whether cellular affects under these conditions. Fission subunit Ssp2 phosphorylated at Thr-189 by upstream Ssp1 low-glucose conditions, similar other systems. Here we find that hyperosmotic stress induces strong Ssp2-T189 Ssp1. Ssp2-pT189 during osmotic transient and regulation targets, unlike sustained low glucose. Cells lacking this mechanism fail proliferate after stress. Activation requires sensing heterotrimer, decreased levels. We observed mitochondrial fission stress, blocking did not affect activation. Stress-activated kinases Sty1 Pmk1 promote contributed subsequent inactivation. Our results show allows cells manage for proliferation new states.