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Research Article
AMPK phosphorylation by Ssp1 is required for proper sexual differentiation in fission yeast
Noelia Valbuena, Sergio Moreno
J Cell Sci 2012 : jcs.098533 doi: 10.1242/jcs.098533 Published 28 February 2012
Noelia Valbuena
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Sergio Moreno
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Summary

The AMP-activated protein kinase (AMPK) is a central regulator of cellular energy homeostasis that, in response to a fall in intracellular ATP levels, activates energy-producing pathways and inhibits energy-consuming processes. Here, we report that fission yeast cells lacking AMPK activity are unable to advance entry into mitosis in response to nitrogen starvation and to undergo proper G1 arrest and cell differentiation. We also show that AMPK is important in the promotion of the nuclear localization and accumulation of the Ste11 transcription factor. As in animal cells, the fission yeast CaMKK orthologue (Ssp1) phosphorylates and activates the catalytic subunit of AMPK (Ssp2) in its activation loop (Thr189) when cells are starved for nitrogen or glucose. Interestingly, we found that the phosphorylation of Ssp2 on Thr189 is required for AMPK nuclear accumulation. Our data demonstrate the existence of a signal transduction pathway activated by nutrient starvation that triggers Ssp2 phosphorylation and AMPK redistribution from the cytoplasm to the nucleus. This pathway is important to advance fission cells into mitosis and to establish a timely pre-Start G1 cell cycle arrest in order to mate.

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AMPK phosphorylation by Ssp1 is required for proper sexual differentiation in fission yeast
Noelia Valbuena, Sergio Moreno
J Cell Sci 2012 : jcs.098533 doi: 10.1242/jcs.098533 Published 28 February 2012
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AMPK phosphorylation by Ssp1 is required for proper sexual differentiation in fission yeast
Noelia Valbuena, Sergio Moreno
J Cell Sci 2012 : jcs.098533 doi: 10.1242/jcs.098533 Published 28 February 2012

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