First published online February 18, 2009
Journal of Cell Science 122, 502e (2009)
© The Company of Biologists Limited
WHI2 saves starving yeast
Tight regulation of cell death and proliferation allows the budding yeast Saccharomyces cerevisiae to adapt to changes in environmental stress and nutritional availability. When nutritional sources become limiting, yeast-cell proliferation transitions from log-phase growth to what is known as the diauxic shift, followed by entry into a quiescent phase. Recent work has shown that hyperactivation of the Ras-cAMP-PKA signalling cascade is associated with apoptosis during the diauxic shift; however, how these events are linked is not well understood. Now, Campbell Gourlay and colleagues (p. 706) show that the protein encoded by WHI2 has a central role in regulating apoptosis of S. cerevisiae during the diauxic shift. They show that, compared with wild-type cells,
whi2 mutants have increased actin aggregation, a loss of mitochondrial membrane potential and an accumulation of reactive oxygen species (ROS), which collectively lead to decreased cell viability. If the Ras-cAMP-PKA signalling cascade is blocked,
whi2 cells are rescued from apoptosis caused by actin aggregation and ROS. Furthermore, the Whi2 protein was found to regulate the trafficking and degradation of Ras2 during the diauxic shift and thereby inhibit the Ras-cAMP-PKA pathway. Therefore, the authors conclude that WHI2 is essential for coordinating yeast-cell survival following nutritional depletion.

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Related articles in JCS:
- Whi2p links nutritional sensing to actin-dependent Ras-cAMP-PKA regulation and apoptosis in yeast
- Jane E. Leadsham, Katherine Miller, Kathryn R. Ayscough, Sonia Colombo, Enzo Martegani, Pete Sudbery, and Campbell W. Gourlay
JCS 2009 122: 706-715.
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