Phosphorylation of Hsl1 by Hog1 leads to a G2 arrest essential for cell survival at high osmolarity

Clotet Bellmunt, Josep; Escoté, Xavier; Àngel Adrover, Miquel; Yaakov, Gilad; Garí Marsol, Eloi; Aldea, Martí; de Nadal, Eulàlia; Posas, Francesc

doi:https://doi.org/10.1038/sj.emboj.7601095

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Issue date

2006

Author

Clotet Bellmunt, Josep

Escoté, Xavier

Àngel Adrover, Miquel

Yaakov, Gilad

Garí Marsol, Eloi

Aldea, Martí

de Nadal, Eulàlia

Posas, Francesc

Suggested citation

Clotet Bellmunt, Josep; Escoté, Xavier; Àngel Adrover, Miquel; Yaakov, Gilad; Garí Marsol, Eloi; Aldea, Martí; ... Posas, Francesc. (2006) . Phosphorylation of Hsl1 by Hog1 leads to a G2 arrest essential for cell survival at high osmolarity. The EMBO Journal, 2006, vol. 25, p. 2338–2346. https://doi.org/10.1038/sj.emboj.7601095.

Abstract

Control of cell cycle progression by stress-activated protein kinases (SAPKs) is essential for cell adaptation to extracellular stimuli. Exposure of yeast to osmostress leads to activation of the Hog1 SAPK, which controls cell cycle at G1 by the targeting of Sic1. Here, we show that survival to osmostress also requires regulation of G2 progression. Activated Hog1 interacts and directly phosphorylates a residue within the Hsl7-docking site of the Hsl1 checkpoint kinase, which results in delocalization of Hsl7 from the septin ring and leads to Swe1 accumulation. Upon Hog1 activation, cells containing a nonphosphorylatable Hsl1 by Hog1 are unable to promote Hsl7 delocalization, fail to arrest at G2 and become sensitive to osmostress. Together, we present a novel mechanism that regulates the Hsl1–Hsl7 complex to integrate stress signals to mediate cell cycle arrest and, demonstrate that a single MAPK coordinately modulates different cell cycle checkpoints to improve cell survival upon stress.

URI

http://hdl.handle.net/10459.1/59047

DOI

https://doi.org/10.1038/sj.emboj.7601095

Is part of

The EMBO Journal, 2006, vol. 25, p. 2338–2346