ArticlePloS one2013
Ssk1p-independent activation of Ssk2p plays an important role in the osmotic stress response in Saccharomyces cerevisiae: alternative activation of Ssk2p in osmotic stress.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Osmostress enhances activating phosphorylation of Hog1 MAP kinase by mono-phosphorylated Pbs2 MAP2K.The EMBO journal · 2020Article
- RNAi screening identifies Trypanosoma brucei stress response protein kinases required for survival in the mouse.Scientific reports · 2017Article
- Ineffective Phosphorylation of Mitogen-Activated Protein Kinase Hog1p in Response to High Osmotic Stress in the Yeast Kluyveromyces lactis.Eukaryotic cell · 2015Article
- The Pho4 transcription factor mediates the response to arsenate and arsenite in Candida albicans.Frontiers in microbiology · 2015Article
- Joint inhibition of TOR and JNK pathways interacts to extend the lifespan of Brachionus manjavacas (Rotifera).Experimental gerontology · 2014Article
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Authors and funding
4 authors.
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Abstract
In Saccharomyces cerevisiae, external high osmolarity activates the HOG MAPK pathway, which controls various aspects of osmoregulation. MAPKKK Ssk2 is activated by Ssk1 in the SLN1 branch of the osmoregulatory HOG MAPK pathway under hyperosmotic stress. We observed that Ssk2 can be activated independent of Ssk1 upon osmotic shock by an unidentified mechanism. The domain for the Ssk1p-independent activation was identified to be located between the amino acids 177∼240. This region might be involved in the binding of an unknown regulator to Ssk2 which in turn activates Ssk2p without Ssk1p under hyperosmotic stress. The osmotic stress response through the Ssk1p-independent Ssk2p activation is strong, although its duration is short compared with the Ssk1p-dependent activation. The alternative Ssk2p activation is also important for the salt resistance.
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