Research ResourceCell Biology

Identifying protein kinase–specific effectors of the osmostress response in yeast

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Sci. Signal.  07 Mar 2017:
Vol. 10, Issue 469, eaag2435
DOI: 10.1126/scisignal.aag2435

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Defining the osmotic stress phosphoproteome

The high-osmolarity glycerol (HOG) pathway is critical for the ability of the budding yeast Saccharomyces cerevisiae to respond to increased extracellular osmolarity. Hog1 is the mitogen-activated protein kinase (MAPK) homolog at the core of this pathway. Romanov et al. combined inhibition of Hog1 with mass spectrometry analysis to identify Hog1-dependent and Hog1-independent osmostress-induced changes in the yeast phosphoproteome. By examining cells at different time points after the induction of osmotic stress, the authors predicted which Hog1-dependent phosphorylation events were likely to be directly mediated by Hog1 and validated these targets in protein-protein proximity assays. The kinase Rck2, a direct target of Hog1, controlled the phosphorylation of many indirect targets of Hog1. Gene ontology analysis indicated that these direct and indirect targets of Hog1 affected diverse cellular functions and identified some processes not previously implicated in the HOG-mediated response to osmotic stress.