Mol. Cells 2008; 26(2): 200-205
Published online January 1, 1970
© The Korean Society for Molecular and Cellular Biology
The mitogen-activated protein kinase (MAPK) signaling pathway is activated in response to extracellular stimuli and regulates various activities in eukaryotic cells. Following exposure to stimuli, MAPK is known to be activated via dual phosphorylation at a conserved TxY motif in the activation loop; both threonine and tyrosine residues are phosphorylated by an upstream kinase. However, the mechanism underlying dual phosphorylation is not clearly understood. In the budding yeast Saccharomyces cerevisiae, the Hog1 MAPK mediates the high-osmolarity glycerol (HOG) signaling pathway. Tandem mass spectrometry and phosphospecific immunoblotting were performed to quantitatively monitor the dynamic changes occurring in the phosphorylation status of the TxY motif of Hog1 on exposure to osmotic stress. The results of our study suggest that the tyrosine residue is preferentially and dynamically phosphorylated following stimulation, and this in turn leads to the dual phosphorylation. The tyrosine residue was hyperphosphorylated in the absence of a threonine residue; this result suggests that the threonine residue is critical for the control of signaling noise and adaptation to osmotic stress.
Keywords Hog1, MAP kinase, mass spectrometry, phosphorylation, MS/MS, signal transduction, yeast
Mol. Cells 2008; 26(2): 200-205
Published online August 31, 2008
Copyright © The Korean Society for Molecular and Cellular Biology.
Min-Yeon Choi, Gum-Yong Kang, Jae-Young Hur, Jin Woo Jung, Kwang Pyo Kim and Sang-Hyun Park
The mitogen-activated protein kinase (MAPK) signaling pathway is activated in response to extracellular stimuli and regulates various activities in eukaryotic cells. Following exposure to stimuli, MAPK is known to be activated via dual phosphorylation at a conserved TxY motif in the activation loop; both threonine and tyrosine residues are phosphorylated by an upstream kinase. However, the mechanism underlying dual phosphorylation is not clearly understood. In the budding yeast Saccharomyces cerevisiae, the Hog1 MAPK mediates the high-osmolarity glycerol (HOG) signaling pathway. Tandem mass spectrometry and phosphospecific immunoblotting were performed to quantitatively monitor the dynamic changes occurring in the phosphorylation status of the TxY motif of Hog1 on exposure to osmotic stress. The results of our study suggest that the tyrosine residue is preferentially and dynamically phosphorylated following stimulation, and this in turn leads to the dual phosphorylation. The tyrosine residue was hyperphosphorylated in the absence of a threonine residue; this result suggests that the threonine residue is critical for the control of signaling noise and adaptation to osmotic stress.
Keywords: Hog1, MAP kinase, mass spectrometry, phosphorylation, MS/MS, signal transduction, yeast
Jae-Young Hur, Gum-Yong Kang, Min-Yeon Choi, Jin Woo Jung, Kwang-Pyo Kim and Sang-Hyun Park
Sunbae Lee*, and Yun Soo Bae
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