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Phosphoproteomic analyses reveal novel cross-modulation mechanisms between two signaling pathways in yeast.

Vaga S, Bernardo-Faura M, Cokelaer T, Maiolica A, Barnes CA, Gillet LC, Hegemann B, van Drogen F, Sharifian H, Klipp E, Peter M, Saez-Rodriguez J, Aebersold R - Mol. Syst. Biol. (2014)

Bottom Line: We observed a pheromone-induced down-regulation of Hog1 phosphorylation due to Gpd1, Ste20, Ptp2, Pbs2, and Ptc1.Distinct Ste20 and Pbs2 phosphosites responded differently to the two stimuli, suggesting these proteins as key mediators of the information exchange.Our results show that the integration of the response to different stimuli requires complex interconnections between signaling pathways.

View Article: PubMed Central - PubMed

Affiliation: Department of Biology, Institute of Molecular Systems Biology ETH Zürich, Zürich, Switzerland.

No MeSH data available.


Related in: MedlinePlus

Classification of phosphopeptides (P-peps) according to how NaCl and pheromone affect the shape of their dynamic curves
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fig04: Classification of phosphopeptides (P-peps) according to how NaCl and pheromone affect the shape of their dynamic curves

Mentions: To better understand how the co-stimulation affected the dynamic P-pep patterns, we manually investigated their 2D representations (Fig3C) along the time-axes for both stimuli. This analysis showed that, in the case of some P-peps, the length of the application of Stimulus_2 (either NaCl or pheromone) significantly changed the shape of the curves plotted against the time following the application of Stimulus_1 (pheromone or NaCl, respectively). In the following, we call this the “Shape Effect” of Stimulus_2 (Fig4A). Most of the P-pep changes following this pattern occurred in the first 5′ following Stimulus_1 application, and they mostly appeared as changes in curve concavity, as an increase/decrease in the number of maximums and minimums of the curves (e.g. a biphasic curve becomes triphasic), or as a change in curve shape with earlier or later onset. All these patterns suggest that Stimulus_2 significantly affected the dynamics of these P-peps by altering their behavior along Stimulus_1 time-axis.


Phosphoproteomic analyses reveal novel cross-modulation mechanisms between two signaling pathways in yeast.

Vaga S, Bernardo-Faura M, Cokelaer T, Maiolica A, Barnes CA, Gillet LC, Hegemann B, van Drogen F, Sharifian H, Klipp E, Peter M, Saez-Rodriguez J, Aebersold R - Mol. Syst. Biol. (2014)

Classification of phosphopeptides (P-peps) according to how NaCl and pheromone affect the shape of their dynamic curves
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4300490&req=5

fig04: Classification of phosphopeptides (P-peps) according to how NaCl and pheromone affect the shape of their dynamic curves
Mentions: To better understand how the co-stimulation affected the dynamic P-pep patterns, we manually investigated their 2D representations (Fig3C) along the time-axes for both stimuli. This analysis showed that, in the case of some P-peps, the length of the application of Stimulus_2 (either NaCl or pheromone) significantly changed the shape of the curves plotted against the time following the application of Stimulus_1 (pheromone or NaCl, respectively). In the following, we call this the “Shape Effect” of Stimulus_2 (Fig4A). Most of the P-pep changes following this pattern occurred in the first 5′ following Stimulus_1 application, and they mostly appeared as changes in curve concavity, as an increase/decrease in the number of maximums and minimums of the curves (e.g. a biphasic curve becomes triphasic), or as a change in curve shape with earlier or later onset. All these patterns suggest that Stimulus_2 significantly affected the dynamics of these P-peps by altering their behavior along Stimulus_1 time-axis.

Bottom Line: We observed a pheromone-induced down-regulation of Hog1 phosphorylation due to Gpd1, Ste20, Ptp2, Pbs2, and Ptc1.Distinct Ste20 and Pbs2 phosphosites responded differently to the two stimuli, suggesting these proteins as key mediators of the information exchange.Our results show that the integration of the response to different stimuli requires complex interconnections between signaling pathways.

View Article: PubMed Central - PubMed

Affiliation: Department of Biology, Institute of Molecular Systems Biology ETH Zürich, Zürich, Switzerland.

No MeSH data available.


Related in: MedlinePlus