Signal processing by the HOG MAP kinase pathway

Signaling pathways relay information about changes in the external environment so that cells can respond appropriately. How much information a pathway can carry depends on its bandwidth. We designed a microfluidic device to reliably change the environment of single cells over a range of frequencies....

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2008-05, Vol.105 (20), p.7165-7170
Main Authors: Hersen, Pascal, McClean, Megan N, Mahadevan, L, Ramanathan, Sharad
Format: Article
Language:English
Subjects:
Biochemistry
Biological Sciences
Biomechanics
Cell lines
Cells
enzyme activity
Frequency ranges
Fungi
Gene Deletion
Gene Expression Regulation
Gene Expression Regulation, Fungal
glycerol
High frequencies
hyper osmolar glycerol
Image Processing, Computer-Assisted
Inflammation
Kinases
laboratory equipment
MAP Kinase Kinase Kinases - metabolism
MAP Kinase Signaling System
Mechanics
Microfluidic Analytical Techniques
Microfluidic devices
Microfluidics
mitogen-activated protein kinase
Mitogen-Activated Protein Kinases - metabolism
Models, Biological
osmolarity
osmoregulation
osmotic pressure
Phosphorylation
Physics
Plasmids - metabolism
protein phosphorylation
Reaction kinetics
Saccharomyces cerevisiae
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins
Signal bandwidth
Signal Transduction
Yeast
Yeasts
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Summary:Signaling pathways relay information about changes in the external environment so that cells can respond appropriately. How much information a pathway can carry depends on its bandwidth. We designed a microfluidic device to reliably change the environment of single cells over a range of frequencies. Using this device, we measured the bandwidth of the Saccharomyces cerevisiae signaling pathway that responds to high osmolarity. This prototypical pathway, the HOG pathway, is shown to act as a low-pass filter, integrating the signal when it changes rapidly and following it faithfully when it changes more slowly. We study the dependence of the pathway's bandwidth on its architecture. We measure previously unknown bounds on all of the in vivo reaction rates acting in this pathway. We find that the two-component Ssk1 branch of this pathway is capable of fast signal integration, whereas the kinase Ste11 branch is not. Our experimental techniques can be applied to other signaling pathways, allowing the measurement of their in vivo kinetics and the quantification of their information capacity.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0710770105