Proteomics

Dataset Information

0

Salt stress phosphorylation network


ABSTRACT: We utilized high resolution, high mass accuracy quantitative proteomics to explore stress signaling in yeast. We accessed changes in protein phosphorylation at various time points after exposure to salt stress and used this information to reconstruct stress signaling networks. We performed similar experiments using yeast knockouts to monitor network re-wiring and performed co-IPs to validate protein-protein interactions predicted by the networks.

INSTRUMENT(S): Orbitrap Fusion ETD, LTQ Orbitrap Elite

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

TISSUE(S): Permanent Cell Line Cell

DISEASE(S): Disease Free

SUBMITTER: Evgenia Shishkova  

LAB HEAD: Joshua J Coon

PROVIDER: PXD006192 | Pride | 2018-04-05

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
12Dec2016_ES_allIPs.xlsx Xlsx
20161204_ES_Cdc14_t0_rep1.raw Raw
20161204_ES_Cdc14_t0_rep2.raw Raw
20161204_ES_Cdc14_t10_rep1.raw Raw
20161204_ES_Cdc14_t10_rep2.raw Raw
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Publications

Network inference reveals novel connections in pathways regulating growth and defense in the yeast salt response.

MacGilvray Matthew E ME   Shishkova Evgenia E   Chasman Deborah D   Place Michael M   Gitter Anthony A   Coon Joshua J JJ   Gasch Audrey P AP  

PLoS computational biology 20180508 5


Cells respond to stressful conditions by coordinating a complex, multi-faceted response that spans many levels of physiology. Much of the response is coordinated by changes in protein phosphorylation. Although the regulators of transcriptome changes during stress are well characterized in Saccharomyces cerevisiae, the upstream regulatory network controlling protein phosphorylation is less well dissected. Here, we developed a computational approach to infer the signaling network that regulates ph  ...[more]

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