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PXD011935

DataSet Summary

  • HostingRepository: PRIDE
  • AnnounceDate: 2019-06-11
  • AnnouncementXML: Submission_2019-06-11_00:08:52.xml
  • DigitalObjectIdentifier:
  • ReviewLevel: Peer-reviewed dataset
  • DatasetOrigin: Original data
  • RepositorySupport: Unsupported dataset by repository
  • PrimarySubmitter: Wolfgang Reiter
  • Title: Novel interconnections of HOG signaling revealed by combined use of two proteomic software packages
  • Description: Modern quantitative mass spectrometry (MS)-based proteomics enables researchers to unravel signaling networks by monitoring proteome-wide cellular responses to different stimuli. MS-based analysis of signaling systems usually requires an integration of multiple quantitative MS experiments, which remains challenging, given that the overlap between these datasets is not necessarily comprehensive. In a previous study we analyzed the impact of the yeast mitogen-activated protein kinase (MAPK) Hog1 on the hyperosmotic stress-affected phosphorylome. Using a combination of a series of hyperosmotic stress and kinase inhibition experiments, we identified a broad range of direct and indirect substrates of the MAPK. Here we re-evaluate this extensive MS dataset and demonstrate that a combined analysis based on two software packages, MaxQuant and Proteome Discoverer, increases the coverage of Hog1 target proteins by 30%. Using protein-protein proximity assays we show that the majority of new targets gained by this analysis are indeed Hog1 interactors. Additionally, kinetic profiles indicate differential trends of Hog1-dependent versus Hog1-independent phosphorylation sites. Our findings highlight a previously unrecognized interconnection between Hog1 signaling and the RAM signaling network, as well as sphingolipid homeostasis.
  • SpeciesList: scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
  • ModificationList: phosphorylated residue; 6x(13)C labeled residue; monohydroxylated residue; deamidated residue; iodoacetamide derivatized residue
  • Instrument: LTQ FT; LTQ Orbitrap Velos; Q Exactive

Dataset History

VersionDatetimeStatusChangeLog Entry
02018-12-04 23:20:14ID requested
12019-06-11 00:08:53announced

Publication List

  1. Romanov N, Hollenstein DM, Janschitz M, Ammerer G, Anrather D, Reiter W, Identifying protein kinase-specific effectors of the osmostress response in yeast. Sci Signal, 10(469):(2017) [pubmed]

Keyword List

  1. submitter keyword: Proteome Discoverer, MaxQuant, Proteomics, Mitogen-activated protein kinase (MAPK), Hyperosmotic stress response, High-osmolarity glycerol (HOG), Hog1, Kic1, Orm2, ORMDL, p38

Contact List

    Wolfgang L. Reiter
    • contact affiliation: Mass Spectrometry Facility, Max F. Perutz Laboratories, University of Vienna, Vienna BioCenter, Vienna, Austria
    • contact email: wolfgang.l.reiter@univie.ac.at
    • lab head:
    Wolfgang Reiter
    • contact affiliation: MAX F. PERUTZ LABORATORIES - University of Vienna
    • contact email: wolfgang.l.reiter@univie.ac.at
    • dataset submitter:

Full Dataset Link List

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