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PXD011935

DataSet Summary

  • HostingRepository: PRIDE
  • AnnounceDate: 2019-06-11
  • AnnouncementXML: Submission_2019-07-12_05:35:32.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
22019-07-12 05:35:33announcedUpdated publication reference for PubMed record(s): 28270554, 31208443.

Publication List

  1. Janschitz M, Romanov N, Varnavides G, Hollenstein DM, Gérecová G, Ammerer G, Hartl M, Reiter W, Novel interconnections of HOG signaling revealed by combined use of two proteomic software packages. Cell Commun Signal, 17(1):66(2019) [pubmed]
  2. 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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