PXD011935 is an
original dataset announced via ProteomeXchange.
Dataset Summary
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. |
HostingRepository | PRIDE |
AnnounceDate | 2019-06-11 |
AnnouncementXML | Submission_2019-07-12_05:35:32.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Wolfgang Reiter |
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
Revision | Datetime | Status | ChangeLog Entry |
0 | 2018-12-04 23:20:14 | ID requested | |
1 | 2019-06-11 00:08:53 | announced | |
⏵ 2 | 2019-07-12 05:35:33 | announced | Updated publication reference for PubMed record(s): 28270554, 31208443. |
Publication List
Janschitz M, Romanov N, Varnavides G, Hollenstein DM, G, é, recov, á 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] |
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
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
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD011935
- Label: PRIDE project
- Name: Novel interconnections of HOG signaling revealed by combined use of two proteomic software packages