PXD010053 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Mapping Proteome-Wide Targets of Protein Kinases in Response to Stresses |
Description | Protein kinases are major regulatory components in almost all cellular processes in eukaryotic cells. By adding phosphate groups, protein kinases regulate the activity, localization, protein-protein interactions and other profiles of their target proteins. It is known that protein kinases such as SNF1 related protein kinase 2 and 3 (SnRK2 and SnRK3), calcium dependent protein kinases (CDPKs), and mitogen activated protein kinases (MAPKs) are central components in plant response to environmental stresses such as drought, high salinity, cold and pathogen attack. Although the phosphorylation-dependent signaling plays critical roles in plant stress biology, only a few targets of these protein kinases have been identified. How these protein kinases regulate the downstream biological processes and mediate the stress responses are still largely unknown. In this study, we developed an isotope labeled protein kinase assay-based approach with enriched phosphoproteome as kinase-substrates pool to identify the putative substrates of 8 protein kinases that function in plant abiotic and biotic stress responses. As a result, we identified more than 5,081 putative targets of osmotic stress-activated SnRK2.4 and SnRK2.6, ABA activated protein kinases SnRK2.6 and Casein-Kinase Like 2 (CKL2), elicitor-activated protein kinase CDPK11 and MPK6, cold-activated protein kinase MPK6, H2O2-activated protein kinase OXI1 and MPK6, salt-induced protein kinase SOS1 and MPK6, as well as the low-potassium-activated protein kinase CIPK23. We also analyzed the conserved motif and functional ontology of these putative kinase targets. These results provide comprehensive information on the role of these protein kinases in the control of cellular activities and could be valuable resource for further study on the mechanism underlying plant response to environmental stresses. |
HostingRepository | PRIDE |
AnnounceDate | 2020-01-16 |
AnnouncementXML | Submission_2020-02-17_03:19:59.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Chuan-Chih Hsu |
SpeciesList | scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702; |
ModificationList | phosphorylated residue |
Instrument | LTQ Orbitrap Velos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2018-06-07 01:37:43 | ID requested | |
1 | 2020-01-16 00:59:03 | announced | |
⏵ 2 | 2020-02-17 03:20:01 | announced | 2020-02-17: Updated publication reference for PubMed record(s): 31992638. |
3 | 2024-10-22 04:45:50 | announced | 2024-10-22: Updated project metadata. |
Publication List
Wang P, Hsu CC, Du Y, Zhu P, Zhao C, Fu X, Zhang C, Paez JS, Macho AP, Tao WA, Zhu JK, Mapping proteome-wide targets of protein kinases in plant stress responses. Proc Natl Acad Sci U S A, 117(6):3270-3280(2020) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: Plant kinase, Stress, Phosphoproteomics |
Contact List
jian-Kang Zhu |
contact affiliation | Shanghai Center for Plant Stress Biology |
contact email | jkzhu@sibs.ac.cn |
lab head | |
Chuan-Chih Hsu |
contact affiliation | Purdue University |
contact email | without1102@gmail.com |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2020/01/PXD010053 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD010053
- Label: PRIDE project
- Name: Mapping Proteome-Wide Targets of Protein Kinases in Response to Stresses