PXD002158 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Members of the Plant CRK-superfamily are Capable of trans-/auto-Phosphorylation of Tyrosine Residues |
Description | Protein phosphorylation on Tyr residues is a key post-translational modification in mammals. In plants, recent studies have identified Tyr-specific protein phosphatase and Tyr-phosphorylated proteins in Arabidopsis by phosphoproteomic screenings, implying that plants have a Tyr phosphorylation signal pathway. However, little is known about the protein kinases (PKs) involved in Tyr phosphorylation in plants. Here, we demonstrate that Arabidopsis calcium-dependent protein kinase (CDPK/CPK)-related PKs (CRKs) have high Tyr autophosphorylation activity and that they can phosphorylate Tyr residue(s) on substrate proteins in Arabidopsis. In order to identify PKs for Tyr phosphorylation, we examined the autophosphorylation activity of 759 PKs using an Arabidopsis protein array based on a wheat cell-free system. In total, we identified 38 PKs with Tyr autophosphorylation activity. The CRK family was a major protein family identified. A cell-free substrate screening revealed that these CRKs phosphorylate beta-tubulin (TBB) 2, TBB7 and certain transcription factors (TFs) such as ethylene response factor 13 (ERF13). All five CRKs tested showed Tyr auto/trans-phosphorylation activity and especially two CRKs, CRK2 and CRK3, showed a high ERF13 Tyr phosphorylation activity. A cell-based transient expression assay revealed that Tyr16/207 sites in ERF13 were phosphorylated by CRK3 and that Tyr phosphorylation of endogenous TBBs occurs in CRK2 overexpressing cells. Furthermore, crk2 and crk3 mutants showed a decrease in the Tyr phosphorylation level of TBBs. These results suggest that CRKs have Tyr kinase activity, and these might be one of the major PKs responsible for protein Tyr-phosphorylation in Arabidopsis plants. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:24:01.769.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Nobuaki Takemori |
SpeciesList | scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702; |
ModificationList | No PTMs are included in the dataset |
Instrument | LTQ |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2015-05-11 01:04:57 | ID requested | |
1 | 2018-10-24 09:45:50 | announced | |
⏵ 2 | 2024-10-22 04:24:03 | announced | 2024-10-22: Updated project metadata. |
Publication List
10.1074/jbc.M114.617274; |
Nemoto K, Takemori N, Seki M, Shinozaki K, Sawasaki T, Members of the Plant CRK Superfamily Are Capable of Trans- and Autophosphorylation of Tyrosine Residues. J Biol Chem, 290(27):16665-77(2015) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: Arabidopsis |
phosphotyrosine signaling |
Contact List
Nobuaki Takemori |
contact affiliation | Ehime University |
contact email | takemori@m.ehime-u.ac.jp |
lab head | |
Nobuaki Takemori |
contact affiliation | Ehime University, JAPAN |
contact email | takemori@m.ehime-u.ac.jp |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD002158
- Label: PRIDE project
- Name: Members of the Plant CRK-superfamily are Capable of trans-/auto-Phosphorylation of Tyrosine Residues