PXD002158

PXD002158 is an original dataset announced via ProteomeXchange.

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

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.

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]

curator keyword: Biological

submitter keyword: Arabidopsis

phosphotyrosine signaling

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

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/2018/10/PXD002158

PRIDE project URI

• PRIDE
  1. PXD002158
     1. Label: PRIDE project
     2. Name: Members of the Plant CRK-superfamily are Capable of trans-/auto-Phosphorylation of Tyrosine Residues