PXD008200

PXD008200 is an original dataset announced via ProteomeXchange.

Title	Combined 15N-Labelling and TandemMOAC Quantifies Phosphorylation of MAP Kinase Substrates Downstream of MKK7 in Arabidopsis
Description	Reversible protein phosphorylation is a widespread posttranslational modification that plays a key role in eukaryotic signal transduction. Due to the large dynamic range of protein abundance, low stoichiometry and transient nature of protein phosphorylation, the detection and accurate quantification of substrate phosphorylation by protein kinases remains a challenge. Here, we combine tandem metal-oxide affinity chromatography (tandemMOAC) with stable isotope 15N metabolic labeling for the mass spectrometry measurement and accurate quantification of low abundant, transiently phosphorylated peptides. Since tandemMOAC is not biased towards the enrichment of acidophilic, basophilic or proline-directed kinase substrates, the method is applicable to identify targets of members of all three classes of protein kinases. Using this phosphoproteomics approach, we identified several mitogen-activated protein kinase (MPK) substrates downstream of the MKK7-MPK3/6 phosphorylation cascade of Arabidopsis. The MKK7-MPK3/6 module is involved in the regulation of plant development and plant basal and systemic immune responses but little is known about downstream cascade components. The identification and validation of dynamin-related protein (DRP) 2 as a novel phosphorylation substrate of the MKK7-MPK3/6 module establishes a novel link between MPK signaling and clathrin-mediated vesicle trafficking.
HostingRepository	PRIDE
AnnounceDate	2018-01-02
AnnouncementXML	Submission_2018-01-02_02:51:50.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Wolfgang Hoehenwarter
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationList	No PTMs are included in the dataset
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2017-11-13 09:35:53	ID requested
⏵ 1	2018-01-02 02:51:51	announced

Huck NV, Leissing F, Majovsky P, Buntru M, Aretz C, Flecken M, M, ü, ller JPJ, Vogel S, Schillberg S, Hoehenwarter W, Conrath U, Beckers GJM, . Front Plant Sci, 8():2050(2017) [pubmed]

curator keyword: Biological

submitter keyword: MAPK, MPK Substrate, Tandem MOAC, Phosphoproteomics, 15N labeling

Wolfgang Hoehenwarter
contact affiliation	Proteome Analytics, Leibniz Institute of Plant Biochemistry
contact email	wolfgang.hoehenwarter@ipb-halle.de
lab head
Wolfgang Hoehenwarter
contact affiliation	Leibniz Institute of Plant Biochemistry
contact email	wolfgang.hoehenwarter@ipb-halle.de
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/2018/01/PXD008200

PRIDE project URI

• PRIDE
  1. PXD008200
     1. Label: PRIDE project
     2. Name: Combined 15N-Labelling and TandemMOAC Quantifies Phosphorylation of MAP Kinase Substrates Downstream of MKK7 in Arabidopsis