PXD002266

PXD002266 is an original dataset announced via ProteomeXchange.

Title	Phosphoproteomics reveals malaria parasite Protein Kinase G as a signalling hub regulating egress and invasion
Description	Our understanding of the key phosphorylation-dependent signalling pathways in the human malaria parasite, Plasmodium falciparum, remains rudimentary. Here we address this issue for the essential cGMP-dependent protein kinase, PfPKG. By employing chemical and genetic tools in combination with quantitative global phosphoproteomics, we identify the phosphorylation sites on 69 proteins that are direct or indirect cellular targets for PfPKG. These PfPKG targets include proteins involved in cell signalling, proteolysis, gene regulation, protein export and ion and protein transport, indicating that cGMP/PfPKG acts as a signalling hub that plays a central role in a number of core parasite processes. We also show that PfPKG activity is required for parasite invasion. This correlates with the finding that the calcium-dependent protein kinase, PfCDPK1, is phosphorylated by PfPKG, as are components of the actomyosin complex, providing mechanistic insight into the essential role of PfPKG in parasite egress and invasion.
HostingRepository	PRIDE
AnnounceDate	2017-09-22
AnnouncementXML	Submission_2017-09-22_02:52:53.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD002266
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Andrew Bottrill
SpeciesList	scientific name: Plasmodium falciparum; NCBI TaxID: 5833;
ModificationList	Phospho; TMT6plex; Oxidation; Carbamidomethyl
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2015-05-29 09:28:28	ID requested
⏵ 1	2017-09-22 02:52:55	announced

Alam MM, Solyakov L, Bottrill AR, Flueck C, Siddiqui FA, Singh S, Mistry S, Viskaduraki M, Lee K, Hopp CS, Chitnis CE, Doerig C, Moon RW, Green JL, Holder AA, Baker DA, Tobin AB, Phosphoproteomics reveals malaria parasite Protein Kinase G as a signalling hub regulating egress and invasion. Nat Commun, 6():7285(2015) [pubmed]

curator keyword: Biological, Biomedical

submitter keyword: Malaria, Parasite, Protein Kinase G, phosphorylation, invasion, signalling, quantitation, tandem mass tags

Professor Andrew B. Tobin
contact affiliation	MRC Toxicology Unit, University of Leicester, Hodgkin Building, Lancaster Road, Leicester, LE1 9HN, UK
contact email	tba@le.ac.uk
lab head
Andrew Bottrill
contact affiliation	University of Leicester
contact email	arb29@le.ac.uk
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/2017/09/PXD002266

PRIDE project URI

• PRIDE
  1. PXD002266
     1. Label: PRIDE project
     2. Name: Phosphoproteomics reveals malaria parasite Protein Kinase G as a signalling hub regulating egress and invasion