PXD001076

PXD001076 is an original dataset announced via ProteomeXchange.

Title	Quantitative phosphoproteomics of cytotoxic T cells to reveal Protein Kinase D 2 regulated networks
Description	The focus of the present study was to characterize the phosphoproteome of cytotoxic T cells and to explore the role of the serine threonine kinase PKD2 (Protein Kinase D2) in the phosphorylation networks of this key lymphocyte population. We used Stable Isotope Labelling of Amino acids in Culture (SILAC) combined with phosphopeptide enrichment and quantitative mass-spectrometry to determine the impact of PKD2 loss on the cytotoxic T cells phosphoproteome. We identified 15,871 phosphorylations on 3,505 proteins in cytotoxic T cells. 450 phosphosites on 281 proteins were down-regulated and 300 phosphosites on 196 proteins were up-regulated in PKD2 null cytotoxic T cells. These data give valuable new insights about the protein phosphorylation networks operational in effector T cells and reveal that PKD2 regulates directly and indirectly about 5% of the cytotoxic T cell phosphoproteome. PKD2 candidate substrates identified in this study include proteins involved in two distinct biological functions: regulation of protein sorting and intracellular vesicle trafficking, and control of chromatin structure, transcription and translation. In other cell types PKD substrates include class II histone deacetylases such as HDAC7 and actin regulatory proteins such as Slingshot. The current data show these are not PKD substrates in primary T cells revealing that the functional role of PKD isoforms is different in different cell lineages.
HostingRepository	PRIDE
AnnounceDate	2014-10-03
AnnouncementXML	Submission_2014-10-03_05:02:47.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Jens Hukelmann
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue; phosphorylated residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2014-06-23 01:04:44	ID requested
⏵ 1	2014-10-03 05:02:48	announced

Navarro MN, Goebel J, Hukelmann JL, Cantrell DA, Quantitative phosphoproteomics of cytotoxic T cells to reveal protein kinase d 2 regulated networks. Mol Cell Proteomics, 13(12):3544-57(2014) [pubmed]

curator keyword: Biological

submitter keyword: PKD2, SILAC, phosphoproteomics, lymphocytes

Doreen Ann Cantrell
contact affiliation	Division of Cell Signalling and Immunology, College of Life Sciences, University of Dundee, Dundee, UK
contact email	d.a.cantrell@dundee.ac.uk
lab head
Jens Hukelmann
contact affiliation	University of Dundee
contact email	jhukelmann@dundee.ac.uk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD001076
     1. Label: PRIDE project
     2. Name: Quantitative phosphoproteomics of cytotoxic T cells to reveal Protein Kinase D 2 regulated networks