PXD012906

PXD012906 is an original dataset announced via ProteomeXchange.

Title	Identification of PKC-alpha dependent phosphoproteins in mouse retina
Description	Adjusting to a wide range of light intensities is an essential feature of retinal rod bipolar cell (RBC) function, and persuasive evidence suggests this modulation involves phosphorylation by protein kinase C-alpha (PKC-alpha). PKC-alpha is a serine/threonine kinase that is strongly expressed in RBCs, but the targets of PKC-alpha phosphorylation in the retina have not been identified. PKC-alpha activity and phosphorylation in RBCs was examined by immunofluorescence confocal microscopy using a conformation-specific PKC-alpha antibody and antibodies to phosphorylated PKC motifs. PKC-alpha activity was dependent on light and expression of TRPM1, and RBC dendrites were the primary sites of light-dependent phosphorylation. PKC-alpha-dependent retinal phosphoproteins were identified using a multiplexed tandem mass tag-based approach to compare total protein and phosphopeptide abundance between phorbol ester-treated wild type and PKC-alpha knockout (PKC-alpha-KO) mouse retinas. Of the 23 proteins showing significant differential abundance between the two groups, most have roles in cytoskeleton/transport, transcriptional regulation, or metabolism/homeostasis. Phosphopeptide mass spectrometry identified over 1100 phosphopeptides in mouse retina, with 12 displaying significantly greater phosphorylation in WT compared to PKC-alpha-KO samples. The differentially phosphorylated proteins fall into the following functional groups: cytoskeleton/transport (4 proteins), ECM/adhesion (2 proteins), signaling (2 proteins), transcriptional regulation (3 proteins), and homeostasis/metabolism (1 protein). Two strongly differentially expressed phosphoproteins, BORG4 and TPBG, were localized to the synaptic layers of the retina, and may play a role in PKC-alpha-dependent modulation of RBC physiology.
HostingRepository	PRIDE
AnnounceDate	2019-07-15
AnnouncementXML	Submission_2019-07-15_01:35:00.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Phillip Wilmarth
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	TMT6plex-126 reporter+balance reagent acylated residue; phosphorylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion ETD

Revision	Datetime	Status	ChangeLog Entry
0	2019-02-28 01:48:03	ID requested
⏵ 1	2019-07-15 01:35:01	announced

Wakeham CM, Wilmarth PA, Cunliffe JM, Klimek JE, Ren G, David LL, Morgans CW, -dependent phosphoproteins in mouse retina. J Proteomics, 206():103423(2019) [pubmed]

submitter keyword: mouse, retina, signaling, protein kinase C-alpha, quantitative proteomics, isobaric labeling

Dr. Catherine Morgans
contact affiliation	Department of Physiology & Pharmacology Oregon Health & Science University 3181 SW Sam Jackson Park Road Portland, Oregon 97239, USA
contact email	morgansc@ohsu.edu
lab head
Phillip Wilmarth
contact affiliation	OHSU
contact email	wilmarth@ohsu.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD012906
     1. Label: PRIDE project
     2. Name: Identification of PKC-alpha dependent phosphoproteins in mouse retina