PXD012906 is an
original dataset announced via ProteomeXchange.
Dataset Summary
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 |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-02-28 01:48:03 | ID requested | |
⏵ 1 | 2019-07-15 01:35:01 | announced | |
2 | 2024-10-22 04:40:10 | announced | 2024-10-22: Updated project metadata. |
Publication List
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] |
Keyword List
submitter keyword: mouse, retina, signaling, protein kinase C-alpha, quantitative proteomics, isobaric labeling |
Contact List
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 | |
Full Dataset Link List
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/2019/07/PXD012906 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD012906
- Label: PRIDE project
- Name: Identification of PKC-alpha dependent phosphoproteins in mouse retina