PXD009143

PXD009143 is an original dataset announced via ProteomeXchange.

Title	Proteomic Analysis and Functional Characterization of P4-ATPase Phospholipid Flippases from Murine Tissues
Description	P4-ATPases are a subfamily of P-type ATPases that flip phospholipids across membranes to generate lipid asymmetry, a property vital to many cellular processes. Mutations in several P4-ATPases have been linked to severe neurodegenerative and metabolic disorders. Most P4-ATPases associate with one of three accessory subunit isoforms known as CDC50A (TMEM30A), CDC50B (TMEM30B), and CDC50C(TMEM30C). To identify P4-ATPases that associate with CDC50A, in vivo, and determine their tissue distribution, we isolated P4-ATPases-CDC50A complexes from retina, brain, liver, testes, and kidney on a CDC50A immunoaffinity column and identified and quantified P4-ATPases from their tryptic peptides by mass spectrometry. Of the 12 P4-ATPase that associate with CDC50 subunits, 10 P4-ATPases were detected. Four P4-ATPases (ATP8A1, ATP11A, ATP11B, ATP11C) were present in all five tissues. ATP10D was found in low amounts in liver, brain, testes, and kidney, and ATP8A2 was present in significant amounts in retina, brain, and testes. ATP8B1 was detected only in liver, ATP8B3 and ATP10A only in testes, and ATP8B2 primarily in brain. We also show that ATP11A, ATP11B and ATP11C, like ATP8A1 and ATP8A2, selectively flip phosphatidylserine and phosphatidylethanolamine across membranes. These studies provide insight into the distribution, relative abundance, subunit interactions and substrate specificity of P4-ATPase-CDC50 complexes.
HostingRepository	PRIDE
AnnounceDate	2018-07-20
AnnouncementXML	Submission_2018-07-20_02:53:33.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Jenny Moon
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	No PTMs are included in the dataset
Instrument	impact II

Revision	Datetime	Status	ChangeLog Entry
0	2018-03-08 03:36:42	ID requested
⏵ 1	2018-07-20 02:53:35	announced

Wang J, Molday LL, Hii T, Coleman JA, Wen T, Andersen JP, Molday RS, Proteomic Analysis and Functional Characterization of P4-ATPase Phospholipid Flippases from Murine Tissues. Sci Rep, 8(1):10795(2018) [pubmed]

curator keyword: Biological

submitter keyword: LC-MS/MS, P4-ATPases, Phospholipid flippases, CDC50A, TMEM30A, affinity chromatography, mouse tissues

Robert S. Molday
contact affiliation	Professor, Biochemistry and Molecular Biology, University of British Columbia, UBC
contact email	molday@mail.ubc.ca
lab head
Jenny Moon
contact affiliation	University of British Columbia
contact email	kyungmee@mail.ubc.ca
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/2018/07/PXD009143

PRIDE project URI

• PRIDE
  1. PXD009143
     1. Label: PRIDE project
     2. Name: Proteomic Analysis and Functional Characterization of P4-ATPase Phospholipid Flippases from Murine Tissues