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PXD046322

PXD046322 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleLipid exchange at ER-trans Golgi contact sites governs polarized cargo sorting
DescriptionOxysterol Binding Protein (OSBP) extracts cholesterol from the ER to deliver it to the TGN via the counter exchange and subsequent hydrolysis of the phosphoinositide PI(4)P. Here, we show that this pathway is essential in polarized epithelial cells where it contributes not only to the proper subcellular distribution of cholesterol, but also to the trans-Golgi sorting and trafficking of numerous plasma membrane cargo proteins with apical or basolateral localization. Reducing the expression of OSBP, blocking its activity or inhibiting a PI4Kinase that fuels OSBP with PI(4)P abolishes the epithelial phenotype. Waves of cargo enrichment in the TGN in phase with OSBP and PI(4)P dynamics suggest that OSBP promotes the formation of lipid gradients along the TGN, which help cargo sorting. During their transient passage through the trans-Golgi, polarized plasma membrane proteins get close to OSBP, but fail to be sorted when OSBP is silenced. Thus, OSBP lipid exchange activity is decisive for polarized cargo sorting and distribution in epithelial cells.
HostingRepositoryPRIDE
AnnounceDate2023-11-20
AnnouncementXMLSubmission_2023-11-20_08:51:01.885.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD046322
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterDavid Kovacs
SpeciesList scientific name: Canis familiaris (Dog) (Canis lupus familiaris); NCBI TaxID: 9615;
ModificationListacetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
InstrumentOrbitrap Exploris 480
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-10-23 06:48:25ID requested
12023-11-20 08:51:02announced
Publication List
10.1083/JCB.202307051;
10.6019/PXD046322;
Keyword List
submitter keyword: proximity proteomic,OSBP, surface proteomic
Contact List
Anne-Sophie Gay
contact affiliationIPMC/CNRS
contact emailgay@ipmc.cnrs.fr
lab head
David Kovacs
contact affiliationIPMC CNRS
contact emailkovacs@ipmc.cnrs.fr
dataset submitter
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Dataset FTP location
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