PXD034896

PXD034896 is an original dataset announced via ProteomeXchange.

Title	Proteomic analysis of S-acylated proteins in human retinal pigment epithelial cells reveals the role of palmitoylation of Niemann–Pick type C1 protein in cholesterol transportation
Description	Palmitoylation is a dynamic process which regulates the activity of the modified proteins. Retinal pigment epithelial (RPE) cells play pivotal roles in visual cycle and maintaining healthy photoreceptor cells. Dysfunctional RPE cells are often associated with degenerative retinal diseases. The aim of the study was to identify potentially palmitoylated proteins in human RPE cells. By using the detergent-resistant membrane, we found 312 potentially palmitoylated peptides which corresponded to 192 proteins in RPE cells, including 60 new candidate proteins which were not reported before. Gene enrichment analysis highlighted significant involvement of the palmitoylated proteins in lipid transporter activity and receptor-mediated endocytosis, among others. We further studied the effect of 3 potential palmitoylation sites (Cys 799, 900 and 816) of Niemann–Pick type C1 protein (NPC1) on cholesterol accumulation. We found that mutation of any single Cys alone had no significant effect on intracellular cholesterol accumulation while simultaneous mutation of Cys 799 and 800 caused significant cholesterol accumulation in late endosome. No further cholesterol accumulation was observed by adding another mutation at Cys 816. At the meantime, the mutated proteins were largely located at the endosome/lysosome. Conclusions: PRE cells have abundant number of palmitoylated proteins which are involved in cellular processes critical to visual function. The palmitoylation at Cys799 and 800 was needed for cholesterol transportation, but not the intracellular localization of NPC1.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_07:58:32.972.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Lei Zhou
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	palmitoylated residue
Instrument	TripleTOF 5600

Revision	Datetime	Status	ChangeLog Entry
0	2022-06-26 07:29:25	ID requested
1	2023-03-10 13:06:04	announced
⏵ 2	2023-11-14 07:58:33	announced	2023-11-14: Updated project metadata.

Li JK, Rao YQ, Koh SK, Zhao P, Zhou L, Li J, Proteomic analysis of s-acylated proteins in human retinal pigment epithelial cells and the role of palmitoylation of Niemann-Pick type C1 protein in cholesterol transport. Front Aging Neurosci, 14():965943(2022) [pubmed]

submitter keyword: Niemann-Pick type C1 protein,retinal pigment epithelial cells, palmitoylation

Lei ZHOU
contact affiliation	Singapore Eye Research Institute
contact email	zhou.lei@seri.com.sg
lab head
Lei Zhou
contact affiliation	Singapore Eye Research Institute
contact email	zhou.lei@seri.com.sg
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/2023/03/PXD034896

PRIDE project URI

• PRIDE
  1. PXD034896
     1. Label: PRIDE project
     2. Name: Proteomic analysis of S-acylated proteins in human retinal pigment epithelial cells reveals the role of palmitoylation of Niemann–Pick type C1 protein in cholesterol transportation