PXD008398

PXD008398 is an original dataset announced via ProteomeXchange.

Title	S-acylated and S-palmitoylated proteins in HeLa
Description	S-fatty-acylation is the covalent attachment of long chain fatty acids, predominately palmitate (C16:0, S-palmitoylation), to cysteine (Cys) residues via a thioester linkage on proteins. This post-translational and reversible lipid modification regulates protein function and localization in eukaryotes and is important in mammalian physiology and human disease. While chemical labeling methods have improved the detection and enrichment of S-fatty-acylated proteins, mapping sites of modification and characterization of endogenously attached fatty acids is still challenging. here, we optimized and compared two methods widely employed to identify S-fatty-acylated proteins by MS-based proteomics. While these methods identified an overlapping list of fatty-acylated proteins, only alk-16 chemical reporter combined with NH2OH specifically and robustly identified S-fatty-acylated proteins. Alk-16 chemical reporter labeling alone gave a list of S/N/O-fatty acylated proteins, while acyl-RAC provided a list of S-acylated proteins. Acyl-RAC identifies any proteins with a thioester modification and is often misused in the literature to validate S-fatty-acylated proteins. It would be preferable, when validating new S-fatty-acylated proteins, to use acyl-RAC and alk-16 (+/-NH2OH) in combination.
HostingRepository	PRIDE
AnnounceDate	2018-03-28
AnnouncementXML	Submission_2018-03-27_23:57:08.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Emmanuelle Thinon
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	N-ethylmaleimide derivatized cysteine; monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2017-12-11 01:24:39	ID requested
⏵ 1	2018-03-27 23:57:09	announced

Thinon E, Fernandez JP, Molina H, Hang HC, Selective Enrichment and Direct Analysis of Protein S-Palmitoylation Sites. J Proteome Res, 17(5):1907-1922(2018) [pubmed]

curator keyword: Biological

submitter keyword: HeLa, LC-MS/MS, label free quatification, S-palmitoylation, S-acylation, fatty acylation, acyl-RAC, alk-16 chemical reporter

Howard C Hang
contact affiliation	Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065, USA
contact email	hhang@rockefeller.edu
lab head
Emmanuelle Thinon
contact affiliation	The Francis Crick Institute
contact email	emmanuellethinon@gmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD008398
     1. Label: PRIDE project
     2. Name: S-acylated and S-palmitoylated proteins in HeLa