PXD015307

PXD015307 is an original dataset announced via ProteomeXchange.

Title	Quantitative profiling of protein sulfhydrome by the BTA-TMT
Description	The redox-based modification of cysteine residues in proteins regulates their function in many biological processes. The gas molecule H2S has been shown to sulfhydrate redox sensitive cysteine residues resulting in an H2S-modified proteome known as the sulfhydrome. Tandem Mass Tags (TMT) multiplexing strategies for large-scale proteomic analyses have become increasingly prevalent. Here we developed TMT-based proteomics approach for selectively trapping and tagging cysteine persulfides in the cellular proteomes. With this approach, we revealed the natural protein sulfhydrome of two human cell lines, and identified insulin as novel sulfhydration substrate in pancreatic beta cells. Moreover, we identified metabolic pathways selectively being targets for H2S. Using this approach, we found that the enzymes involved in cellular energy pathway are primarily subjected to a Redox Thiol Switch (RTS), which is a switch of one modification to another on the same cysteine residue. We further showed that protein S-glutathioinylation, a specific reversible thiol modification in cysteine residues under oxidative stress conditions, which can be switched to S-sulfhydration. We propose that a RTSGS from S-glutathioinylation to S-sulfhydration is a key mechanism to fine tune cellular energy metabolism in response to different levels of oxidative stress.
HostingRepository	PRIDE
AnnounceDate	2020-03-09
AnnouncementXML	Submission_2020-03-09_00:48:22.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Ling Li
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; scientific name: Rattus norvegicus (Rat); NCBI TaxID: 10116; scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue
Instrument	Orbitrap Fusion Lumos; LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2019-09-04 01:16:14	ID requested
⏵ 1	2020-03-09 00:48:24	announced

Gao XH, Li L, Parisien M, Wu J, Bederman I, Gao Z, Krokowski D, Chirieleison SM, Abbott D, Wang B, Arvan P, Cameron M, Chance M, Willard B, Hatzoglou M, Discovery of a Redox Thiol Switch: Implications for Cellular Energy Metabolism. Mol Cell Proteomics, 19(5):852-870(2020) [pubmed]

submitter keyword: Cysteine sulfhydration, TMT,

Belinda Willard
contact affiliation	Proteomics and Metabolomics Core, Cleveland Clinic
contact email	willarb@ccf.org
lab head
Ling Li
contact affiliation	Cleveland Clinic
contact email	lil5@ccf.org
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/2020/03/PXD015307

PRIDE project URI

• PRIDE
  1. PXD015307
     1. Label: PRIDE project
     2. Name: Quantitative profiling of protein sulfhydrome by the BTA-TMT