PXD038010

PXD038010 is an original dataset announced via ProteomeXchange.

Title	Global profiling identifies a stress-responsive tyrosine site on EDC3 regulating biomolecular condensate formation
Description	RNA granules are cytoplasmic condensates that organize biochemical and signaling complexes in response to cellular stress. Functional proteomic investigations under RNA granule-inducing conditions are needed to identify protein sites involved in coupling stress response with ribonucleoprotein regulation. Here, we apply chemical proteomics using sulfonyl-triazole (SuTEx) probes to capture cellular responses to oxidative and nutrient stress. The stress responsive tyrosine and lysine sites detected mapped to known proteins involved in processing body (PB) and stress granule (SG) pathways, including LSM14A, FUS, and EDC3. Notably, disruption of EDC3 tyrosine 475 (Y475) resulted in hypo-phosphorylation at S161 and S131, and altered protein-protein interactions (PPI) with decapping complex components (DDX6, DCP1A/B) and 14-3-3 proteins. This resulting mutant form of EDC3 was capable of rescuing the PB-deficient phenotype of EDC3 knockout cells. Taken together, our findings identify Y475 as an arsenic-responsive site that regulates RNA granule formation by coupling EDC3 post-translational modification and PPI states.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_09:06:15.752.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD038010
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Dina Bai
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2022-11-07 09:55:55	ID requested
1	2023-10-23 08:54:16	announced
⏵ 2	2023-11-14 09:06:24	announced	2023-11-14: Updated project metadata.

10.6019/PXD038010;

Ciancone AM, Hosseinibarkooie S, Bai DL, Borne AL, Ferris HA, Hsu KL, Global profiling identifies a stress-responsive tyrosine site on EDC3 regulating biomolecular condensate formation. Cell Chem Biol, 29(12):1709-1720.e7(2022) [pubmed]

submitter keyword: LC-MSMS, stress granules, LLPS, SuTEx, P-bodies, stress, chemoproteomics, RNA granule, condensate, tyrosine,EDC3

Ku-Lung (Ken) Hsu
contact affiliation	Department of Chemistry University of Virginia
contact email	kh4ch@virginia.edu
lab head
Dina Bai
contact affiliation	University of Virginia
contact email	dlb6z@virginia.edu
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/2023/10/PXD038010

PRIDE project URI

• PRIDE
  1. PXD038010
     1. Label: PRIDE project
     2. Name: Global profiling identifies a stress-responsive tyrosine site on EDC3 regulating biomolecular condensate formation