PXD007878

PXD007878 is an original dataset announced via ProteomeXchange.

Title	Large-Scale Characterization of Phosphorylation-Induced Conformational and Stability Changes in Breast Cancer
Description	Large-scale studies of protein phosphorylation have generally focused on determining the sites and stoichiometry of phosphorylated proteins derived from different biological specimens such as cell lines and tissue samples. While such information is important for understanding the role of phosphorylation in biological systems, it fails to expose the relationship between protein phosphorylation and protein function. Because of the close link between protein function and protein folding stability, knowledge about phosphorylation-induced protein folding stability changes can lead to a better understanding of the functional effects of protein phosphorylation. As part of this work, the Stability of Proteins from Rate of OXidation (SPROX) and Limited Proteolysis (LiP) techniques were utilized to identify phosphorylation-induced conformational and stability changes in proteins derived from a human breast cancer cell line MCF-7. This was accomplished by comparing the conformation properties of proteins in two MCF-7 cell lysates including one that was and one that was not dephosphorylated with alkaline phosphatase. The SPROX technique, which probes the global unfolding/refolding properties of proteins, identified 168 proteins with phosphorylation-induced stability changes, and the LiPs technique, which probes the more local unfolding/refolding properties of proteins, identified 251 proteins with phosphorylation-induced stability changes. A total of 49 proteins identified here with phosphorylation-induced conformational changes, were previously identified in phosphoproteomic studies to be differentially phosphorlyated in different human breast cancer subtypes. A total of 98 proteins identified here overlapped with protein hits previously found to be differentially stabilized in four human breast cancer phenotypes, suggesting that the phosphorylated changes observed here may be disease related. The experimental approach and results reported here create a novel perspective in understanding large-scale molecular influence of phosphorylation and a shortcut in finding possible functionally significant PTMs in cellular proteins.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:41:06.138.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	He Meng
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	methylthiolated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2017-09-29 05:53:54	ID requested
1	2019-11-12 09:53:39	announced
⏵ 2	2024-10-22 04:41:10	announced	2024-10-22: Updated project metadata.

10.1021/acs.jproteome.7b00795;

Meng H, Fitzgerald MC, Proteome-Wide Characterization of Phosphorylation-Induced Conformational Changes in Breast Cancer. J Proteome Res, 17(3):1129-1137(2018) [pubmed]

ProteomeXchange project tag: Cancer (B/D-HPP), Biology/Disease-Driven Human Proteome Project (B/D-HPP), Human Proteome Project

curator keyword: Biological, Biomedical

submitter keyword: protein stability, phosphorylation,Human breast cancer, protein conformation

Michael C. Fitzgerald
contact affiliation	Professor, Chemistry, Duke University
contact email	michael.c.fitzgerald@duke.edu
lab head
He Meng
contact affiliation	Duke University
contact email	he.meng@duke.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/2019/11/PXD007878

PRIDE project URI

• PRIDE
  1. PXD007878
     1. Label: PRIDE project
     2. Name: Large-Scale Characterization of Phosphorylation-Induced Conformational and Stability Changes in Breast Cancer