PXD011525

PXD011525 is an original dataset announced via ProteomeXchange.

Title	Global redox proteome and phosphoproteome analysis reveals novel mode of Akt regulation
Description	A major knowledge gap in cell signalling is defining the crosstalk between multiple types of post-translational modification (PTM). Here, we take a multi-omic approach (redox proteome, phosphoproteome and total proteome) to delineate signalling networks in adipocytes modulated by reactive oxygen species (ROS) and protein phosphorylation. Our integrative analysis of these datasets revealed widespread and complex crosstalk between oxidative stress-induced cysteine oxidation and phosphorylation-based signalling. In particular, we demonstrate dysregulation in the kinase substrate relationships of Akt, mTOR and AMPK. Furthermore, we identify that Cys60 and Cys77 in the pleckstrin homology (PH) domain of Akt are required for its recruitment to the plasma membrane, its subsequent activation, and its regulation by redox. These multi-omics datasets provide insight into how redox signalling driven by oxidative stress interacts with protein phosphorylation and should serve as a useful resource for dissecting oxidative stress-induced PTMs and understanding their contribution to a variety of diseases.
HostingRepository	PRIDE
AnnounceDate	2019-12-11
AnnouncementXML	Submission_2019-12-11_04:20:45.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Zhiduan Su
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	TMT6plex-126 reporter+balance reagent acylated residue; phosphorylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2018-10-30 03:57:15	ID requested
⏵ 1	2019-12-11 04:20:46	announced

Su Z, Burchfield JG, Yang P, Humphrey SJ, Yang G, Francis D, Yasmin S, Shin SY, Norris DM, Kearney AL, Astore MA, Scavuzzo J, Fisher-Wellman KH, Wang QP, Parker BL, Neely GG, Vafaee F, Chiu J, Yeo R, Hogg PJ, Fazakerley DJ, Nguyen LK, Kuyucak S, James DE, Global redox proteome and phosphoproteome analysis reveals redox switch in Akt. Nat Commun, 10(1):5486(2019) [pubmed]

curator keyword: Biological

submitter keyword: redox proteome, phosphoproteome, crosstalk, Akt

David E. James
contact affiliation	Leonard P Ullmann Chair in Metabolic Systems Biology, The Charles Perkins Centre School of Life and Environmental Sciences and Sydney Medical School D17 - Charles Perkins Centre | The University of Sydney | NSW | 2006
contact email	david.james@sydney.edu.au
lab head
Zhiduan Su
contact affiliation	The University of Sydney
contact email	zhiduan.su@sydney.edu.au
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/2019/12/PXD011525

PRIDE project URI

• PRIDE
  1. PXD011525
     1. Label: PRIDE project
     2. Name: Global redox proteome and phosphoproteome analysis reveals novel mode of Akt regulation