PXD051411

PXD051411 is an original dataset announced via ProteomeXchange.

Title	Kinase-catalyzed Biotinylation for Discovery and Validation of Substrates to Multi-specificity Kinases NME1 and NME2
Description	Protein phosphorylation by kinases regulates mammalian cell functions, such as growth, division, and signal transduction. Among human kinases, NME1 and NME2 are associated with metastatic tumor suppression, but remain understudied due to the lack of tools to monitor their cellular substrates. In particular, NME1 and NME2 are multi-specificity kinases phosphorylating serine, threonine, histidine, and aspartic acid residues of substrates, and the heat and acid sensitivity of phosphohistidine and phosphoaspartate complicates substrate discovery and validation. To provide new substrate monitoring tools, we established the γ-phosphate modified ATP analog, ATP-biotin, as a cosubstrate for phosphorylbiotinylation of NME1 and NME2 cellular substrates. Building upon this ATP-biotin compatibility, the Kinase-catalyzed Biotinylation with Inactivated Lysates for Discovery of Substrates (K-BILDS) method enabled validation of a known substrate and the discovery of seven NME1 and three NME2 substrates. Given the paucity of methods to study kinase substrates, ATP-biotin and the K-BILDS method are valuable tools to characterize the roles of NME1 and NME2 in human cell biology.
HostingRepository	PRIDE
AnnounceDate	2024-10-17
AnnouncementXML	Submission_2024-10-17_05:10:18.654.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD051411
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Eric Davis
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2024-04-12 15:29:50	ID requested
⏵ 1	2024-10-17 05:10:19	announced

10.6019/PXD051411;

Gary CR, Acharige NPN, Oyewumi TO, Pflum MKH, Kinase-catalyzed biotinylation for discovery and validation of substrates to multispecificity kinases NME1 and NME2. J Biol Chem, 300(8):107588(2024) [pubmed]

10.1016/j.jbc.2024.107588;

submitter keyword: proteomics, histidine kinase, phosphorylation, NME, substrate specificity, ATP-biotin,protein kinase

Mary K Pflum
contact affiliation	Wayne State Chemistry
contact email	pflum@wayne.edu
lab head
Eric Davis
contact affiliation	Wayne State University
contact email	gm9453@wayne.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/2024/10/PXD051411

PRIDE project URI

• PRIDE
  1. PXD051411
     1. Label: PRIDE project
     2. Name: Kinase-catalyzed Biotinylation for Discovery and Validation of Substrates to Multi-specificity Kinases NME1 and NME2