PXD073760

PXD073760 is an original dataset announced via ProteomeXchange.

Title	Affinity-Based Interactome Mapping of Inositol Pyrophosphates Reveals 4/6-PP-InsP5-–Binding Proteins in Plants
Description	Inositol pyrophosphates (PP-InsPs) are central regulators of eukaryotic signaling events. While certain PP-InsP isomers have been conclusively linked to the regulation of phosphate homeostasis through interaction with SPX domain containing proteins in plants, the functions of the recently discovered isomer 4/6-PP-InsP5 remain largely unknown. Here, we employed two complementary affinity-based strategies – a matrix approach and a photoaffinity probe – to systematically identify 4/6-PP-InsP5-binding proteins in Arabidopsis thaliana. The two methods yielded partially overlapping protein sets, with photoaffinity enrichment likely capturing additional transient and/or weak interactions. Moreover, competition experiments with different isomers were applied to obtain information about potential isomer-specific interactions. As a proof-of-concept, one candidate interactor (FHA domain-containing protein AtFHA2) was shown to bind 4-PP-InsP5 in vitro with markedly higher affinity than InsP6, while no reliable binding parameters could be obtained for its the enantiomeric isomer 6-PP-InsP5. Thus, besides the SPX domain, FHA domain containing proteins, of which 18 exist in Arabidopsis, are potentially regulated by inositol pyrophosphates. More generally, our findings reveal a diverse protein network associated with 4/6-PP-InsP5 and establish a versatile platform for dissecting its biological roles in plants and other organisms.
HostingRepository	PRIDE
AnnounceDate	2026-06-08
AnnouncementXML	Submission_2026-06-07_16:09:22.182.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Sara Christina Stolze
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: NEWT:3702;
ModificationList	No PTMs are included in the dataset
Instrument	Orbitrap Exploris 480; Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2026-01-29 02:52:47	ID requested
⏵ 1	2026-06-07 16:09:22	announced

Ritter K, Gaugler V, Stolze SC, Ghosh R, Jayamon A, Yadav R, Wollensack F, Laha D, Nakagami H, Schaaf G, Jessen HJ, -Binding Proteins in Plants. Adv Sci (Weinh), 13(26):e24290(2026) [pubmed]

10.1002/advs.202524290;

submitter keyword: Inositol pyrophosphates, plants, phosphate homeostasis

Hirofumi Nakagami
contact affiliation	Basic Immune System of Plants / Protein Mass Spectrometry Max Planck Institute for Plant Breeding Research Carl-von-Linne-Weg 10, 50829 Cologne, Germany
contact email	nakagami@mpipz.mpg.de
lab head
Sara Christina Stolze
contact affiliation	Plant Proteomics and Mass Spectrometry Group Max Planck Institute for Plant Breeding Research Carl-von-Linné Weg 10 50829 Cologne
contact email	stolze@mpipz.mpg.de
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/2026/06/PXD073760

PRIDE project URI

• PRIDE
  1. PXD073760
     1. Label: PRIDE project
     2. Name: Affinity-Based Interactome Mapping of Inositol Pyrophosphates Reveals 4/6-PP-InsP5-–Binding Proteins in Plants