PXD044354

PXD044354 is an original dataset announced via ProteomeXchange.

Title	Receptor kinase signalling of BRI1 and SIRK1 is tightly balanced by their interactomes as revealed from domain-swap chimaera in AE-MS approaches.
Description	Plants response to different external and internal stimulation by activation of signal transduction pathways. Receptor kinases are localized at plasma membrane and were characterized to be involved in perception of signals at the cell surface. Here we use affinity enrichment mass spectrometry acquisition (AE-MS) of the LRR receptor kinases BRI1 and SIRK1 to study the stimulus-dependent interactomes in response to brassinolide and/or sucrose. Our results reveal the different recruitment ability of BRI1 and SIRK1 under BL and sucrose treatment. Specifically, BRI1 and SIRK1 are involved in fine-tuning the readiness of the plant to respond to the internal balance of the phytohormone branssinolide and sucrose levels. By using domain-swap chimera, we attribute structural features of the receptors to the interaction with their co-receptors, signaling transduction proteins or substrate transporters. Although SIRK1 and BRI1 regulates cell expansion through different mechanisms, the chimeras could compliment both sirk1 and bri1 phenotype, but not the double mutant. We proposed this mechanism is associated with recruited interactors at the plasma membrane. Our work reveals a tightly controlled balance of signaling cascade activation dependent on the internal status of the plant.
HostingRepository	PRIDE
AnnounceDate	2025-05-06
AnnouncementXML	Submission_2025-05-06_12:02:22.076.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Lin Xi
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2023-08-04 07:23:58	ID requested
⏵ 1	2025-05-06 12:02:22	announced

Xi L, Wu X, Wang J, Zhang Z, He M, Zeeshan Z, Stefan T, Schulze WX, Receptor Kinase Signaling of BRI1 and SIRK1 Is Tightly Balanced by Their Interactomes as Revealed From Domain-Swap Chimaera in AE-MS Approaches. Mol Cell Proteomics, 23(11):100857(2024) [pubmed]

10.1016/j.mcpro.2024.100857;

submitter keyword: LRR-receptor kinase, supervised machine learning, signaling specificity, affinity enrichment mass-spectrometry (AE-MS), domain-swap chimera

Waltraud Schulze
contact affiliation	Department of Plant Systems Biology, University of Hohenheim, 70599 Stuttgart, Germany
contact email	wschulze@uni-hohenheim.de
lab head
Lin Xi
contact affiliation	University of Hohenheim
contact email	lin.xi.260@uni-hohenheim.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD044354
     1. Label: PRIDE project
     2. Name: Receptor kinase signalling of BRI1 and SIRK1 is tightly balanced by their interactomes as revealed from domain-swap chimaera in AE-MS approaches.