Proteomics

Dataset Information

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Identification of putative phosphorylation substrates of BRI1 in response to brassinolide and sucrose

ABSTRACT: Plants respond to various external and internal stimuli by activating signal transduction pathways. The plasma membrane, acting as the cell boundary, provides a platform for various signaling components. These include cell surface receptor-like kinases, intrinsic transporters, membrane-anchored proteins, and cytosolic signaling components attached to the membrane from its cytosolic side. Phosphorylation is one of the most sensitive and essential post-translational modifications. To identify the sequential kinase-target relationships and understand the triggers for downstream regulatory complexes, we employed a phosphoproteomic approach. By subjecting plants to brassinolide and/or sucrose, we aim to identify the BR-BRI1 downstream substrates and investigate the possible impact of sucrose on this signaling pathway.

INSTRUMENT(S):

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell, Root

SUBMITTER: Lin Xi  

LAB HEAD: Waltraud Schulze

PROVIDER: PXD052599 | Pride | 2025-05-07

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
102_Col_0.raw Raw
106_Col_suc.raw Raw
110_Col_BL.raw Raw
126_bri1_0.raw Raw
127_bri1_0.raw Raw
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Publications

Receptor Kinase Signaling of BRI1 and SIRK1 Is Tightly Balanced by Their Interactomes as Revealed From Domain-Swap Chimaera in AE-MS Approaches.

Xi Lin L   Wu Xuna X   Wang Jiahui J   Zhang Zhaoxia Z   He Mingjie M   Zeeshan Zeeshan Z   Stefan Thorsten T   Schulze Waltraud X WX  

Molecular & cellular proteomics : MCP 20241015 11

At the plasma membrane, in response to biotic and abiotic cues, specific ligands initiate the formation of receptor kinase heterodimers, which regulate the activities of plasma membrane proteins and initiate signaling cascades to the nucleus. In this study, we utilized affinity enrichment mass spectrometry to investigate the stimulus-dependent interactomes of LRR receptor kinases in response to their respective ligands, with an emphasis on exploring structural influences and potential cross-talk  ...[more]

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