Proteome-wide cellular thermal shift assay reveals unexpected cross-talk between brassinosteroid and auxin signaling.
Qing LuYonghong ZhangJoakim HellnerCaterina GianniniXiangyu XuJarne PauwelsQian MaWim DejongheHuibin HanBrigitte van de CotteFrancis ImpensKris GevaertIve De SmetJiří FrimlDaniel Martinez MolinaEugenia RussinovaPublished in: Proceedings of the National Academy of Sciences of the United States of America (2022)
SignificanceChemical genetics, which investigates biological processes using small molecules, is gaining interest in plant research. However, a major challenge is to uncover the mode of action of the small molecules. Here, we applied the cellular thermal shift assay coupled with mass spectrometry (CETSA MS) to intact Arabidopsis cells and showed that bikinin, the plant-specific glycogen synthase kinase 3 (GSK3) inhibitor, changed the thermal stability of some of its direct targets and putative GSK3-interacting proteins. In combination with phosphoproteomics, we also revealed that GSK3s phosphorylated the auxin carrier PIN-FORMED1 and regulated its polarity that is required for the vascular patterning in the leaf.
Keyphrases
- mass spectrometry
- pi k akt
- signaling pathway
- cell cycle arrest
- induced apoptosis
- transcription factor
- high throughput
- liquid chromatography
- cell wall
- protein kinase
- multiple sclerosis
- high resolution
- arabidopsis thaliana
- ms ms
- gas chromatography
- endoplasmic reticulum stress
- capillary electrophoresis
- cell death
- tandem mass spectrometry