Proteomics

Dataset Information

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Proteome-wide cellular thermal shift assay reveals novel crosstalk between brassinosteroid and auxin signaling


ABSTRACT: We demonstrated that bikinin changed the thermal stability of some of its target proteins as well as several known or putative interacting proteins of Arabidopsis GSK3s. By combining the thermal- and the phospho-proteomes of bikinin we uncovered the auxin carrier PIN-FORMED1 (PIN1) as a novel substrate of the Arabidopsis GSK3s. We showed that inhibition the kinase activity of GSK3s by brassinosteroids or the specific chemical inhibitor bikinin led to the loss of PIN1 polarity, revealing a novel crosstalk between brassinosteroid and auxin signaling. Hence, our study demonstrates the applicability of CETSA MS in plant intact cells for identification of small-molecule targets and for discovery of novel protein-protein interactions.

INSTRUMENT(S): Q Exactive

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

TISSUE(S): Cell Suspension Culture

SUBMITTER: Xiangyu Xu  

LAB HEAD: Ive DeSmet

PROVIDER: PXD029936 | Pride | 2022-03-08

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
E22632_C2_u_2p_PSB-254_1.raw Raw
E22634_C2_u_2p_PSB-254_2.raw Raw
E22636_C2_u_2p_PSB-254_3.raw Raw
E22640_C2_u_2p_PSB-254_5.raw Raw
E22642_C2_u_2p_PSB-254_6.raw Raw
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