Proteomics

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Affinity purification of Flag-tagged BSU1 fragments expressed in Arabidopsis thaliana bri1-5 seedlings


ABSTRACT: The immunoprecipitation followed by mass-spectrometry (AP-MS) experiment was performed as follows. The N-terminal Kelch domain, the C-terminal phosphatase domain or a catalytically inactive version of the C-terminal phosphatase domain of the Kelch phosphatase BSU1 from Arabidopsis thaliana were constitutively expressed with a C-terminal Flag tag in the Arabidopsis thaliana bri1-5 brassinosteroid signaling mutants. AP-MS experiments were performed at seedling stage.

INSTRUMENT(S):

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

TISSUE(S): Plant Cell, Whole Body

SUBMITTER: Michael Hothorn  

LAB HEAD: Michael Hothorn

PROVIDER: PXD072713 | Pride | 2026-05-22

REPOSITORIES: Pride

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Publications

Plant Kelch phosphatases are Ser/Thr phosphatases involved in cell cycle regulation.

Rico-Resendiz Felix F   Pri-Tal Oded O   Raia Pierre P   Moretti Andrea A   Chen Houming H   Yu Jun J   Broger Larissa L   Fuchs Christelle C   Hothorn Ludwig A LA   Loubéry Sylvain S   Hothorn Michael M  

Proceedings of the National Academy of Sciences of the United States of America 20260520 21


Brassinosteroids (BRs) are plant steroid hormones sensed by the membrane receptor kinase BRI1. Activation of BRI1 leads to the dephosphorylation of BZR1/BES1 transcription factors. Overexpression of the Kelch phosphatase BRI1 SUPPRESSOR 1 (BSU1) rescued the growth defects of <i>bri1</i> mutants. Subsequent studies identified BSU1 as a protein tyrosine phosphatase, which promotes BR signaling by dephosphorylating a phosphotyrosine in the glycogen synthase kinase 3 BIN2. Crystal structures of the  ...[more]

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