Methylation of a phosphatase specifies dephosphorylation and degradation of activated brassinosteroid receptors.

@article{Wu2011MethylationOA,
  title={Methylation of a phosphatase specifies dephosphorylation and degradation of activated brassinosteroid receptors.},
  author={Guang Shao Wu and Xiuling Wang and Xianbin Li and Yuji Kamiya and Marisa S Otegui and Joanne Chory},
  journal={Science signaling},
  year={2011},
  volume={4 172},
  pages={ra29}
}
Internalization of cell surface receptors, followed by either recycling back to the plasma membrane or degradation, is crucial for receptor homeostasis and signaling. The plant brassinosteroid (BR) receptor, BRASSINOSTEROID INSENSITIVE 1 (BRI1), undergoes constitutive cycling between the plasma membrane and the internal membranes. We show that protein phosphatase 2A (PP2A) dephosphorylated BRI1 and that Arabidopsis thaliana rcn1, a mutant for a PP2A subunit, caused an increase in BRI1 abundance… CONTINUE READING
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