PP2A activates brassinosteroid-responsive gene expression and plant growth by dephosphorylating BZR1.

Abstract:

:When brassinosteroid levels are low, the GSK3-like kinase BIN2 phosphorylates and inactivates the BZR1 transcription factor to inhibit growth in plants. Brassinosteroid promotes growth by inducing dephosphorylation of BZR1, but the phosphatase that dephosphorylates BZR1 has remained unknown. Here, using tandem affinity purification, we identified protein phosphatase 2A (PP2A) as a BZR1-interacting protein. Genetic analyses demonstrated a positive role for PP2A in brassinosteroid signalling and BZR1 dephosphorylation. Members of the B' regulatory subunits of PP2A directly interact with BZR1's putative PEST domain containing the site of the bzr1-1D mutation. Interaction with and dephosphorylation by PP2A are enhanced by the bzr1-1D mutation, reduced by two intragenic bzr1-1D suppressor mutations, and abolished by deletion of the PEST domain. This study reveals a crucial function for PP2A in dephosphorylating and activating BZR1 and completes the set of core components of the brassinosteroid-signalling cascade from cell surface receptor kinase to gene regulation in the nucleus.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

Tang W,Yuan M,Wang R,Yang Y,Wang C,Oses-Prieto JA,Kim TW,Zhou HW,Deng Z,Gampala SS,Gendron JM,Jonassen EM,Lillo C,DeLong A,Burlingame AL,Sun Y,Wang ZY

doi

10.1038/ncb2151

subject

Has Abstract

pub_date

2011-02-01 00:00:00

pages

124-31

issue

2

eissn

1465-7392

issn

1476-4679

pii

ncb2151

journal_volume

13

pub_type

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