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 Bioljournal_title
Nature cell biologyauthors
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 ZYdoi
10.1038/ncb2151subject
Has Abstractpub_date
2011-02-01 00:00:00pages
124-31issue
2eissn
1465-7392issn
1476-4679pii
ncb2151journal_volume
13pub_type
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