期刊
NATURE CELL BIOLOGY
卷 13, 期 2, 页码 124-U49出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb2151
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- Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the US Department of Energy [DE-FG02-08ER15973]
- NIH [R01GM066258]
- National Science Foundation of China [30870213, 90917008]
- NSF [IOS-0724688, IOS-0846282]
- Herman Frasch Foundation
- China Scholarship Council
- U.S. Department of Energy (DOE) [DE-FG02-08ER15973] Funding Source: U.S. Department of Energy (DOE)
- Direct For Biological Sciences
- Division Of Integrative Organismal Systems [0846282] Funding Source: National Science Foundation
When brassinosteroid levels are low, the GSK3-like kinase BIN2 phosphorylates and in activates 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 an 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 suppress or 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.
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