김태욱
2018-02-02T06:22:56Z
2018-02-02T06:22:56Z
2011-02
NATURE CELL BIOLOGY, v. 13, NO 2, Page. 124-49
1465-7392
http://www.nature.com/articles/ncb2151
http://hdl.handle.net/20.500.11754/35039
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.
en
NATURE PUBLISHING GROUP
PROTEIN PHOSPHATASE 2A
RECEPTOR KINASE BRI1
SIGNAL-TRANSDUCTION
BETA-CATENIN
TRANSCRIPTION FACTORS
ARABIDOPSIS-THALIANA
REGULATORY SUBUNIT
PLASMA-MEMBRANE
MECHANISMS
MODULATE
PP2A activates brassinosteroid-responsive gene expression and plant growth by dephosphorylating BZR1
Article
2
13
10.1038/ncb2151
124-49
NATURE CELL BIOLOGY
Tang, Wenqiang
Yuan, Min
Wang, Ruiju
Yang, Yihong
Wang, Chunming
Oses-Prieto, Juan
Kim, Tae-Wuk
Zhou, Hong-Wei
Deng, Zhiping
Gampala, Srinivas
2011206935
S
COLLEGE OF NATURAL SCIENCES[S]
DEPARTMENT OF LIFE SCIENCE
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