期刊
SCIENCE SIGNALING
卷 4, 期 172, 页码 -出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/scisignal.2001258
关键词
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资金
- Howard Hughes Medical Institute
- U.S. Department of Agriculture (National Research Initiative Competitive) [2006-35304-16586]
- National Science Foundation (NSF) [IOS-06-49389, MCB-0619736, MCB-0843151]
- Ruth L. Kirschstein NIH
- Japan Society for the Promotion of Science
- [18-06765]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0843151] Funding Source: National Science Foundation
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 and BR signaling. We report the identification, in A. thaliana, of a suppressor of bri1, sbi1, which caused selective accumulation of BR-activated BRI1, but not the BR co-receptor BAK1 (BRI1-ASSOCIATED KINASE 1), in the membranous compartment. SBI1 mRNA was induced by BRs, and SBI1 encodes a leucine carboxylmethyltransferase (LCMT) that methylated PP2A and controlled its membrane-associated subcellular localization. We propose that BRs increase production of SBI1, which methylates PP2A, thus facilitating its association with activated BRI1. This leads to receptor dephosphorylation and degradation, and thus to the termination of BR signaling.
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