Spatiotemporal Dynamics of the BRI1 Receptor and its Regulation by Membrane Microdomains in Living Arabidopsis Cells
Language English Country Great Britain, England Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
25896454
DOI
10.1016/j.molp.2015.04.005
PII: S1674-2052(15)00202-6
Knihovny.cz E-resources
- Keywords
- BR signaling, BRI1, endocytosis, membrane microdomains, spatiotemporal dynamics,
- MeSH
- Arabidopsis cytology metabolism MeSH
- Brassinosteroids pharmacology MeSH
- Spatio-Temporal Analysis * MeSH
- Diffusion MeSH
- Endocytosis drug effects MeSH
- Clathrin metabolism MeSH
- Membrane Microdomains drug effects metabolism MeSH
- Protein Multimerization drug effects MeSH
- Motion MeSH
- Protein Kinases metabolism MeSH
- Arabidopsis Proteins metabolism MeSH
- Plant Cells drug effects metabolism MeSH
- Signal Transduction drug effects MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Brassinosteroids MeSH
- BRI1 protein, Arabidopsis MeSH Browser
- Clathrin MeSH
- Protein Kinases MeSH
- Arabidopsis Proteins MeSH
The major brassinosteroid (BR) receptor of Arabidopsis BRASSINOSTEROID INSENSITIVE1 (BRI1) plays fundamental roles in BR signaling, but the molecular mechanisms underlying the effects of BR on BRI1 internalization and assembly state remain unclear. Here, we applied variable angle total internal reflection fluorescence microscopy and fluorescence cross-correlation spectroscopy to analyze the dynamics of GFP-tagged BRI1. We found that, in response to BR, the degree of co-localization of BRI1-GFP with AtFlot1-mCherry increased, and especially BR stimulated the membrane microdomain-associated pathway of BRI1 internalization. We also verified these observations in endocytosis-defective chc2-1 mutants and the AtFlot1 amiRNA 15-5 lines. Furthermore, examination of the phosphorylation status of bri1-EMS-suppressor 1 and measurement of BR-responsive gene expression revealed that membrane microdomains affect BR signaling. These results suggest that BR promotes the partitioning of BRI1 into functional membrane microdomains to activate BR signaling.
College of Biological Sciences and Biotechnology Beijing Forestry University Beijing 100083 China
College of Horticulture and Plant Protection Yangzhou University Yangzhou 225009 China
Department of Cell Biology Palacky University Olomouc Olomouc 78371 Czech Republic
Institute of Cellular and Molecular Botany University of Bonn Kirschallee 1 D 53115 Bonn Germany
References provided by Crossref.org
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