Spatiotemporal Dynamics of the BRI1 Receptor and its Regulation by Membrane Microdomains in Living Arabidopsis Cells
Jazyk angličtina Země Velká Británie, Anglie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
25896454
DOI
10.1016/j.molp.2015.04.005
PII: S1674-2052(15)00202-6
Knihovny.cz E-zdroje
- Klíčová slova
- BR signaling, BRI1, endocytosis, membrane microdomains, spatiotemporal dynamics,
- MeSH
- Arabidopsis cytologie metabolismus MeSH
- brassinosteroidy farmakologie MeSH
- časoprostorová analýza * MeSH
- difuze MeSH
- endocytóza účinky léků MeSH
- klathrin metabolismus MeSH
- membránové mikrodomény účinky léků metabolismus MeSH
- multimerizace proteinu účinky léků MeSH
- pohyb těles MeSH
- proteinkinasy metabolismus MeSH
- proteiny huseníčku metabolismus MeSH
- rostlinné buňky účinky léků metabolismus MeSH
- signální transdukce účinky léků MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- brassinosteroidy MeSH
- BRI1 protein, Arabidopsis MeSH Prohlížeč
- klathrin MeSH
- proteinkinasy MeSH
- proteiny huseníčku 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
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