Spatiotemporal Dynamics of the BRI1 Receptor and its Regulation by Membrane Microdomains in Living Arabidopsis Cells

作     者：Li Wang Hong Li Xueqin Lv Tong Chen Ruili Li Yiqun xuei Jianjun Jiang Biao Jin Frantisek Baluska Jozef Samaj Xuelu Wang Jinxing Lin 

作者机构：Key Laboratory of Ptant Resources Institute of Botany Chinese Academy of Sciences Beijing 100093 China College of Horticulture and Plant Protection Yangzhou University Yangzhou 225009 China College of Biological Sciences and Biotechnology Beijing Forestry University Beijing 100083 China State Key Laboratory of Genetic Engineering and Institute of Plant Biology School of Life Sciences Fudan University Shanghai 200433 China Institute of Cellular and Molecular Botany University of Bonn Kirschallee 1 D-53115 Bonn Germany Department of Cell Biology Palacky University OIomouc Olomouc 78371 Czech Republic College of Life Science and Technology Huazhong Agricultural University Wuhan 430070 China These authors contributed equally to the article. 

出 版 物：《Molecular Plant》 (分子植物（英文版）)

年 卷 期：2015年第8卷第9期

页      面：1334-1349页

核心收录：

学科分类：0710[理学-生物学] 07[理学] 071009[理学-细胞生物学] 09[农学] 071007[理学-遗传学] 0901[农学-作物学] 090102[农学-作物遗传育种] 

基　　金：supported by the Program of Introducing Talents of Discipline to Universities (111 project) Major Science Foundation of Ministry of Education of China 国家自然科学基金 the Open Research Funds of the State Key Laboratory of Genetic Engineering, Fudan University the Center of the Region Hana for Biotechnological and Agricultural Research, Faculty of Science, Palacky University, Olomouc, Czech Republic 

主　　题：BRI1 BR signaling endocytosis membrane microdomains spatiotemporal dynamics 

摘      要：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 BRII. We found that, in response to BR, the degree of co-localization of BRI1-GFP with AtFIotl-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 AtFIotl amiRNA 15-5 lines. Furthermore, examination of the phosphorylation status of bril-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.