A green fluorescent protein fusion to actin-binding domain 2 of Arabidopsis fimbrin highlights new features of a dynamic actin cytoskeleton in live plant cells

被引:200
作者
Sheahan, MB
Staiger, CJ
Rose, RJ
McCurdy, DW [1 ]
机构
[1] Univ Newcastle, Sch Environm Life Sci, Callaghan, NSW 2308, Australia
[2] Univ Newcastle, Australian Res Council Ctr Excellence Integrat Le, Callaghan, NSW 2308, Australia
[3] Purdue Univ, Dept Biol Sci, W Lafayette, IN 47907 USA
关键词
D O I
10.1104/pp.104.049411
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The actin cytoskeleton coordinates numerous cellular processes required for plant development. The functions of this network are intricately linked to its dynamic arrangement, and thus progress in understanding how actin orchestrates cellular processes relies on critical evaluation of actin organization and turnover. To investigate the dynamic nature of the actin cytoskeleton, we used a fusion protein between green fluorescent protein (GFP) and the second actin-binding domain (fABD2) of Arabidopsis (Arabidopsis thaliana) fimbrin, AtFIM1. The GFP-fABD2 fusion protein labeled highly dynamic and dense actin networks in diverse species and cell types, revealing structural detail not seen with alternative labeling methods, such as the commonly used mouse talin GFP fusion (GFP-mTalin). Further, we show that expression of the GFP-fABD2 fusion protein in Arabidopsis, unlike GFP-mTalin, has no detectable adverse effects on plant morphology or development. Time-lapse confocal microscopy and fluorescence recovery after photobleaching analyses of the actin cytoskeleton labeled with GFP-fABD2 revealed that lateral-filament migration and sliding of individual actin filaments or bundles are processes that contribute to the dynamic and continually reorganizing nature of the actin scaffold. These new observations of the dynamic actin cytoskeleton in plant cells using GFP-fABD2 reveal the value of this probe for future investigations of how actin filaments coordinate cellular processes required for plant development.
引用
收藏
页码:3968 / 3978
页数:11
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