Defects in Dynamics and Functions of Actin Filament in Arabidopsis Caused by the Dominant-Negative Actin fiz1-Induced Fragmentation of Actin Filament
Defects in Dynamics and Functions of Actin Filament in Arabidopsis Caused by the Dominant-Negative Actin fiz1-Induced Fragmentation of Actin Filament
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DOI：
10.1093/pcp/pcp189
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发表时间：
2010-02-01
影响因子：
4.9
通讯作者：
Tasaka, Masao
中科院分区：
文献类型：
--
作者：
Kato, Takehide;Morita, Miyo Terao;Tasaka, Masao
我们从拟南芥中分离到一个新的显性肌动蛋白突变体Frizzy1(Fiz1)。在Fiz1突变体中，ACT8疏水环上的Glu272被赖氨酸取代，这对聚合非常重要。肌动蛋白细丝的实时成像显示，Fiz1突变以半显性方式诱导了肌动蛋白细丝的断裂。此外，高尔基体堆叠和线粒体的动力学被fiz1效应打乱。这些结果表明，Fiz1突变对肌动蛋白聚合具有显性-负性影响，从而导致肌动蛋白细丝功能的缺陷，如细胞器运输。
We isolated frizzy1 (fiz1), a novel dominant actin mutant from Arabidopsis. In the fiz1 mutant, Glu272 was substituted with lysine in the hydrophobic loop of ACT8, which is very important for the polymerization. Live imaging of actin filaments revealed that the fiz1 mutation induced fragmentation of actin filaments in a semi-dominant manner. In addition, the dynamics of Golgi stacks and mitochondria were disrupted by the fiz1 effects. From these results, it was strongly suggested that the fiz1 mutation had dominant-negative effects on actin polymerization, which causes defects in the functions of actin filaments such as organelle transport.