A new dynamin-like protein, ADL6, is involved in trafficking from the trans-Golgi network to the central vacuole in Arabidopsis
A new dynamin-like protein, ADL6, is involved in trafficking from the trans-Golgi network to the central vacuole in Arabidopsis
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DOI：
10.1105/tpc.13.7.1511
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发表时间：
2001-07-01
期刊：
影响因子：
11.6
通讯作者：
Hwang, I
中科院分区：
文献类型：
--
作者：
Jin, JB;Kim, YA;Hwang, I
Dynamin是一种高相对分子质量的GTP酶，在动物细胞内吞作用过程中，在质膜上形成囊泡过程中起着关键作用。本文报道了拟南芥中一种新的动力蛋白同源物的鉴定结果，命名为拟南芥动力蛋白类似物6(ADL6)。ADL6在结构上与Dynamin I非常相似：N端有一个保守的GTP酶结构域，中心有一个Pleckstrin同源结构域，C端有一个富含Pro的基序。在细胞中，ADL6的大部分与膜相关。免疫组织化学和体内靶向实验表明ADL6定位于高尔基体。显性负性突变体ADL6[K51E]在拟南芥原生质体中的表达抑制了运往裂解液泡的货物蛋白的运输，并使它们在反高尔基网络中积累。相反，ADL6[K51E]的表达并不影响运往质膜的货运蛋白H+-ATPase：绿色荧光蛋白的运输。这些结果表明，在植物细胞中，ADL6参与了液泡运输的囊泡形成，而不是运输到质膜。
Dynamin, a high-molecular-weight GTPase, plays a critical role in vesicle formation at the plasma membrane during endocytosis in animal cells. Here we report the identification of a new dynamin homolog in Arabidopsis named Arabidopsis dynamin-like 6 (ADL6). ADL6 is quite similar to dynamin I in its structural organization: a conserved GTPase domain at the N terminus, a pleckstrin homology domain at the center, and a Pro-rich motif at the C terminus. In the cell, a majority of ADL6 is associated with membranes. Immunohistochemistry and in vivo targeting experiments revealed that ADL6 is localized to the Golgi apparatus. Expression of the dominant negative mutant ADL6[K51E] in Arabidopsis protoplasts inhibited trafficking of cargo proteins destined for the lytic vacuole and caused them to accumulate at the trans-Golgi network. In contrast, expression of ADL6[K51E] did not affect trafficking of a cargo protein, H+-ATPase:green fluorescent protein, destined for the plasma membrane. These results suggest that ADL6 is involved in vesicle formation for vacuolar trafficking at the trans-Golgi network but not for trafficking to the plasma membrane in plant cells.