The C-TERMINUS of AtGRIP is crucial for its self-association and for targeting to Golgi stacks in Arabidopsis.
The C-TERMINUS of AtGRIP is crucial for its self-association and for targeting to Golgi stacks in Arabidopsis.
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DOI：
10.1371/journal.pone.0098963
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发表时间：
2014
期刊：
影响因子：
3.7
通讯作者：
Li Y
中科院分区：
文献类型：
--
作者：
Zhao L;Li Y
在动物和真菌中，二聚化对于将GRIP结构域蛋白质靶向高尔基体至关重要。拟南芥基因组中只有一个基因AtGRIP编码GRIP结构域蛋白。目前还不清楚AtGRIP是否具有与GRIP结构域蛋白相似的性质。在本研究中，蛋白质印迹和酵母双杂交分析表明，AtGRIPs可以形成一个平行的同源二聚体。此外，酵母双杂交分析表明，AtGRIPa 711 -753、AtGRIPa 711 -766和AtGRIPa 711 -776不与自身相互作用，但完整的GRIP结构域与AtGRIP C端相互作用。共聚焦显微镜显示，只有一个完整的GRIP结构域与AtGRIP C-末端可以定位到高尔基体堆栈在拟南芥叶原生质体。BLAST分析表明，GRIP蛋白的C末端在植物界是保守的。突变和酵母双杂交分析表明，AtGRIP的L742有助于二聚化和高尔基体定位是至关重要的。这些结果表明，GRIP蛋白的C-末端是必不可少的自我协会和在植物细胞中的高尔基体堆栈的目标。我们认为，GRIP蛋白的几个属性不同的植物和动物细胞之间。
In animals and fungi, dimerization is crucial for targeting GRIP domain proteins to the Golgi apparatus. Only one gene in the Arabidopsis genome, AtGRIP, codes for a GRIP domain protein. It remains unclear whether AtGRIP has properties similar to those of GRIP domain proteins. In this study, western blot and yeast two-hybrid analyses indicated that AtGRIPs could form a parallel homodimer. In addition, yeast two-hybrid analysis indicated that AtGRIPaa711–753, AtGRIPaa711–766 and AtGRIPaa711–776 did not interact with themselves, but the intact GRIP domain with the AtGRIP C-terminus did. Confocal microscopy showed that only an intact GRIP domain with an AtGRIP C-terminus could localize to the Golgi stacks in Arabidopsis leaf protoplasts. A BLAST analysis showed that the C-terminus of GRIP proteins was conserved in the plant kingdom. Mutagenesis and yeast two-hybrid analyses showed that the L742 of AtGRIP contributed to dimerization and was crucial for Golgi localization. These results indicate that the C-terminus of GRIP proteins is essential for self-association and for targeting of Golgi stacks in plant cells. We suggest that several properties of GRIP proteins differ between plant and animal cells.
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