Mouse prenylated Rab acceptor is a novel Golgi membrane protein.
Mouse prenylated Rab acceptor is a novel Golgi membrane protein.
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DOI：
10.1006/bbrc.2000.3316
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发表时间：
2000-08
影响因子：
3.1
通讯作者：
Z. Liang;G. Li
中科院分区：
文献类型：
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作者：
Z. Liang;G. Li
我们已经克隆了小鼠异戊二烯化Rab受体（mPRA），它与各种Rab蛋白在酵母双杂交系统中相互作用。本研究探讨了其细胞内定位和定位信号的特点。mPRA被认为是一个完整的膜蛋白，被定位到高尔基复合体在稳定状态下，通过共聚焦荧光显微镜测定。将绿色荧光蛋白连接到mPRA的N-末端，融合蛋白在BHK细胞中表达，并显示出与天然mPRA相同的高尔基体定位。从N-和C-末端的mPRA的系统性截短显示，整个N-末端的一半（91个残基）的蛋白质是高尔基体定位。与此相反，从C-末端仅5个残基的缺失减少了mPRA的高尔基体定位，导致其在ER中的积累。这些数据表明，C-末端的一半（94个残基）的mPRA是必要的和足够的适当折叠，ER出口，和高尔基体定位。mPRA的高尔基定位表明，它可能在高尔基复合体的结构组织和功能中发挥作用。
We have cloned a mouse prenylated Rab acceptor (mPRA), which interacts with various Rab proteins in the yeast two-hybrid system. This study investigated its intracellular localization and characterized the localization signal. The mPRA was found to be an integral membrane protein that was localized to the Golgi complex at steady state as determined by confocal fluorescence microscopy. With green fluorescent protein attached to the N-terminus of mPRA, the fusion protein was expressed in BHK cells and was shown to exhibit the same Golgi localization as the native mPRA. Systematic truncations from the N- and C-termini of mPRA revealed that the entire N-terminal half (91 residues) of the protein was dispensable for the Golgi localization. In contrast, deletion of only 5 residues from the C-terminus diminished the Golgi localization of mPRA, leading to its accumulation in the ER. The data indicate that the C-terminal half (94 residues) of mPRA is necessary and sufficient for proper folding, ER export, and Golgi localization. The Golgi localization of mPRA suggests that it may play a role in the structural organization and function of the Golgi complex.