Regulation of Golgi structure through heterotrimeric G proteins
Regulation of Golgi structure through heterotrimeric G proteins
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DOI：
10.1016/s0092-8674(00)80449-3
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发表时间：
1997-11-28
期刊：
影响因子：
64.5
通讯作者：
Malhotra, V
中科院分区：
文献类型：
--
作者：
Jamora, C;Takizawa, PA;Malhotra, V
我们以前已经表明，ilimaquinone（IQ），海绵代谢产物，导致完全囊泡的高尔基体堆栈。通过重建的I-介导的囊泡化的高尔基体透化细胞，我们现在证明，这个过程不需要ARF和coatomers，这是必要的高尔基体衍生的COPI囊泡的形成。我们发现IQ介导的高尔基体囊泡化被G-α（s）-GDP和G-α（13）-GDP抑制。有趣的是，在缺乏IQ的情况下，添加β-γ亚基足以使高尔基体囊泡化。我们的研究结果表明，I-介导的高尔基体囊泡发生通过激活异源三聚体G蛋白，它是免费的β-γ，而不是激活的α亚基，触发高尔基体囊泡。
We have previously shown that ilimaquinone (IQ), a marine sponge metabolite, causes complete vesiculation of the Golgi stacks. By reconstituting the I-mediated vesiculation of the Golgi apparatus in permeabilized cells, we now demonstrate that this process does not require ARF and coatomers, which are necessary for the formation of Golgi-derived COPI vesicles. We find that IQ-mediated Golgi vesiculation is inhibited by G-alpha(s)-GDP and G-alpha(13)-GDP. Interestingly, adding beta-gamma subunits in the absence of IQ is sufficient to vesiculate Golgi stacks. Our findings reveal that I-mediated Golgi vesiculation occurs through activation of heterotrimeric G proteins and that it is the free beta-gamma, and not the activated alpha subunit, that triggers Golgi vesiculation.