A common mechanism for the regulation of vesicular SNAREs on phospholipid membranes
A common mechanism for the regulation of vesicular SNAREs on phospholipid membranes
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DOI：
10.1042/bj20031164
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发表时间：
2004-02-01
影响因子：
4.1
通讯作者：
Davletov, B
中科院分区：
文献类型：
--
作者：
Hu, K;Rickman, C;Davletov, B
SNARE（可溶性N-乙基马来酰亚胺敏感融合蛋白附着蛋白受体）蛋白家族是真核生物细胞内运输中膜融合所必需的。v-SNARE（囊泡SNARE）必须与相对膜中的靶SNARE接合以形成融合SNARE复合物。膜融合的时间和空间控制对于细胞生理学的许多方面是重要的，并且可能涉及驻留在细胞内膜上的SNARE的调节。在这里，我们表明，v-SNARE小突触素2，也被称为VAMP（囊泡相关膜蛋白）2，是限制形成的SNARE复合物在肾上腺髓质嗜铬颗粒在相同的程度，在脑纯化的突触囊泡。我们的分析表明，以前报道的突触泡蛋白-小突触泡蛋白相互作用是不太可能参与调节的v-SNARE。事实上，通过在纯脂质体膜中重建两种不同的v-SNARE同源物，小突触泡蛋白2和小纤维泡蛋白/VAMP 3，可以再现这种限制。总的来说，我们的数据揭示了一个共同的机制，控制陷阱的参与，完整的磷脂膜，而不是蛋白质下调囊泡陷阱在不同的细胞器。
The SNARE (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor) family of proteins is essential for membrane fusion in intracellular traffic in eukaryotic organisms. v-SNAREs (vesicular SNAREs) must engage target SNAREs in the opposing membrane to form the fusogenic SNARE complex. Temporal and spatial control of membrane fusion is important for many aspects of cell physiology and may involve the regulation of the SNAREs resident on intracellular membranes. Here we show that the v-SNARE synaptobrevin 2, also known as VAMP (vesicle-associated membrane protein) 2, is restricted from forming the SNARE complex in chromaffin granules from adrenal medullae to the same degree as in brain-purified synaptic vesicles. Our analysis indicates that the previously reported synaptophysin-synaptobrevin interaction is not likely to be involved in regulation of the v-SNARE. Indeed, the restriction can be reproduced for two distinct v-SNARE homologues, synaptobrevin 2 and cellubrevin/VAMP3, by reconstituting them in pure liposomal membranes. Overall, our data uncover a common mechanism for the control of SNARE engagement where intact phospholipid membranes rather than proteins down-regulate vesicular SNAREs in different cellular organelles.