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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >A dual mechanism controlling the localization and function of exocytic v-SNAREs
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A dual mechanism controlling the localization and function of exocytic v-SNAREs

机译：控制胞外v-SNAREs定位和功能的双重机制

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SNARE [soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor] proteins are essential for membrane fusion but their regulation is not yet fully understood. We have previously shown that the amino-terminal Longin domain of the v-SNARE TI-VAMP (tetanus neurotoxin-insensitive vesicle-associated membrane protein)/VAMP7 plays an inhibitory role in neurite outgrowth. The goal of this study was to investigate the regulation of TI-VAMP as a model of v-SNARE regulation. We show here that the Longin domain (LD) plays a dual role. First, it negatively regulates the ability of TI-VAMP and of a Longin/Synaptobrevin chimera to participate in SNARE complexes. Second, it interacts with the adaptor complexAP-3 and this interaction targets TI-VAMP to late endosomes. Accordingly, in mocha cells lacking AP-3delta, TI-VAMP is retained in an early endosomal compartment. Furthermore, TI-VAMPc, an isoform of TI-VAMP lacking part of the LD, does not interact with AP-3, and therefore is not targeted to late endosomes; however, this shorter LD still inhibits SNARE-complex formation. These findings support a mechanism controlling both localization and function of TI-VAMP through the LD and clathrin adaptors. Moreover, they point to the amino-terminal domains of SNARE proteins as multifunctional modules responsible for the fine tuning of SNARE function. [References: 39]
机译：SNARE [可溶性NSF（N-乙基马来酰亚胺敏感因子）附着蛋白受体]蛋白对于膜融合是必不可少的，但其调控尚不完全清楚。先前我们已经表明，v-SNARE TI-VAMP（破伤风神经毒素不敏感囊泡相关膜蛋白）/ VAMP7的氨基末端Longin域在神经突生长中起抑制作用。这项研究的目的是研究TI-VAMP作为v-SNARE调控模型的调控。我们在这里显示Longin域（LD）扮演双重角色。首先，它负调控TI-VAMP和Longin / Synaptobrevin嵌合体参与SNARE复合体的能力。其次，它与衔接子复合物AP-3相互作用，并且这种相互作用将TI-VAMP靶向晚期内体。因此，在缺乏AP-3δ的摩卡细胞中，TI-VAMP保留在早期的内体区室中。此外，TI-VAMPc是缺少LD部分的TI-VAMP的同工型，不会与AP-3相互作用，因此不针对晚期内体。然而，这个较短的LD仍然抑制了SNARE复合物的形成。这些发现支持了通过LD和网格蛋白衔接子控制TI-VAMP的定位和功能的机制。此外，它们指向SNARE蛋白的氨基末端结构域，作为负责SNARE功能微调的多功能模块。 [参考：39]

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