Faigle W, Colucci-Guyon E, Louvard D, Amigorena S, Galli T
Group of Cellular Biology of Tumoral Immunity, Institut National de la Santé et de la Recherche Médicale U520, Institut Curie, F-75248 Paris Cédex 05, France.
Mol Biol Cell. 2000 Oct;11(10):3485-94. doi: 10.1091/mbc.11.10.3485.
Soluble N-ethyl maleimide-sensitive fusion protein attachment protein receptors (SNAREs) are core machinery for membrane fusion during intracellular vesicular transport. Synaptosome-associated protein of 23 kDa (SNAP23) is a target SNARE previously identified at the plasma membrane, where it is involved in exocytotic membrane fusion. Here we show that SNAP23 associates with vimentin filaments in a Triton X-100 insoluble fraction in fibroblasts in primary culture and HeLa cells. Upon treatment of human fibroblasts with N-ethyl-maleimide, SNAP23 dissociates from vimentin filaments and forms a protein complex with syntaxin 4, a plasma membrane SNARE. The vimentin-associated pool of SNAP23 can therefore be a reservoir, which would supply the plasma membrane fusion machinery, in fibroblasts. Our observation points to a yet unexplored role of intermediate filaments.
可溶性N - 乙基马来酰亚胺敏感融合蛋白附着蛋白受体（SNAREs）是细胞内囊泡运输过程中膜融合的核心机制。23 kDa的突触体相关蛋白（SNAP23）是先前在质膜上鉴定出的一种靶标SNARE，它参与胞吐性膜融合。在这里，我们表明SNAP23在原代培养的成纤维细胞和HeLa细胞的Triton X - 100不溶性组分中与波形蛋白丝相关联。用N - 乙基马来酰亚胺处理人成纤维细胞后，SNAP23从波形蛋白丝上解离，并与质膜SNARE syntaxin 4形成蛋白复合物。因此，在成纤维细胞中，与波形蛋白相关的SNAP23池可以作为一个储备库，为质膜融合机制提供物质。我们的观察结果指出了中间丝尚未被探索的作用。
