Mechanism of caveolin filament assembly
Mechanism of caveolin filament assembly
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DOI：
10.1073/pnas.172196599
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发表时间：
2002-08-20
影响因子：
11.1
通讯作者：
Anderson, RGW
中科院分区：
文献类型：
--
作者：
Fernandez, I;Ying, YS;Anderson, RGW
Caveolin-1 是第一个被鉴定的蛋白质，它与小窝膜内表面上发现的大约 10 纳米的细丝共定位。我们结合使用电子显微镜 (EM)、圆二色性和分析超速离心来确定 Caveolin-1 (Cavj(1-101)) 的前 101 个氨基酸缔合时形成的低聚物的结构。我们确定这个caveolin-1片段中的氨基酸79-96排列成a-螺旋。 Cav(1-101)寡聚物直径约为11 nm，含有七个Cav(1-101)分子。这些亚基反过来能够组装成 50 nm 长 x 11 nm 直径的细丝，与小窝丝状外套中细丝的形态密切匹配。我们认为七聚体亚基部分是通过七个 Cav(1-101) 单元的 a 螺旋之间的横向相互作用形成的。因此，Caveolin-1 似乎是小凹丝状外皮的结构分子。
Caveolin-1 was the first protein identified that colocalizes with the approximate to10-nm filaments found on the inside surface of caveolae membranes. We have used a combination of electron microscopy (EM), circular dichroism, and analytical ultracentrifugation to determine the structure of the oligomers that form when the first 101 aa of caveolin-1 (Cavj(1-101)) are allowed to associate. We determined that amino acids 79-96 in this caveolin-1 fragment are arranged in an a-helix. Cav(1-101) oligomers are approximate to11 nm in diameter and contain seven molecules of Cav(1-101). These subunits, in turn, are able to assemble into 50 nm long x 11 nm diameter filaments that closely match the morphology of the filaments in the caveolae filamentous coat. We propose that the heptameric subunit forms in part through lateral interactions between the a-helices of the seven Cav(1-101) units. Caveolin-1, therefore, appears to be the structural molecule of the caveolae filamentous coat.