OLIGOMERIC STRUCTURE OF CAVEOLIN - IMPLICATIONS FOR CAVEOLAE MEMBRANE ORGANIZATION
OLIGOMERIC STRUCTURE OF CAVEOLIN - IMPLICATIONS FOR CAVEOLAE MEMBRANE ORGANIZATION
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DOI：
10.1073/pnas.92.20.9407
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发表时间：
1995-09-26
影响因子：
11.1
通讯作者：
LISANTI, MP
中科院分区：
文献类型：
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作者：
SARGIACOMO, M;SCHERER, PE;LISANTI, MP
小窝蛋白是一种分子量为22-kDa的蛋白质，定位于细胞质膜的细胞质表面，称为小窝。我们提出小窝蛋白可能作为一种支架蛋白，在小窝内组织和集中信号分子。在这里，我们表明，小窝蛋白与自身相互作用，形成homooligomers。这些纯化的小窝蛋白同源寡聚体的电子显微镜可视化表明，它们作为单独的球形颗粒出现。通过使用小窝蛋白作为谷胱甘肽S-转移酶融合蛋白的重组表达，我们定义了小窝蛋白胞质N末端结构域的一个区域，该区域介导这些小窝蛋白-小窝蛋白相互作用。我们认为，小窝蛋白homooligomers可能起到集中小窝蛋白相互作用的分子内小窝。在这方面，将小窝蛋白同低聚体视为具有多个“钩”或小窝蛋白相互作用分子的附着位点的“鱼饵”可能是有用的。
A 22-kDa protein, caveolin, is localized to the cytoplasmic surface of plasma membrane specializations called caveolae, We have proposed that caveolin may function as a scaffolding protein to organize and concentrate signaling molecules within caveolae. Here, we show that caveolin interacts with itself to form homooligomers. Electron microscopic visualization of these purified caveolin homooligomers demonstrates that they appear as individual spherical particles. By using recombinant expression of caveolin as a glutathione S-transferase fusion protein, we have defined a region of caveolin's cytoplasmic N-terminal domain that mediates these caveolin-caveolin interactions. We suggest that caveolin homooligomers may function to concentrate caveolin-interacting molecules within caveolae. In this regard, it may be useful to think of caveolin hommoligomers as ''fishing lures'' with multiple ''hooks'' or attachment sites for caveolin-interacting molecules.