Distribution of Can1p into stable domains reflects lateral protein segregation within the plasma membrane of living S. cerevisiae cells
Distribution of Can1p into stable domains reflects lateral protein segregation within the plasma membrane of living S. cerevisiae cells
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DOI：
10.1242/jcs.01493
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发表时间：
2004-12-01
影响因子：
4
通讯作者：
Tanner, W
中科院分区：
文献类型：
--
作者：
Malinska, K;Malinsky, J;Tanner, W
最近，脂筏为基础的子域内的质膜活酿酒酵母细胞可视化使用绿色荧光蛋白融合，和非重叠的子域含有Pma 1 p或Can 1 p的区别。在这项研究中，长期稳定的子域进行了调查。用latrunculin A和nocodazole进行的实验排除了参与亚结构域稳定的细胞骨架成分。细胞壁的假定作用也被排除，因为细胞的原生质体化既不改变亚结构域的模式也不改变亚结构域的稳定性。相比之下，预期的内部动态的膜子域记录FRAP实验。最后，其他两个蛋白质被定位在Can 1 p/Pma 1 p质膜分区的框架内。我们发现，Fur 4p（另一个H+同向转运体）和Sur 7 p（未知功能的蛋白质）占据Can 1 p子域。
Recently, lipid-raft-based subdomains within the plasma membrane of living Saccharomyces cerevisiae cells were visualized using green fluorescent protein fusions, and non-overlapping subdomains containing either Pma1p or Can1p were distinguished. In this study, the long-term stability of the subdomains was investigated. Experiments with latrunculin A and nocodazole ruled out the involvement of cytoskeletal components in the stabilization of the subdomains. Also a putative role of the cell wall was excluded, because protoplasting of the cells changed neither the pattern nor the stability of the subdomains. By contrast, the expected inner dynamics of the membrane subdomains was documented by FRAP experiments. Finally, two other proteins were localized within the frame of the Can1p/Pma1p plasma-membrane partition. We show that Fur4p (another H+ symporter) and Sur7p (a protein of unknown function) occupy the Can1p subdomain.