REGULATION OF THE ASSOCIATION OF MEMBRANE SKELETAL PROTEIN-4.1 WITH GLYCOPHORIN BY A POLYPHOSPHOINOSITIDE
REGULATION OF THE ASSOCIATION OF MEMBRANE SKELETAL PROTEIN-4.1 WITH GLYCOPHORIN BY A POLYPHOSPHOINOSITIDE
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DOI：
10.1038/318295a0
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发表时间：
1985-01-01
期刊：
影响因子：
64.8
通讯作者：
MARCHESI, VT
中科院分区：
文献类型：
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作者：
ANDERSON, RA;MARCHESI, VT
红细胞膜的许多物理性质似乎取决于膜骨架，其通过与跨膜蛋白1 -5的结合而附着于膜。膜骨架蛋白，蛋白4.1，是关键的组装膜骨架，因为它的能力，以促进协会之间的血影蛋白和肌动蛋白5 -9。蛋白4.1也通过至少两个位点与膜结合：血型糖蛋白上的高亲和力位点2，10和与带3相关的低亲和力位点（参考文献11）。血型糖蛋白4.1协会已被提出参与维持细胞形状2，12，13。在这里，我们表明，血型糖蛋白和蛋白4.1之间的关联是由一个多磷酸肌醇辅因子。这一观察结果提示了一种机制，可以解释最近报道的红细胞形状对膜中聚磷酸肌醇水平的依赖性14 -16。
Many of the physical properties of the erythrocyte membrane appear to depend on the membrane skeleton, which is attached to the membrane through associations with transmembrane proteins1–5. A membrane skeletal protein, protein 4.1, is pivotal in the assembly of the membrane skeleton because of its ability to promote associations between spectrin and actin5–9. Protein 4.1 also binds to the membrane through at least two sites: a high-affinity site on the glycophorins2,10and a site of lower affinity associated with band 3 (ref. 11). The glycophorin–protein 4.1 association has been proposed to be involved in maintenance of cell shape2,12,13. Here we show that the association between glycophorin and protein 4.1 is regulated by a polyphosphoinositide cofactor. This observation suggests a mechanism which may explain the recently reported dependence of red cell shape on the level of polyphosphoinositides in the membrane14–16.