Wyatt K, Cherry R J
Department of Chemistry and Biological Chemistry, University of Essex, Colchester, UK.
Biochim Biophys Acta. 1992 Jan 31;1103(2):327-30. doi: 10.1016/0005-2736(92)90104-t.
A population of band 3 proteins in the human erythrocyte membrane is known to have restricted rotational mobility due to interaction with cytoskeletal proteins. We have further investigated the cause of this restriction by measuring the effects on band 3 rotational mobility of rebinding ankyrin and band 4.1 to ghosts stripped of these proteins as well as spectrin and actin. Rebinding either ankyrin or 4.1 alone has no detectable effect on band 3 mobility. Rebinding both these proteins together does, however, reimpose a restriction on band 3 rotation. The effect on band 3 rotational mobility of rebinding ankyrin and 4.1 are similar irrespective of whether or not band 4.2 is removed from the membrane. We suggest that ankyrin and 4.1 together promote the formation of slowly rotating clusters of band 3.
已知人类红细胞膜中的一群带3蛋白由于与细胞骨架蛋白相互作用而具有受限的旋转流动性。我们通过测量将锚蛋白和带4.1重新结合到去除了这些蛋白以及血影蛋白和肌动蛋白的血影上对带3旋转流动性的影响，进一步研究了这种限制的原因。单独重新结合锚蛋白或4.1对带3的流动性没有可检测到的影响。然而，将这两种蛋白一起重新结合确实会再次对带3的旋转施加限制。无论带4.2是否从膜上去除，重新结合锚蛋白和4.1对带3旋转流动性的影响都是相似的。我们认为，锚蛋白和4.1共同促进了带3缓慢旋转簇的形成。
