Phosphatidylserine binding sites in red cell spectrin
Phosphatidylserine binding sites in red cell spectrin
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DOI：
10.1016/j.bcmd.2004.02.001
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发表时间：
2004-05-01
影响因子：
2.3
通讯作者：
Mohandas, N
中科院分区：
文献类型：
--
作者：
An, XL;Guo, XH;Mohandas, N
Spectrin已被证明与磷脂酰丝氨酸（PS）相互作用，然而，在Spectrin中，PS的确切结合位点尚未确定。在目前的研究中，我们利用包含两个谱蛋白链全部序列的重组谱蛋白片段确定了谱蛋白中特定的PS结合位点。我们发现，高亲和力的位点位于38个三螺旋结构重复序列中的8个，这些重复序列构成了两条链的大部分；它们是：alpha8和alpha9-10，以及beta2， beta3, beta4, beta12， beta13和beta14，并且在β链的非同源n端结构域也发现了PS亲和力。值得注意的是，β -spectrin中的ps结合位点聚集在锚蛋白和4.1 R的附着位点附近，4.1 R是参与spectrin与膜的附着的蛋白质。我们推测，spectrin与膜补体中PS的直接相互作用调节了它与蛋白质的相互作用，并且(考虑到已知的4。在红细胞膜中观察到的富含PS的脂质结构域的形成可能是其结果。(C) 2004爱思唯尔公司版权所有。
Spectrin has been shown to interact with phosphatidylserine (PS), however, the precise binding sites for PS in spectrin have not been defined. In the present study, we have identified specific PS binding sites in spectrin using recombinant spectrin fragments encompassing the entire sequences of both spectrin chains. We show that sites of high affinity are located within eight of the 38 triple-helical structural repeats which make up the bulk of both chains; these are: alpha8 and alpha9-10, and beta2, beta3, beta4, beta12, beta13, and beta14, and PS affinity was also found in the non-homologous N-terminal domain of the beta-chain. It is noteworthy that the PS-binding sites in beta-spectrin are clustered in close proximity to the sites of attachment both of ankyrin and of 4.1 R, the proteins engaged in attachment of spectrin to the membrane. We conjecture that direct interaction of spectrin with PS in the membrane complements modulates its interactions with the proteins, and that (considering also the known affinity of 4. 1 R for PS) the formation of PS-rich lipid domains, which have been observed in the red cell membrane, may be a result. (C) 2004 Elsevier Inc. All rights reserved.