Concentration of an integral membrane protein, CD43 (leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletons.
Concentration of an integral membrane protein, CD43 (leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletons.
复制标题
整合性膜蛋白CD43（白细胞素，唾液磷脂）的浓度通过其细胞质结构域与基于肌动蛋白的细胞骨架的相互作用，在裂解沟中。
DOI：
10.1083/jcb.120.2.437
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发表时间：
1993-01
影响因子：
7.8
通讯作者：
Tsukita, S
中科院分区：
文献类型：
--
作者：
Yonemura, S;Nagafuchi, A;Sato, N;Tsukita, S
在胸腺细胞和嗜碱性白血病细胞等白细胞中，一种称为 CD43（白唾液酸蛋白或唾液酸蛋白）的糖基化整合膜蛋白在胞质分裂过程中高度集中在卵裂沟中，这种蛋白在 Wiskott-Aldrich 综合征患者中存在缺陷。不仅在有丝分裂期，而且在间期，CD43 都与 ezrin-radixin-moesin 家族成员精确共定位。 （ERM），之前报道其在质膜-肌动蛋白丝关联中发挥重要作用。在电子显微镜水平上，在整个细胞周期中，CD43 和 ERM 都与微绒毛紧密相关，为肌动蛋白丝提供膜附着位点。我们构建了编码由小鼠E-钙粘蛋白胞外结构域和大鼠CD43跨膜/胞质结构域组成的嵌合分子的cDNA，并将其导入缺乏内源性CD43和E-钙粘蛋白的小鼠L成纤维细胞中。在分裂转染子中，嵌合分子与 ERM 一起集中在裂解沟中，并且两种蛋白质在整个细胞周期中精确地共定位。此外，使用该转染系统，我们缩小了负责裂解沟中 CD43 浓度的结构域。基于这些发现，我们得出结论，CD43 通过其细胞质结构域与 ERM 和肌动蛋白丝的直接或间接相互作用而集中在卵裂沟中。
In leukocytes such as thymocytes and basophilic leukemia cells, a glycosilated integral membrane protein called CD43 (leukosialin or sialophorin), which is defective in patients with Wiskott-Aldrich syndrome, was highly concentrated in the cleavage furrow during cytokinesis. Not only at the mitotic phase but also at interphase, CD43 was precisely colocalized with ezrin-radixin-moesin family members. (ERM), which were previously reported to play an important role in the plasma membrane-actin filament association in general. At the electron microscopic level, throughout the cell cycle, both CD43 and ERM were tightly associated with microvilli, providing membrane attachment sites for actin filaments. We constructed a cDNA encoding a chimeric molecule consisting of the extracellular domain of mouse E-cadherin and the transmembrane/cytoplasmic domain of rat CD43, and introduced it into mouse L fibroblasts lacking both endogenous CD43 and E-cadherin. In dividing transfectants, the chimeric molecules were concentrated in the cleavage furrow together with ERM, and both proteins were precisely colocalized throughout the cell cycle. Furthermore, using this transfection system, we narrowed down the domain responsible for the CD43-concentration in the cleavage furrow. Based on these findings, we conclude that CD43 is concentrated in the cleavage furrow through the direct or indirect interaction of its cytoplasmic domain with ERM and actin filaments.