Different behavior of l-Afadin and Neurabin-II during the formation and destruction of cell – cell adherens junction
Different behavior of l-Afadin and Neurabin-II during the formation and destruction of cell – cell adherens junction
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DOI：
10.1038/sj.onc.1202451
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发表时间：
1999-02
期刊：
影响因子：
8
通讯作者：
T. Sakisaka;H. Nakanishi;Kenichi Takahashi;K. Mandai;Masako Miyahara;A. Satoh;K. Takaishi;Y. Takai
中科院分区：
文献类型：
--
作者：
T. Sakisaka;H. Nakanishi;Kenichi Takahashi;K. Mandai;Masako Miyahara;A. Satoh;K. Takaishi;Y. Takai
我们最近分离到两个新的肌动蛋白微丝结合蛋白，L-afadin和Neurabin-II，并证明它们定位于上皮细胞的细胞-细胞黏附连接(AJ)。我们在此发现，在MDCK细胞AJ的形成和破坏过程中，L-afadin、Neurabin-II、ZO-1和E-cadherin表现出相似和不同的行为。在MDCK细胞中，L-非粘附素和E-钙粘附素的积聚，而不是ZO-1的积聚，随着Rac小G蛋白活性的变化而平行变化。用2μ的钙离子培养mDCK细胞，可引起E-钙粘附素的迅速内吞，但不能引起L-阿法丁或ZO-1的内吞。加入佛波醇12-肉豆蔻酸酯13-乙酸酯后，这些细胞形成紧密连接的结构，其中ZO-1和L-Fafadin积聚，而不是Neurabin-II或E-cadherin积聚。我们进一步发现，在表达E-钙粘素的非上皮性EL细胞中，L-钙粘附素、Neurabin-II、ZO-1和E-钙粘附素均定位于AJ。在钙粘附素缺乏的L细胞中，L-非铁蛋白主要定位于细胞-细胞接触部位，而ZO-1主要定位于细胞突起的顶端。Neurabin-II未在质膜区域聚集。与α-，β-连环蛋白、E-钙粘附素、ZO-1或阻滞素均无明显相互作用。
We have recently isolated two novel actin filament-binding proteins, l-afadin and neurabin-II and shown that they are localized at cell–cell adherens junction (AJ) in epithelial cells. We found here that l-afadin, neurabin-II, ZO-1, and E-cadherin showed similar and different behavior during the formation and destruction of cell–cell AJ in MDCK cells. In MDCK cells, the accumulation of both l-afadin and E-cadherin, but not that of ZO-1, changed in parallel depending on Rac small G protein activity. Dissociation of MDCK cells by culturing the cells at 2 μ M Ca 2+ caused rapid endocytosis of E-cadherin, but not that of l-afadin or ZO-1. Addition of phorbol 12-myristate 13-acetate to these dissociated cells formed a tight junction-like structure where ZO-1 and l-afadin, but not neurabin-II or E-cadherin, accumulated. We furthermore found that, in non-epithelial EL cells, which expressed E-cadherin and attached to each other, l-afadin, neurabin-II, ZO-1 and E-cadherin were all localized at AJ. In cadherin-deficient L cells, l-afadin was mainly localized at cell–cell contact sites, but ZO-1 was mainly localized at the tip area of cell processes. Neurabin-II did not accumulate at the plasma membrane area. Neither l-afadin nor neurabin-II significantly interacted with α-, β-catenin, E-cadherin, ZO-1 or occludin.