Direct association of connexin36 with zonula occludens-2 and zonula occludens-3.
Direct association of connexin36 with zonula occludens-2 and zonula occludens-3.
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DOI：
10.1016/j.neuint.2009.01.003
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发表时间：
2009-05
影响因子：
4.2
通讯作者：
Nagy, James I.
中科院分区：
文献类型：
--
作者：
Li, Xinbo;Lu, Shijun;Nagy, James I.
缝隙连接蛋白36(C×36)在神经元中广泛表达，并与含有PDZ结构域的阻塞性小带蛋白1(ZO-1)相互作用。我们研究了C×36是否也能与闭锁小带蛋白家族的其他成员，即ZO-2和ZO-3相互作用，据报道，ZO-2和ZO-3与C×36共同定位于小鼠视网膜的缝隙连接。转染C×36的HeLa细胞和培养的βTC-3细胞均表达ZO-2和ZO-3，并且这两种ZO蛋白均与C×36共定位于细胞间的缝隙连接。在C×36转染的HeLa细胞裂解产物中，ZO-2和ZO-3与C×36共沉淀，而C×36缺失SAYV PDZ相互作用基序的细胞不存在C×36/ZO-2结合。体外下拉实验表明，C×36与PDZ1相互作用，但不与ZO-2或ZO-3中的另外两个PDZ结构域相互作用。缺失PDZ结合基序的截短C×36不能结合ZO-2或ZO-3的PDZ1结构域。C×36 C末端的14个氨基酸与ZO-2和ZO-3的PDZ1结构域相互作用，并抑制C×36与这些ZO蛋白的PDZ1结构域的结合。这些结果表明，C×36与ZO-2和ZO-3的第一个PDZ结构域有关，这种联系需要C-末端的SAYV序列。这些发现，再加上ZO-2与包括转录因子在内的各种蛋白质的已知联系，表明ZO-2可能在由C×36组成的缝隙连接处锚定调节蛋白。
The gap junction protein connexin36 (C×36) is widely expressed in neurons and was previously shown to interact with the PDZ domain-containing protein zonula occludens-1 (ZO-1). We investigated whether C×36 is also able to interact with other members of zonula occludens family of proteins, namely, ZO-2 and ZO-3, the former of which was reported to be co-localized with C×36 at gap junctions in mouse retina. HeLa cells transfected with C×36 and cultured βTC-3 cells were found to express ZO-2 and ZO-3, and both of these ZO proteins were co-localized with C×36 at gap junctional cell-cell contacts. In lysates of C×36-transfected HeLa cells, ZO-2 and ZO-3 were shown to co-immunoprecipitate with C×36, whereas C×36/ZO-2 association was absent in cells transfected with truncated C×36 lacking its C-terminus SAYV PDZ interaction motif. In vitro pull-down assays revealed that C×36 interacts with the PDZ1, but not with the other two PDZ domains in ZO-2 or ZO-3. Truncated C×36 lacking its PDZ binding motif failed to bind the PDZ1 domain of either ZO-2 or ZO-3. A fourteen amino acid peptide corresponding to the C-terminus of C×36 was also shown to interact with the PDZ1 domains of ZO-2 and ZO-3, and this peptide inhibited the association of C×36 with the PDZ1 domains of these ZO proteins. These results indicate that C×36 associates with the first PDZ domain of ZO-2 and ZO-3 and that this association requires the C-terminus SAYV sequence in C×36. These findings, together with the known association of ZO-2 with a variety of proteins, including transcription factors, suggest that ZO-2 may serve to anchor regulatory proteins at gap junctions composed of C×36.
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三个紧密连接相关的Maguks ZO-1，ZO-2和ZO-3与Claudins的Cooh Termini直接结合。
DOI：
10.1083/jcb.147.6.1351
发表时间：
1999-12-13
期刊：
The Journal of cell biology
影响因子：
--
作者：
Itoh M;Furuse M;Morita K;Kubota K;Saitou M;Tsukita S
通讯作者：
Tsukita S
影响因子：
4
作者：
Allagnat, F;Martin, D;Haefliger, JA
通讯作者：
Haefliger, JA
影响因子：
25
作者：
Arumugam, H;Liu, XH;Belousov, AB
通讯作者：
Belousov, AB
DOI：
10.1073/pnas.0804793105
发表时间：
2008-08-26
影响因子：
11.1
作者：
Flores, Carmen E.;Li, Xinbo;Pereda, Alberto E.
通讯作者：
Pereda, Alberto E.
影响因子：
5.3
作者：
Martin, AO;Mathieu, MN;Guérineau, NC
通讯作者：
Guérineau, NC