人类ZO-1蛋白第二个PDZ结构域的溶液结构与功能
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摘要
细胞连接是存在于多细胞动物细胞间的一种特化结构,多存在于上皮组织。在脊椎动物上皮组织中,主要有三类细胞连接:紧密连接,粘性连接和间隙连接。每一种连接在形态、位置与功能上都各有不同。紧密连接在位置上是这三种连接上最靠近极性上皮细胞顶膜的,也是将相邻的细胞膜连的最为紧密的。功能上紧密连接负责控制小分子和离子在细胞间通路的通过,同时作为屏障阻碍细胞侧膜上膜蛋白在细胞顶膜和基底膜之间的流动从而维持上皮细胞的极性。粘性连接在位置上位于紧密连接之下,对相邻细胞的连接也没有紧密连接那么紧,粘性连接处的细胞间距在10-20纳米。缝隙连接又成为通讯连接,通过由connexin组成六聚体connexon彼此对接形成胞间通道,从而参与突触电信号的传递和胞间营养物质的共享等重要生命活动。
ZO1蛋白首先在紧密连接中被发现,它在细胞膜处同构成紧密连接的主要的跨膜蛋白Claudins, occludin以及JAM等都有相互作用,在胞内又同细胞骨架蛋白以及一些核酸结合蛋白相互作用。ZO1在调节紧密连接的建立,细胞内信号的传递方面起着重要作用。同时,在缺乏紧密连接的细胞中也发现了ZO1蛋白,如粘性连接处和缝隙连接处。在粘性连接处,ZO1同链蛋白等粘性连接的主要组成部分catenin等有相互作用;在缝隙连接处,ZO1同多种连接子蛋白connexin相互作用,调节connexin在细胞质和细胞膜之间的分不平衡进而调控缝隙连接斑块的大小。
我们的工作中,利用核磁共振波谱学(NMR)的方法解析了人类ZO1蛋白第二个PDZ结构域(ZO1PDZ2)的溶液结构。ZO1PDZ2为结构域交换的二体,通过将二体中每条多肽链N端的20个残基彼此交换形成非常稳定的同二聚体。这种同二聚体保留了PDZ结构域同配基相互作用所学要的位于α2与β2之间的疏水口袋。
我们利用NMR化学位移扰动的方法以及等温量热实验进一步研究了ZO1PDZ2同其配基的相互作用,发现ZO1PDZ2表现出了II型PDZ结构域的结合特征,选择C端0位和-2位为疏水氨基酸残基的小肽相互作用。同时,我们确认了Cx45可以通过它的C端同ZO1相互作用,并将之前认为的Cx45的作用范围,即PDZ1-PDZ2精确到了PDZ2。此外,我们还发现ZO1PDZ2可以同Cx25和Cx59的C端小肽相互作用,这两种相互作用是没有文献报道过的,它们的生理学意义还有待进一步的实验发掘。
通过插入突变实验,我们成功的在ZO1PDZ2的第22位缬氨酸之前插入了1-6氨基酸不等,其中当插入氨基酸达到3个或3个以上时,ZO1PDZ2会从同二聚体被突变成单体,分子量的确定是通过分子筛实验和沉降速率分析型超离心实验完成的。这种从二体到单体的突变成功为我们揭示出了ZO1PDZ2不同于经典PDZ结构域的单体构象而形成二体构象的原因。第22位缬氨酸刚好位于ZO1PDZ2按经典PDZ结构域定义的β2和β3之间,这里的残基较其他PDZ结构域少形成转角较难,所以β2同β3没有形成反平行的折叠片,而形成了一条连续的两倍长度的β链。ZO1PDZ2突变后的单体保留了同Cx43的相互作用,但相互作用强度大大减弱;同时该突变体不再能够同ZO2PDZ2以及ZO3PDZ2相互作用。
找到了ZO1PDZ2形成二体的原因有利于我们进一步研究ZO1PDZ2在细胞内的功能。我们构建了全长ZO1的突变体,该突变体的PDZ2结构域被引入了如前所述的插入突变,因此ZO1突变体不再能够通过PDZ2二聚。MDCK细胞在紧密连接建立初期,其跨膜电阻(TER)曲线会经历依次迅速增高再回落,而ZO1缺失的细胞的TER曲线则一直较为平缓。我们将野生型ZO1及其突变体转染到内源ZO1被沉默的MDCK细胞中并们发现,野生型ZO1使得平缓TER曲线恢复了先迅速升高再降低的特点,而ZO1突变体没有这个能力。因此,我们认为ZO1蛋白中其PDZ2结构域的二聚对于紧密连接的建立是必须的。
Cell junctions exist within the tissue of a multicellular organism as a specialized structure. They are especially abundant in epithelial tissues. In vertebrates, there are three major types of cell junctions, which are tight jucntion (TJ), adherent junction (AJ) and gap junction (GJ). All the three junctions differ from each other in their morphous, location and function. TJs locate most apical in the lateral membrane, they connect the two adjencent cells tightly. TJ function as gate to regulate the ion and small molecule to pass through intercellular pathway. Furthermore, TJ maintain the polarity of epithelial cells by separating transmembrane proteins. AJ locates near TJ in epithelial cells, and will leave a 10-20 nm space between the adjacent cells. GJ is constituted by two anchored connexon which contains 6 connexins. As a channel, GJ allows the sharing of signals and nutrition between connecting cells.
Zonular occludens 1(ZO1) was found in TJs, and later in AJs and GJs. As a scaffolding protein, ZO1 binds directly with caludins, occlundin and JAMs to regulate TJs. Also ZO1 associats with actin and ZONAB, which implied ZO1 was invovled in cell signaling, proliferation and differentiation. In cells which lack of TJs, ZO1 was found in AJs interacting with catenin. In GJs, many connexins have been reported to interact with ZO1. For examply, Cx43 intheract with ZO1 through its very C-terminal, and the interaction regulate the balance of the amount of Cx43 between GJ plaques and nonjunctional pools.
In our work, we determined the solution structure of the second PDZ domain of ZO1 (ZO1PDZ2) which exhibited a highly stable domain-swapped homodimer form. 20 residues in the N-terminal in one chain swapped into the other chain. The homodiemr is very stable and reserved the hydrophobic pocket for PDZ binding ligands.
By NMR chemical shift perturbation issue and ITC issue, ZO1PDZ2 was found to bind the C-terminal of connexins in a way of type II PDZ domain. Cx25, Cx45 and Cx59 were found to interact with ZO1PDZ2 for the first time, which need to be investigated more by in vivo experiments.
ZO1PDZ2 could be converted to a monomeric form by inserting three or more residues in the middle of its secondβstrand, which implied the mechanism of the domain-swapping in ZO1PDZ2. FPLC issue and SV-AUC issue were employed to measure the molecular weight of ZO1PDZ2 and its mutants. the monomer mutant could bind the C-terminal peptide of Cx43, but in a weaker way. Furthermore, the interaction between ZO1PDZ2 and ZO2PDZ2 or ZO3PDZ2 was also abolished by the insertion mutation.
A ZO1 mutant with an insertion into its PDZ2 domain was generated and in vivo investigations were carried out using transepithelial electrical resistance experiments in Madin-Darby canine kidney cells. The result indicated that, unlike expression of wild-type ZO1, expression of the ZO1 mutant could not rescue the delay of TJ assembly caused by endogenous ZO1 knockdown. This is the first direct experimental evidence for the important role of the ZO1 PDZ2 domain in the formation of TJs and these data strongly suggest that the domain-swapping of PDZ2 in vivo is essential for ZO1 functionality in TJ assembly.
ZO1蛋白首先在紧密连接中被发现,它在细胞膜处同构成紧密连接的主要的跨膜蛋白Claudins, occludin以及JAM等都有相互作用,在胞内又同细胞骨架蛋白以及一些核酸结合蛋白相互作用。ZO1在调节紧密连接的建立,细胞内信号的传递方面起着重要作用。同时,在缺乏紧密连接的细胞中也发现了ZO1蛋白,如粘性连接处和缝隙连接处。在粘性连接处,ZO1同链蛋白等粘性连接的主要组成部分catenin等有相互作用;在缝隙连接处,ZO1同多种连接子蛋白connexin相互作用,调节connexin在细胞质和细胞膜之间的分不平衡进而调控缝隙连接斑块的大小。
我们的工作中,利用核磁共振波谱学(NMR)的方法解析了人类ZO1蛋白第二个PDZ结构域(ZO1PDZ2)的溶液结构。ZO1PDZ2为结构域交换的二体,通过将二体中每条多肽链N端的20个残基彼此交换形成非常稳定的同二聚体。这种同二聚体保留了PDZ结构域同配基相互作用所学要的位于α2与β2之间的疏水口袋。
我们利用NMR化学位移扰动的方法以及等温量热实验进一步研究了ZO1PDZ2同其配基的相互作用,发现ZO1PDZ2表现出了II型PDZ结构域的结合特征,选择C端0位和-2位为疏水氨基酸残基的小肽相互作用。同时,我们确认了Cx45可以通过它的C端同ZO1相互作用,并将之前认为的Cx45的作用范围,即PDZ1-PDZ2精确到了PDZ2。此外,我们还发现ZO1PDZ2可以同Cx25和Cx59的C端小肽相互作用,这两种相互作用是没有文献报道过的,它们的生理学意义还有待进一步的实验发掘。
通过插入突变实验,我们成功的在ZO1PDZ2的第22位缬氨酸之前插入了1-6氨基酸不等,其中当插入氨基酸达到3个或3个以上时,ZO1PDZ2会从同二聚体被突变成单体,分子量的确定是通过分子筛实验和沉降速率分析型超离心实验完成的。这种从二体到单体的突变成功为我们揭示出了ZO1PDZ2不同于经典PDZ结构域的单体构象而形成二体构象的原因。第22位缬氨酸刚好位于ZO1PDZ2按经典PDZ结构域定义的β2和β3之间,这里的残基较其他PDZ结构域少形成转角较难,所以β2同β3没有形成反平行的折叠片,而形成了一条连续的两倍长度的β链。ZO1PDZ2突变后的单体保留了同Cx43的相互作用,但相互作用强度大大减弱;同时该突变体不再能够同ZO2PDZ2以及ZO3PDZ2相互作用。
找到了ZO1PDZ2形成二体的原因有利于我们进一步研究ZO1PDZ2在细胞内的功能。我们构建了全长ZO1的突变体,该突变体的PDZ2结构域被引入了如前所述的插入突变,因此ZO1突变体不再能够通过PDZ2二聚。MDCK细胞在紧密连接建立初期,其跨膜电阻(TER)曲线会经历依次迅速增高再回落,而ZO1缺失的细胞的TER曲线则一直较为平缓。我们将野生型ZO1及其突变体转染到内源ZO1被沉默的MDCK细胞中并们发现,野生型ZO1使得平缓TER曲线恢复了先迅速升高再降低的特点,而ZO1突变体没有这个能力。因此,我们认为ZO1蛋白中其PDZ2结构域的二聚对于紧密连接的建立是必须的。
Cell junctions exist within the tissue of a multicellular organism as a specialized structure. They are especially abundant in epithelial tissues. In vertebrates, there are three major types of cell junctions, which are tight jucntion (TJ), adherent junction (AJ) and gap junction (GJ). All the three junctions differ from each other in their morphous, location and function. TJs locate most apical in the lateral membrane, they connect the two adjencent cells tightly. TJ function as gate to regulate the ion and small molecule to pass through intercellular pathway. Furthermore, TJ maintain the polarity of epithelial cells by separating transmembrane proteins. AJ locates near TJ in epithelial cells, and will leave a 10-20 nm space between the adjacent cells. GJ is constituted by two anchored connexon which contains 6 connexins. As a channel, GJ allows the sharing of signals and nutrition between connecting cells.
Zonular occludens 1(ZO1) was found in TJs, and later in AJs and GJs. As a scaffolding protein, ZO1 binds directly with caludins, occlundin and JAMs to regulate TJs. Also ZO1 associats with actin and ZONAB, which implied ZO1 was invovled in cell signaling, proliferation and differentiation. In cells which lack of TJs, ZO1 was found in AJs interacting with catenin. In GJs, many connexins have been reported to interact with ZO1. For examply, Cx43 intheract with ZO1 through its very C-terminal, and the interaction regulate the balance of the amount of Cx43 between GJ plaques and nonjunctional pools.
In our work, we determined the solution structure of the second PDZ domain of ZO1 (ZO1PDZ2) which exhibited a highly stable domain-swapped homodimer form. 20 residues in the N-terminal in one chain swapped into the other chain. The homodiemr is very stable and reserved the hydrophobic pocket for PDZ binding ligands.
By NMR chemical shift perturbation issue and ITC issue, ZO1PDZ2 was found to bind the C-terminal of connexins in a way of type II PDZ domain. Cx25, Cx45 and Cx59 were found to interact with ZO1PDZ2 for the first time, which need to be investigated more by in vivo experiments.
ZO1PDZ2 could be converted to a monomeric form by inserting three or more residues in the middle of its secondβstrand, which implied the mechanism of the domain-swapping in ZO1PDZ2. FPLC issue and SV-AUC issue were employed to measure the molecular weight of ZO1PDZ2 and its mutants. the monomer mutant could bind the C-terminal peptide of Cx43, but in a weaker way. Furthermore, the interaction between ZO1PDZ2 and ZO2PDZ2 or ZO3PDZ2 was also abolished by the insertion mutation.
A ZO1 mutant with an insertion into its PDZ2 domain was generated and in vivo investigations were carried out using transepithelial electrical resistance experiments in Madin-Darby canine kidney cells. The result indicated that, unlike expression of wild-type ZO1, expression of the ZO1 mutant could not rescue the delay of TJ assembly caused by endogenous ZO1 knockdown. This is the first direct experimental evidence for the important role of the ZO1 PDZ2 domain in the formation of TJs and these data strongly suggest that the domain-swapping of PDZ2 in vivo is essential for ZO1 functionality in TJ assembly.
引文
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