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1 Department of Molecular Biology and Biochemistry, Osaka Graduate School of Medicine/Faculty of Medicine, Suita 565-0871, Osaka, Japan
2 Division of Molecular and Cellular Biology, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine/Faculty of Medicine, Kobe 650-0017, Hyogo, Japan
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Abstract |
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Introduction |
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The major cell adhesion molecules (CAMs) at TJs are claudin, occludin, and junctional adhesion molecule (JAM) (Tsukita et al. 2001). Claudin is a Ca2+-independent CAM with four transmembrane segments and comprises a family with over 20 members. Claudin forms TJ strands to seal the apposed plasma membranes of adjacent cells. The structure of occludin is similar to that of claudin, but its function has not yet been established. JAM is a Ca2+-independent immunoglobulin-like CAM with a single transmembrane segment and comprises a family with four members. These CAMs are associated with the actin cytoskeleton through ZO-1, -2, and -3. In addition, JAM binds the cell polarity complex consisting of Par-3, -6, and aPKC and is involved in the formation of TJs at the apical side of AJs. However, it still remains unknown how TJs are formed at the apical side of AJs.
At AJs, cadherin and nectin are two major CAMs (Takeichi 1991; Takai et al. 2003). Cadherin is a key Ca2+-dependent CAM with a single transmembrane segment and comprises a family with over 80 members (Takeichi 1991; Yagi & Takeichi 2000). E-Cadherin expressed in epithelial cells directly binds β-catenin, which in turn interacts with 
-catenin, resulting in the association of E-cadherin with the actin cytoskeleton (Takeichi 1991; Tepass et al. 2000; Thiery 2002). Nectin is a Ca2+-independent immunoglobulin-like CAM with a single transmembrane segment and comprises a family with four members (Takai et al. 2003). Nectin binds afadin through which it is associated with the actin cytoskeleton.
Nectin initiates cell–cell adhesion and then recruits E-cadherin to the nectin-based cell–cell contact sites to form AJs. It also first recruits JAM and then claudin and occludin to the apical side of AJs, eventually resulting in the formation of TJs. Afadin, catenins, and the actin cytoskeleton associated with them are essential for the recruitment of E-cadherin to the nectin-based cell–cell adhesion sites, whereas afadin, ZOs, and the actin cytoskeleton associated with them are essential for the recruitment of JAM, claudin, and occludin to the apical side of the nectin-based cell–cell adhesion sites. Accumulating evidence has shown that the formation of cadherin-based AJs is not essential for the formation of TJs (Harris & Peifer 2004; Okamoto et al. 2005; Yamada et al. 2006; Capaldo & Macara 2007), although circumstantial evidence had led to the belief that the establishment of cadherin-based AJs is a prerequisite for the formation of TJs (Gumbiner et al. 1988).
To understand the molecular mechanisms underlying the formation of the junctional complexes of AJs and TJs, we expressed various combinations of CAMs of AJs and TJs in murine L fibroblasts and analyzed the resulting cell–cell adhesion membrane domains. Murine L cells endogenously express nectin-1, -2, and JAM-A to very small extents but express no cadherin or claudin and do not have AJs or TJs (Nagafuchi et al. 1987; Sakisaka et al. 2001; Morris et al. 2006). Here, we demonstrated the novel role of nectin in the co-localization of JAM and claudin at the same cell–cell adhesion membrane domain.
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Results |
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When each of the AJ and TJ CAMs, nectin-3, E-cadherin, JAM-A, and claudin-1, was expressed in L cells, each cell line (Nectin-3-L, E-Cadherin-L, JAM-A-L, and Claudin-1-L cells, respectively) formed cell–cell adhesion based on each CAM (Fig. 1A–D), consistent with earlier observations (Nagafuchi et al. 1987; Furuse et al. 1998b; Satoh-Horikawa et al. 2000; Itoh et al. 2001). We defined cell–cell adhesion area based on each CAM, of which immunofluorescence signal is concentrated at cell–cell contact sites, as a cell–cell adhesion membrane domain. We then co-expressed one of the AJ CAMs and one of the TJ CAMs in L cells and prepared four L cell lines, Nectin-3-JAM-A-L (co-expressing nectin-3 and JAM-A), E-Cadherin-JAM-A-L (co-expressing JAM-A and E-cadherin), Nectin-3-Claudin-1-L (co-expressing nectin-3 and claudin-1), and E-Cadherin-Claudin-1-L (co-expressing E-cadherin and claudin-1) cells. In all of these cell lines, the immunofluorescence signals for each TJ CAM and each AJ CAM localized at the cell–cell contact sites and were distinctly separated from one another, although these signals appeared to partially overlap (Fig. 2A–D). These results indicate that each combination of one of the AJ CAMs and one of the TJ CAMs forms separate cell–cell adhesion membrane domains, consistent with the localization of their endogenous molecules in epithelial cells (Furuse et al. 1998a; Takahashi et al. 1999; Itoh et al. 2001).
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Induction by nectin-3 of the co-localization of JAM-A and claudin-1 at the same cell–cell adhesion membrane domain
When nectin-3 was additionally co-expressed in JAM-A-Claudin-1-L cells (Nectin-3-JAM-A-Claudin-1-L cells), all the three immunofluorescence signals were concentrated at the cell–cell contact sites: the signals for JAM-A and claudin-1 definitely overlapped with each other, although they appeared to partially overlap with that for nectin-3, which was distinctly separated from those for JAM-A and claudin-1 (Fig. 3A). When E-cadherin was additionally co-expressed in JAM-A-Claudin-1-L cells (E-Cadherin-JAM-A-Claudin-1-L cells), all the three signals were concentrated at the cell–cell contact sites (Fig. 3B). Although these three signals appeared to partially overlap, they were distinctly separated from each other and the signals for JAM-A and claudin-1 definitely did not overlap. These results indicate that the CAMs at TJs, JAM-A and claudin-1, alone do not efficiently co-localize with one another and that nectin-3, but not E-cadherin, is required for this co-localization, although nectin-3 itself does not co-localize with JAM-A or claudin-1.
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We finally examined whether afadin is necessary for the nectin-3-induced co-localization of JAM-A and claudin-1 at the same cell–cell adhesion membrane domain. When afadin was knocked down in Nectin-3-JAM-A-Claudin-1-L cells, the amount of afadin protein decreased to approximately 40% of that of the control level as estimated by Western blotting (Fig. 4Aa). The amount of nectin-3, JAM-A, claudin-1, ZO-1, or actin protein did not change. Consistent with this, the immunofluorescence signal for afadin was markedly reduced and was not concentrated at the cell–cell contact sites in afadin-knock down cells (Fig. 4Ab1 and Ab2). The signal for nectin-3 was concentrated at the cell–cell contact sites in the afadin-knock down cells. The signals for JAM-A and claudin-1 were also concentrated at the cell–cell contact sites, but the signals for JAM-A and claudin-1 were distinctly separated from each other, although these signals appeared to partially overlap (Fig. 4Ba and Bb). These results indicate that afadin is necessary for the nectin-induced co-localization of two TJ CAMs at the same cell–cell adhesion membrane domain.
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Discussion |
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-catenin are endogenously expressed in L cells, but the amounts of β-catenin and -catenin are reduced because these proteins are unstable in the absence of cadherin and therefore degraded (Tachibana et al. 2000; Yokoyama et al. 2001). However, when E-cadherin is expressed in L cells, the amounts of β-catenin and -catenin are restored. When one of the AJ CAMs (nectin-3 or E-cadherin) and one of the TJ CAMs (JAM-A or claudin-1) were co-expressed in L cells, all combinations formed separate cell–cell adhesion membrane domains, although they appeared to partially overlap. These results indicate that TJ CAMs and AJ CAMs do not substantially merge at cell–cell contact sites.
We previously showed that endogenous nectin and cadherin molecules co-localize at AJs in both fibroblasts and epithelial cells and that the association between nectin and cadherin molecules is physically mediated by afadin, -catenin, and their binding proteins (Takahashi et al. 1999; Tachibana et al. 2000; Pokutta et al. 2002). When nectin-3 and E-cadherin were co-expressed in L cells, these two CAMs merged at cell–cell contact sites and formed the same cell–cell adhesion membrane domain. This result was consistent with our earlier observations (Takahashi et al. 1999; Tachibana et al. 2000). On the other hand, it has been previously reported that JAM-A and claudins, such as claudin-3 and -4, co-localize at TJs in epithelial cells and that both TJ CAMs interact with ZO proteins through their cytoplasmic tails (Itoh et al. 2001; Matsuda et al. 2004). In their freeze-fracture replica electron microscopic examination using epithelial cells, the immunogold signal for JAM-A was associated with the structures of TJ strands (Itoh et al. 2001). However, when JAM-A and claudin-1 were co-expressed in L cells, these two CAMs did not merge at the cell–cell contact sites and formed separate membrane domains. On the other hand, when nectin-3 or E-cadherin was additionally co-expressed in JAM-A-Claudin-1-L cells, nectin-3, but not E-cadherin, induced the co-localization of JAM-A and claudin-1 at the same cell–cell adhesion membrane domain. These results indicate that nectin plays a novel role in the co-localization of JAM and claudin at the same cell–cell adhesion membrane domain.
Afadin-null mice become embryonically lethal, because their embryos show developmental defects at stages during and after gastrulation (Ikeda et al. 1999; Zhadanov et al. 1999). The developmental defects are caused by the failure of the formation of normal AJs and TJs. Essentially the same results were obtained from afadin-null embryoid bodies, which were generated from afadin-null embryonic stem cells (Ikeda et al. 1999; Komura et al. 2008). In addition, afadin-knock down in MDCK cells inhibits not only the formation of AJs but also TJs (Sato et al. 2006). The recruitment of JAM-A to the apical side of the nectin-based cell–cell adhesion sites is mediated by the interaction between afadin and ZO-1 (Fukuhara et al. 2002). Consistent with these earlier observations, we found here that afadin is necessary for the nectin-3-induced co-localization of JAM-A and claudin-1 at the same cell–cell adhesion domain in L cells.
It remains unclear how nectin-3 induces the co-localization of JAM-A and claudin-1 at the same cell–cell adhesion membrane domain, but not only afadin but also ZO-1 may be involved in this ability of nectin-3, because afadin and ZO-1 directly interact with one another (Yamamoto et al. 1997). Although ZO-1 interacts with both claudin-1 and JAM-A, ZO-1 alone cannot make both molecules co-localize. Because the knock-down of afadin inhibited the ability of nectin-3, afadin, which interacts with nectin-3, may concentrate both the claudin-1–ZO-1 and the JAM-A–ZO-1 complexes at the same cell–cell adhesion membrane domain through the direct interaction of afadin with ZO-1. In addition, afadin and ZO-1 interact indirectly through the actin cytoskeleton associated with afadin and re-organized by the nectin-induced activation of Rac and Cdc42 small G proteins (Yamada et al. 2004; Kawakatsu et al. 2005). These micro-domain structures at the peripheral membrane region induced by the nectin-based cell–cell adhesion may efficiently induce the co-localization of JAM and claudin at the same cell–cell adhesion membrane domain, although this domain is formed separately at the site different from the nectin-induced cell–cell adhesion membrane domain.
TJs are formed at the apical side of AJs in epithelial cells (Farquhar & Palade 1963), but the molecular mechanism of this apico-basal alignment remains unknown. The apico-basal length of fibroblasts is not long enough and the apico-basal cell polarity is not markedly developed compared to that of epithelial cells. In addition, although TJs and AJs are continuously and circumferentially connected along cell–cell contact sites and observed as a belt-like structure in epithelial cells, the cell–cell adhesion membrane domains produced by exogenous CAM(s) in L cells are discontinuous. Our series of studies showed that the nectin-afadin system has a critical role not only in the formation of AJs but also of TJs. However, further studies are necessary for a better understanding of the molecular mechanisms of the apico-basal cell polarization in epithelial cells.
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Experimental procedures |
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The cDNA fragment of nectin-3 was prepared as previously described (Satoh-Horikawa et al. 2000; Takekuni et al. 2003) and subcloned into the pCAGIZeo vector (pCAGIZeo-nectin-3). Similarly, the cDNA fragment of human JAM-A obtained from Dr Toru Kita (Kyoto University, Kyoto, Japan) was subcloned into the pCAGIZeo vector (pCAGIZeo-JAM-A).
Cell culture and transfection
Wild-type L, JAM-A-L, Claudin-1-L, E-Cadherin-L, and E-Cadherin-Claudin-1-L cells were kindly supplied by the late Dr Shoichiro Tsukita (Kyoto University, Kyoto, Japan). L cells were maintained in Dulbecco's modified Eagle's medium supplemented with 10% fetal calf serum. Nectin-3-L cells were prepared as previously described (Satoh-Horikawa et al. 2000). Nectin-3-E-Cadherin-L cells were prepared as previously described (Hoshino et al. 2004). To establish JAM-A-E-Cadherin-L, JAM-A-Claudin-1-L, and E-Cadherin-JAM-A-Claudin-1-L cells, pCAGIZeo-JAM-A was transfected into E-Cadherin-L, Claudin-1-L, and E-Cadherin-Claudin-1-L cells, respectively. To establish Nectin-3-JAM-A-L, Nectin-3-Claudin-1-L, and Nectin-3-JAM-A-Claudin-1-L cells, pCAGIZeo-nectin-3 was transfected into JAM-A-L, Claudin-1-L, and JAM-A-Claudin-1-L cells, respectively. All transfections were performed using Lipofectamine and Plus reagents (Invitrogen) and transfected cells were selected by Zeocin (InvivoGen).
Antibodies
A mouse anti-afadin monoclonal antibody (mAb) was prepared as described (Sakisaka et al. 1999). A rat anti-nectin-3 mAb was prepared as described (Satoh-Horikawa et al. 2000). A rat anti-E-cadherin mAb was supplied by Dr Masatoshi Takeichi (Center for Developmental Biology, RIKEN, Kobe, Japan). A rabbit anti-JAM-A polyclonal antibody (pAb), anti-claudin-1 pAb, and anti-ZO-1 pAb were purchased from Zymed Laboratories Inc. A mouse anti-ZO-1 mAb was purchased from Sanko Junyaku. A mouse anti-JAM1 (JAM-A) mAb and goat anti-nectin-3 pAb were purchased from Santa Cruz Biotechnology. A mouse anti-Actin mAb was purchased from Chemicon. Horseradish peroxidase-conjugated secondary antibodies (Abs) were purchased from GE Healthcare. Fluorophore (FITC, Cy3, and Cy5)-conjugated secondary Abs were purchased from Chemicon and Jackson Immuno Research.
Immunofluorescence microscopy
Cells (1 x 105) were plated on coverslips in 24-well culture dishes. After 72-h, the cells were fixed in a mixture of 50% acetone and 50% methanol at –20 °C for 1 min. They were then washed twice with PBS, incubated with 1% BSA in PBS for 1 h, and then incubated with primary Abs for 1 h in a moist chamber. After washing three times with PBS, the cells were incubated with the appropriate fluorophore-conjugated secondary Abs for 30 min. Finally, they were washed three times with PBS and then mounted in Prolong Gold mount gel (Invitrogen). The samples were analyzed by digital eclipse C1si-ready confocal laser-scanning microscopy (NIKON).
siRNA experiments
For RNAi knock down, a double-stranded 21-nucleotide RNA duplex to afadin (5'-GAUUGGACAUUGAUGAGAATT-3') and a similar duplex to luciferase (5'-CGUACGCGGAAUAC UUCGATT-3') with no significant homology to any known mammalian gene sequences (control) were purchased from Sigma Genosys. The transfection of siRNA was performed using Lipofectamine RNAiMax reagent (Invitrogen) according to manufacturer's protocols.
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Acknowledgements |
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Footnotes |
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* Correspondence: ytakai{at}med.kobe-u.ac.jp
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References |
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Accepted: 30 April 2008
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