Identification of three human type-II classic cadherins and frequent heterophilic interactions between different subclasses of type-II classic cadherins

Shimoyama, Yutaka; Tsujimoto, Gozoh; Kitajima, Masaki; NATORI, Michiya

doi:10.1042/bj3490159

Cited by 110 publications

(89 citation statements)

References 27 publications

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“…Other sequences in the extracellular domain, however, vary, and this sequence variation confers the adhesive specificity on each member (Nose et al 1988). For example, E-cadherin preferentially binds E-cadherin, and N-cadherin does so to N-cadherin; although, the degree of the selectivity changes depending on the partners (Shimoyama et al 2000;Patel et al 2006). This nature of classic cadherins has been implicated in the sorting of different cell types (Takeichi 1988).…”

Section: Cadherinsmentioning

confidence: 99%

Adherens Junction: Molecular Architecture and Regulation

Meng¹,

Takeichi²

2009

Cold Spring Harbor Perspectives in Biology

490

449

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Section: Cadherinsmentioning

confidence: 99%

Adherens Junction: Molecular Architecture and Regulation

Meng¹,

Takeichi²

2009

Cold Spring Harbor Perspectives in Biology

490

449

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“…Whereas classical cadherins are primarily homophilic, the degree of heterophilic interaction among them is a controversial issue (2). Whereas some reports indicate exclusively homophilic binding for at least some classical cadherins (31,32), others suggest broad-range cross-reactivity between them, particularly for the type II cadherins (33)(34)(35). To investigate the specificity of interaction between different γ-Pcdh isoforms, we used both our quantitative cell aggregation assay as well as standard qualitative microscopic analysis of aggregates formed by mixing two fluorescently labeled cell groups.…”

Section: γ-Pcdhs Mediate Trans Interactions With Properties Distinct mentioning

confidence: 99%

Combinatorial homophilic interaction between γ-protocadherin multimers greatly expands the molecular diversity of cell adhesion

Schreiner

Weiner

2010

Proc. Natl. Acad. Sci. U.S.A.

223

436

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The specificity of interactions between neurons is believed to be mediated by diverse cell adhesion molecules, including members of the cadherin superfamily. Whereas mechanisms of classical cadherin adhesion have been studied extensively, much less is known about the related protocadherins (Pcdhs), which together make up the majority of the superfamily. Here we use quantitative cell aggregation assays and biochemical analyses to characterize cis and trans interactions among the 22-member γ-Pcdh family, which have been shown to be critical for the control of synaptogenesis and neuronal survival. We show that γ-Pcdh isoforms engage in trans interactions that are strictly homophilic. In contrast to classical cadherins, γ-Pcdh interactions are only partially Ca 2+ -dependent, and their specificity is mediated through the second and third extracellular cadherin (EC) domains (EC2 and EC3), rather than through EC1. The γ-Pcdhs also interact both covalently and noncovalently in the cis-orientation to form multimers both in vitro and in vivo. In contrast to γ-Pcdh trans interactions, cis interactions are highly promiscuous, with no isoform specificity. We present data supporting a model in which γ-Pcdh cistetramers represent the unit of their adhesive trans interactions. Unrestricted tetramerization in cis, coupled with strictly homophilic interactions in trans, predicts that the 22 γ-Pcdhs could form 234,256 distinct adhesive interfaces. Given the demonstrated role of the γ-Pcdhs in synaptogenesis, our data have important implications for the molecular control of neuronal specificity.cadherin | calcium-dependent | synaptogenesis | recognition | trafficking

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“…12,13 As has been demonstrated for type I cadherins, type II cadherins interact with ␣-and ␤-catenins. 14 Using an L-fibroblast cDNA transfection system and a long-term cell-aggregation assay, Shimoyama et al 15 clearly demonstrated that all 8 type II cadherins exhibited cell-cell binding activity comparable to that of E-cadherin. Heterophilic interactions among the type II cadherins were frequently observed, whereas each type I cadherin subtype has a unique binding specificity that confers specific cell-adhesive properties on the cells in which it is expressed (homophilic interaction).…”

mentioning

confidence: 99%

Expression of cadherin‐8 in renal cell carcinoma and fetal kidney

Blaschke

Mueller

Marković-Lipkovski

et al. 2002

Intl Journal of Cancer

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Renal cell carcinomas (RCCs) represent 3% of all adult malignancies and are often associated with poor prognosis due to early metastasis and limited beneficial effects of current therapeutic modalities. 1 Most of these tumors originate from the proximal tubule. According to cell morphology and growth pattern, 3 main histologic tumor types can be distinguished, including clear cell carcinoma, papillary renal carcinoma and chromophobe RCC. 2 Several factors that may contribute to the process of malignant cell transformation in RCC have previously been characterized, including physical agents, chemical agents, habits, genetics (chromosomal rearrangement) and end-stage renal disease. 3 However, the pathogenic mechanisms that promote tumor progression, i.e., tumor invasion and metastasis, still have to be defined. There is accumulating evidence that cadherins may be involved in the pathogenesis of various human carcinomas by modulating celladhesive properties.The cadherin superfamily represents a group of cell-surface glycoproteins involved in cell recognition, cell signaling, cell communication, morphogenesis as well as angiogenesis and includes the groups of classic cadherins, desmosomal cadherins, protocadherins, 7TM-cadherins and T-cadherin. 4 The human classic cadherins are a group of cell-surface molecules mediating Ca 2ϩ -dependent cell adhesion by homo-or heterophilic interaction. These proteins, m.w. approximately 120 -130 kDa, are composed of an extracellular domain with 5 subdomains, each of which contains a cadherin-specific motif at the N-terminal site, a single transmembrane domain and a rather short and highly conserved cytoplasmic domain at the C-terminal site. The adhesive action of cadherins depends on the presence of Ca 2ϩ and on the function of the intracellular domain. 5 Cadherins are linked to the actin filament network through cytoplasmic interactions with catenins. These catenins regulate cadherin-mediated cell-cell adhesion. 6 In addition, these molecules may function as a downstream transcriptional activator. 7,8 More than 12 different molecules of the classic human cadherins have been identified so far by cDNA cloning. With respect to sequence homology and conservation of several amino acid residue motifs in the extracellular domain, Suzuki et al. 9 first proposed subdividing the classic human cadherins into 2 subgroups: type I (E-, N-and P-cadherins, cadherin-4) and type II (cadherins 5-15). Cadherin-8, a type II cadherin, was cloned by Tanihara et al. 10 and is characterized by strong sequence homology with the classical type I cadherins. 11 In mice, cadherin-8 expression is restricted to the developing CNS and thymus. 12,13 As has been demonstrated for type I cadherins, type II cadherins interact with ␣-and ␤-catenins. 14 Using an L-fibroblast cDNA transfection system and a long-term cell-aggregation assay, Shimoyama et al. 15 clearly demonstrated that all 8 type II cadherins exhibited cell-cell binding activity comparable to that of E-cadherin. Heterophilic interactions among the type I...

show abstract

Identification of three human type-II classic cadherins and frequent heterophilic interactions between different subclasses of type-II classic cadherins

Cited by 110 publications

References 27 publications

Adherens Junction: Molecular Architecture and Regulation

Adherens Junction: Molecular Architecture and Regulation

Combinatorial homophilic interaction between γ-protocadherin multimers greatly expands the molecular diversity of cell adhesion

Expression of cadherin‐8 in renal cell carcinoma and fetal kidney

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