Phylogenetic analysis of the cadherin superfamily

Pouliot, Yannick

doi:10.1002/bies.950141104

Cited by 51 publications

(35 citation statements)

References 36 publications

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“…In contrast to classic cadherins, which bind catenins by the cytoplasmic domains and have genes with as much as 12 introns, nonclassic cadherins do not interact with catenins and genes have many fewer introns (485). Phylogenetic analyses suggest that there are four paralogous subfamilies (E-, N-, P-, and R-cadherins) of vertebrate classic cadherin proteins (168) and that these genes duplicated early in evolution (362).…”

Section: B Evolution Of Junction Proteinsmentioning

confidence: 99%

Cell Adhesion, Polarity, and Epithelia in the Dawn of Metazoans

Cereijido

Contreras

Shoshani

2004

Physiological Reviews

151

100

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Transporting epithelia posed formidable conundrums right from the moment that Du Bois Raymond discovered their asymmetric behavior, a century and a half ago. It took a century and a half to start unraveling the mechanisms of occluding junctions and polarity, but we now face another puzzle: lest its cells died in minutes, the first high metazoa (i.e., higher than a sponge) needed a transporting epithelium, but a transporting epithelium is an incredibly improbable combination of occluding junctions and cell polarity. How could these coincide in the same individual organism and within minutes? We review occluding junctions (tight and septate) as well as the polarized distribution of Na+-K+-ATPase both at the molecular and the cell level. Junctions and polarity depend on hosts of molecular species and cellular processes, which are briefly reviewed whenever they are suspected to have played a role in the dawn of epithelia and metazoan. We come to the conclusion that most of the molecules needed were already present in early protozoan and discuss a few plausible alternatives to solve the riddle described above.

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Section: B Evolution Of Junction Proteinsmentioning

confidence: 99%

Cell Adhesion, Polarity, and Epithelia in the Dawn of Metazoans

Cereijido

Contreras

Shoshani

2004

Physiological Reviews

151

100

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“…rMEGF1, rat multiple EGF-like motifs containing protein; rLAMA2, rat laminin ␣2 chain; N1␤, neurexin 1␤. these genes duplicated early in evolution (32). The conservation of intron positions among classic cadherins suggests that there was a constraint on unequal crossing-over among these genes (9).…”

Section: Phylogenetic Analysis Of Protocadherinmentioning

confidence: 99%

Large exons encoding multiple ectodomains are a characteristic feature of protocadherin genes

Wu¹

2000

Proceedings of the National Academy of Sciences

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Recent studies revealed a striking difference in the genomic organization of classic cadherin genes and one family of ''nonclassic cadherin'' genes designated protocadherins. Specifically, the DNA sequences encoding the ectodomain repeats of classic cadherins are interrupted by multiple introns. By contrast, all of the encoded ectodomains of each member of the protocadherin gene clusters are present in one large exon. To determine whether large ectodomain exons are a general feature of protocadherin genes we have investigated the genomic organization of several additional human protocadherin genes by using DNA sequence information in GenBank. These genes include protocadherin 12 (Pcdh12), an ortholog of the mouse vascular endothelial cadherin-2 gene; hFmi1 and hFmi2, homologs of the Drosophila planar cell polarity gene, flamingo; hFat2, a homolog of the Drosophila tumor suppressor gene fat; and the Drosophila DN-cadherin and DE-cadherin genes. Each of these genes was found to be a member of the protocadherin subfamily, based on amino acid sequence comparisons of their ectodomains. Remarkably, all of these protocadherin genes share a common feature: most of the genomic DNA sequences encoding their ectodomains are not interrupted by an intron. We conclude that the presence of unusually large exons is a characteristic feature of protocadherin genes.

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“…In this context, it might be of interest that the molecular structure of N-cadherin is also relatively highly conserved between these two species (Miyatani et al, 1989;Pouliot, 1992).…”

Section: Restricted Expression Of N-cadherinmentioning

confidence: 99%

Expression of N‐cadherin mRNA during development of the mouse brain

Redies

Takeichi

1993

Developmental Dynamics

109

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The expression of N-cadherin mRNA was mapped in the brain of mice between embryonic day 12 (E12) and the adult stage by in situ hybridization of digoxigenin-labeled riboprobe. Two phases of N-cadherin expression can be distinguished. During the first phase (about E l 2 to E16), expression is ubiquitous throughout the brain and most prominent in the proliferative neuroepithelium. During the second phase (about El6 to postnatal day 6), N-cadherin expression is restricted to particular nuclei or laminae that share common functional features and neuroanatomical connections. Several of the N-cadherinpositive structures receive direct afferents from retinal ganglion cells or from the superior colliculus. Others belong to the reticular system and to the limbic system of the brain. In neocortex, N-cadherin is expressed by deeper layer cells. In the adult brain, only low levels of N-cadherin expression remain in very few types of cells, for example in the Purkinje cells of the cerebellum.These results are similar to data from chicken brain and suggest that the generalized expression of N-cadherin during the early phase and the restriction expression of this molecule in particular functional systems during the later phase is, at least in part, phylogenetically conserved between chicken and mouse. Moreover, the results show that N-cadherin expression extends to phylogenetically newer structures, e.g., the mammalian neocortex. 0 1993 Wiley-Liss, Inc.

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Phylogenetic analysis of the cadherin superfamily

Cited by 51 publications

References 36 publications

Cell Adhesion, Polarity, and Epithelia in the Dawn of Metazoans

Cell Adhesion, Polarity, and Epithelia in the Dawn of Metazoans

Large exons encoding multiple ectodomains are a characteristic feature of protocadherin genes

Expression of N‐cadherin mRNA during development of the mouse brain

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