The Premetazoan Ancestry of Cadherins

Abedin, Monika; King, Nicole

doi:10.1126/science.1151084

Cited by 234 publications

(190 citation statements)

References 33 publications

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“…Furthermore, we observed that within a given subfamily, the distribution and pattern of the linker types are generally conserved across species. Remarkably, these Ca 2þ -free linkers are also present in the majority of the choanoflagellate Monosiga brevicollis (M. brevicollis) cadherins (27) (Table S3). Of note, the largest M. brevicollis cadherin, MBCDH18 (27) with 58 EC domains, contains as many as 19 Ca 2þ -free linkers (Fig.…”

Section: Constructsmentioning

confidence: 99%

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Crystal structures of Drosophila N-cadherin ectodomain regions reveal a widely used class of Ca ²⁺ -free interdomain linkers

Jin

Walker

Felsövályi

et al. 2011

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

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Vertebrate classical cadherins mediate selective calcium-dependent cell adhesion by mechanisms now understood at the atomic level. However, structures and adhesion mechanisms of cadherins from invertebrates, which are highly divergent yet function in similar roles, remain unknown. Here we present crystal structures of three-and four-tandem extracellular cadherin (EC) domain segments from Drosophila N-cadherin (DN-cadherin), each including the predicted N-terminal EC1 domain (denoted EC1') of the mature protein. While the linker regions for the EC1'-EC2' and EC3'-EC4' pairs display binding of three Ca 2 ions similar to that of vertebrate cadherins, domains EC2' and EC3' are joined in a "kinked" orientation by a previously uncharacterized Ca 2 -free linker. Biophysical analysis demonstrates that a construct containing the predicted N-terminal nine EC domains of DN-cadherin forms homodimers with affinity similar to vertebrate classical cadherins, whereas deleting the ninth EC domain ablates dimerization. These results suggest that, unlike their vertebrate counterparts, invertebrate cadherins may utilize multiple EC domains to form intercellular adhesive bonds. Sequence analysis reveals that similar Ca 2 -free linkers are widely distributed in the ectodomains of both vertebrate and invertebrate cadherins.

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Section: Constructsmentioning

confidence: 99%

“…Of note, the choanoflagellate M. brevicollis genome contains 23 cadherin genes (27). Among the 19 M. brevicollis cadherins that contain two or more EC domains, 13 are predicted to contain Ca 2þ -free linkers (Table S3).…”

Section: Ca 2þ -Free Linkers May Represent Functionally Important Strmentioning

confidence: 99%

Crystal structures of Drosophila N-cadherin ectodomain regions reveal a widely used class of Ca ²⁺ -free interdomain linkers

Jin

Walker

Felsövályi

et al. 2011

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

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“…Their recent detection in the closest unicellular relatives of metazoans, the choanoflagellates, has highlighted their potential role in the origin of multicellularity (Abedin and King, 2008). Comparative studies on the classic cadherin subfamily has revealed that the structural element called Primitive Classic Cadherin Domain (PCCD) complex, otherwise termed nonchordate classic cadherin domain, is also present in cephalochordates, but has been lost in both tunicates and vertebrates (Oda et al, 2002).…”

Section: Corroborative Evidence For Olfactores Monophylymentioning

confidence: 99%

Additional molecular support for the new chordate phylogeny

Delsuc

Tsagkogeorga

Lartillot

et al. 2008

Genesis

216

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Summary: Recent phylogenomic analyses have suggested tunicates instead of cephalochordates as the closest living relatives of vertebrates. In direct contradiction with the long accepted view of Euchordates, this new phylogenetic hypothesis for chordate evolution has been the object of some skepticism. We assembled an expanded phylogenomic dataset focused on deuterostomes. Maximum-likelihood using standard models and Bayesian phylogenetic analyses using the CAT site-heterogeneous mixture model of amino-acid replacement both provided unequivocal support for the sister-group relationship between tunicates and vertebrates (Olfactores). Chordates were recovered as monophyletic with cephalochordates as the most basal lineage. These results were robust to both gene sampling and missing data. New analyses of ribosomal rRNA also recovered Olfactores when compositional bias was alleviated. Despite the inclusion of 25 taxa representing all major lineages, the monophyly of deuterostomes remained poorly supported. The implications of these phylogenetic results for interpreting chordate evolution are discussed in light of recent advances from evolutionary developmental biology and genomics. genesis 46:592-604, 2008. V V C 2008 Wiley-Liss, Inc.

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“…T he cadherin gene family is hypothesized to have had special importance for metazoan origins (1)(2)(3)(4)(5). Cadherins are cellsurface receptors that function in cell adhesion, cell polarity, and tissue morphogenesis (6)(7)(8).…”

mentioning

confidence: 99%

Origin of metazoan cadherin diversity and the antiquity of the classical cadherin/β-catenin complex

Nichols

Roberts

Richter

et al. 2012

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

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The evolution of cadherins, which are essential for metazoan multicellularity and restricted to metazoans and their closest relatives, has special relevance for understanding metazoan origins. To reconstruct the ancestry and evolution of cadherin gene families, we analyzed the genomes of the choanoflagellate Salpingoeca rosetta, the unicellular outgroup of choanoflagellates and metazoans Capsaspora owczarzaki, and a draft genome assembly from the homoscleromorph sponge Oscarella carmela. Our finding of a cadherin gene in C. owczarzaki reveals that cadherins predate the divergence of the C. owczarzaki, choanoflagellate, and metazoan lineages. Data from these analyses also suggest that the last common ancestor of metazoans and choanoflagellates contained representatives of at least three cadherin families, lefftyrin, coherin, and hedgling. Additionally, we find that an O. carmela classical cadherin has predicted structural features that, in bilaterian classical cadherins, facilitate binding to the cytoplasmic protein β-catenin and, thereby, promote cadherin-mediated cell adhesion. In contrast with premetazoan cadherin families (i.e., those conserved between choanoflagellates and metazoans), the later appearance of classical cadherins coincides with metazoan origins.

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The Premetazoan Ancestry of Cadherins

Cited by 234 publications

References 33 publications

Crystal structures of Drosophila N-cadherin ectodomain regions reveal a widely used class of Ca ²⁺ -free interdomain linkers

Crystal structures of Drosophila N-cadherin ectodomain regions reveal a widely used class of Ca ²⁺ -free interdomain linkers

Additional molecular support for the new chordate phylogeny

Origin of metazoan cadherin diversity and the antiquity of the classical cadherin/β-catenin complex

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The Premetazoan Ancestry of Cadherins

Cited by 234 publications

References 33 publications

Crystal structures of Drosophila N-cadherin ectodomain regions reveal a widely used class of Ca 2+ -free interdomain linkers

Crystal structures of Drosophila N-cadherin ectodomain regions reveal a widely used class of Ca 2+ -free interdomain linkers

Additional molecular support for the new chordate phylogeny

Origin of metazoan cadherin diversity and the antiquity of the classical cadherin/β-catenin complex

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Crystal structures of Drosophila N-cadherin ectodomain regions reveal a widely used class of Ca ²⁺ -free interdomain linkers

Crystal structures of Drosophila N-cadherin ectodomain regions reveal a widely used class of Ca ²⁺ -free interdomain linkers