Molecular evolution of the cadherin superfamily Export

@article{citeulike:4006135, abstract = {This review deals with the large and pleiotropic superfamily of cadherins and its molecular evolution. We compiled literature data and an in-depth phylogenetic analysis of more than 350 members of this superfamily from about 30 species, covering several but not all representative branches within metazoan evolution. We analyzed the sequence homology between either ectodomains or cytoplasmic domains, and we reviewed protein structural data and genomic architecture. Cadherins and cadherin-related molecules are defined by having an ectodomain in which at least two consecutive calcium-binding cadherin repeats are present. There are usually 5 or 6 domains, but in some cases as many as 34. Additional protein modules in the ectodomains point at adaptive evolution. Despite the occurrence of several conserved motifs in subsets of cytoplasmic domains, these domains are even more diverse than ectodomains and most likely have evolved separately from the ectodomains. By fine tuning molecular classifications, we reduced the number of solitary superfamily members. We propose a cadherin major branch, subdivided in two families and 8 subfamilies, and a cadherin-related major branch, subdivided in four families and 11 subfamilies. Accordingly, we propose a more appropriate nomenclature. Although still fragmentary, our insight into the molecular evolution of these remarkable proteins is steadily growing. Consequently, we can start to propose testable hypotheses for structure–function relationships with impact on our models of molecular evolution. An emerging concept is that the ever evolving diversity of cadherin structures is serving dual and important functions: specific cell adhesion and intricate cell signaling.}, author = {Hulpiau, P. and Vanroy, F.}, citeulike-article-id = {4006135}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.biocel.2008.09.027}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S1357272508004044}, doi = {10.1016/j.biocel.2008.09.027}, issn = {13572725}, journal = {The International Journal of Biochemistry \& Cell Biology}, keywords = {adhesion, cadherins, evolution}, month = {February}, number = {2}, pages = {349--369}, posted-at = {2009-02-04 07:50:22}, priority = {2}, title = {Molecular evolution of the cadherin superfamily}, url = {http://dx.doi.org/10.1016/j.biocel.2008.09.027}, volume = {41}, year = {2009} }

TY - JOUR ID - citeulike:4006135 L3 - citeulike-article-id:4006135 N2 - This review deals with the large and pleiotropic superfamily of cadherins and its molecular evolution. We compiled literature data and an in-depth phylogenetic analysis of more than 350 members of this superfamily from about 30 species, covering several but not all representative branches within metazoan evolution. We analyzed the sequence homology between either ectodomains or cytoplasmic domains, and we reviewed protein structural data and genomic architecture. Cadherins and cadherin-related molecules are defined by having an ectodomain in which at least two consecutive calcium-binding cadherin repeats are present. There are usually 5 or 6 domains, but in some cases as many as 34. Additional protein modules in the ectodomains point at adaptive evolution. Despite the occurrence of several conserved motifs in subsets of cytoplasmic domains, these domains are even more diverse than ectodomains and most likely have evolved separately from the ectodomains. By fine tuning molecular classifications, we reduced the number of solitary superfamily members. We propose a cadherin major branch, subdivided in two families and 8 subfamilies, and a cadherin-related major branch, subdivided in four families and 11 subfamilies. Accordingly, we propose a more appropriate nomenclature. Although still fragmentary, our insight into the molecular evolution of these remarkable proteins is steadily growing. Consequently, we can start to propose testable hypotheses for structure–function relationships with impact on our models of molecular evolution. An emerging concept is that the ever evolving diversity of cadherin structures is serving dual and important functions: specific cell adhesion and intricate cell signaling. IS - 2 JF - The International Journal of Biochemistry & Cell Biology SN - 13572725 EP - 369 TI - Molecular evolution of the cadherin superfamily VL - 41 SP - 349 KW - adhesion KW - cadherins KW - evolution AU - Hulpiau, P AU - Vanroy, F PY - 2009/02// UR - http://dx.doi.org/10.1016/j.biocel.2008.09.027 ER -