Cargando…
Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal)
Cell surface of eukaryotic cells is covered with a wide variety of sialylated molecules involved in diverse biological processes and taking part in cell–cell interactions. Although the physiological relevance of these sialylated glycoconjugates in vertebrates begins to be deciphered, the origin and...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5000683/ https://www.ncbi.nlm.nih.gov/pubmed/27517905 http://dx.doi.org/10.3390/ijms17081286 |
_version_ | 1782450338220998656 |
---|---|
author | Teppa, Roxana E. Petit, Daniel Plechakova, Olga Cogez, Virginie Harduin-Lepers, Anne |
author_facet | Teppa, Roxana E. Petit, Daniel Plechakova, Olga Cogez, Virginie Harduin-Lepers, Anne |
author_sort | Teppa, Roxana E. |
collection | PubMed |
description | Cell surface of eukaryotic cells is covered with a wide variety of sialylated molecules involved in diverse biological processes and taking part in cell–cell interactions. Although the physiological relevance of these sialylated glycoconjugates in vertebrates begins to be deciphered, the origin and evolution of the genetic machinery implicated in their biosynthetic pathway are poorly understood. Among the variety of actors involved in the sialylation machinery, sialyltransferases are key enzymes for the biosynthesis of sialylated molecules. This review focus on β-galactoside α2,3/6-sialyltransferases belonging to the ST3Gal and ST6Gal families. We propose here an outline of the evolutionary history of these two major ST families. Comparative genomics, molecular phylogeny and structural bioinformatics provided insights into the functional innovations in sialic acid metabolism and enabled to explore how ST-gene function evolved in vertebrates. |
format | Online Article Text |
id | pubmed-5000683 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-50006832016-09-01 Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal) Teppa, Roxana E. Petit, Daniel Plechakova, Olga Cogez, Virginie Harduin-Lepers, Anne Int J Mol Sci Review Cell surface of eukaryotic cells is covered with a wide variety of sialylated molecules involved in diverse biological processes and taking part in cell–cell interactions. Although the physiological relevance of these sialylated glycoconjugates in vertebrates begins to be deciphered, the origin and evolution of the genetic machinery implicated in their biosynthetic pathway are poorly understood. Among the variety of actors involved in the sialylation machinery, sialyltransferases are key enzymes for the biosynthesis of sialylated molecules. This review focus on β-galactoside α2,3/6-sialyltransferases belonging to the ST3Gal and ST6Gal families. We propose here an outline of the evolutionary history of these two major ST families. Comparative genomics, molecular phylogeny and structural bioinformatics provided insights into the functional innovations in sialic acid metabolism and enabled to explore how ST-gene function evolved in vertebrates. MDPI 2016-08-09 /pmc/articles/PMC5000683/ /pubmed/27517905 http://dx.doi.org/10.3390/ijms17081286 Text en © 2016 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Teppa, Roxana E. Petit, Daniel Plechakova, Olga Cogez, Virginie Harduin-Lepers, Anne Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal) |
title | Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal) |
title_full | Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal) |
title_fullStr | Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal) |
title_full_unstemmed | Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal) |
title_short | Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal) |
title_sort | phylogenetic-derived insights into the evolution of sialylation in eukaryotes: comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (st3gal and st6gal) |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5000683/ https://www.ncbi.nlm.nih.gov/pubmed/27517905 http://dx.doi.org/10.3390/ijms17081286 |
work_keys_str_mv | AT tepparoxanae phylogeneticderivedinsightsintotheevolutionofsialylationineukaryotescomprehensiveanalysisofvertebratebgalactosidea236sialyltransferasesst3galandst6gal AT petitdaniel phylogeneticderivedinsightsintotheevolutionofsialylationineukaryotescomprehensiveanalysisofvertebratebgalactosidea236sialyltransferasesst3galandst6gal AT plechakovaolga phylogeneticderivedinsightsintotheevolutionofsialylationineukaryotescomprehensiveanalysisofvertebratebgalactosidea236sialyltransferasesst3galandst6gal AT cogezvirginie phylogeneticderivedinsightsintotheevolutionofsialylationineukaryotescomprehensiveanalysisofvertebratebgalactosidea236sialyltransferasesst3galandst6gal AT harduinlepersanne phylogeneticderivedinsightsintotheevolutionofsialylationineukaryotescomprehensiveanalysisofvertebratebgalactosidea236sialyltransferasesst3galandst6gal |