The vertebrate sialylation machinery: structure-function and molecular evolution of GT-29 sialyltransferases

Every eukaryotic cell is covered with a thick layer of complex carbohydrates with essential roles in their social life. In Deuterostoma, sialic acids present at the outermost positions of glycans of glycoconjugates are known to be key players in cellular interactions including host-pathogen interact...

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Published inGlycoconjugate journal Vol. 40; no. 4; pp. 473 - 492
Main Author Harduin Lepers, Anne
Format Journal Article
LanguageEnglish
Published New York Springer US 01.08.2023
Springer Nature B.V
Springer Verlag
SeriesGlycoconjugate Journal
Subjects
Acids
Biochemistry
Biology
Biomedical and Life Sciences
Carbohydrates
Carbon
Chemical Sciences
Evolution
Functional morphology
Glycoconjugates
Glycolipids
Glycoproteins
Golgi apparatus
Host-pathogen interactions
Life Sciences
Molecular evolution
or physical chemistry
Pathogens
Pathology
Polysaccharides
Reptiles & amphibians
Review
Sialic acids
Structure-function relationships
Theoretical and
Vertebrates
Evolution
Sialic acid
Enzyme activity
Sialyltransferase
Structure-function
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Summary:Every eukaryotic cell is covered with a thick layer of complex carbohydrates with essential roles in their social life. In Deuterostoma, sialic acids present at the outermost positions of glycans of glycoconjugates are known to be key players in cellular interactions including host-pathogen interactions. Their negative charge and hydrophilic properties enable their roles in various normal and pathological states and their expression is altered in many diseases including cancers. Sialylation of glycoproteins and glycolipids is orchestrated by the regulated expression of twenty sialyltransferases in human tissues with distinct enzymatic characteristics and preferences for substrates and linkages formed. However, still very little is known on the functional organization of sialyltransferases in the Golgi apparatus and how the sialylation machinery is finely regulated to provide the ad hoc sialome to the cell. This review summarizes current knowledge on sialyltransferases, their structure–function relationships, molecular evolution, and their implications in human biology.
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ISSN:0282-0080
1573-4986
1573-4986
DOI:10.1007/s10719-023-10123-w