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Density-dependent lectin-glycan interactions as a paradigm for conditional regulation by posttranslational modifications.

ABSTRACT: Mice with null mutations in specific Golgi glycosyltransferases show evidence of glycan compensation where missing carbohydrate epitopes are found on biosynthetically related structures. Repetitive saccharide sequences within the larger glycan structures are functional epitopes recognized by animal lectins. These studies provide the first in vivo support for the existence of a feedback system that maintains and regulates glycan epitope density in cells. Receptor regulation by lectin-glycan interactions and the Golgi provides a mechanism for the adaptation of cell surface receptors and solute transporters in response to environmental cues and intracellular signaling. We suggest that other posttranslational modification systems might have similar conditional features regulated by density-dependent ligand-epitope interactions.

SUBMITTER: Dennis JW

PROVIDER: S-EPMC3617338 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

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Density-dependent lectin-glycan interactions as a paradigm for conditional regulation by posttranslational modifications.

Dennis James W JW Brewer C Fred CF

Molecular & cellular proteomics : MCP 20130201 4

Mice with null mutations in specific Golgi glycosyltransferases show evidence of glycan compensation where missing carbohydrate epitopes are found on biosynthetically related structures. Repetitive saccharide sequences within the larger glycan structures are functional epitopes recognized by animal lectins. These studies provide the first in vivo support for the existence of a feedback system that maintains and regulates glycan epitope density in cells. Receptor regulation by lectin-glycan inter ...[more]

PMID: 23378517

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Dataset Information

Density-dependent lectin-glycan interactions as a paradigm for conditional regulation by posttranslational modifications.

Publications

Density-dependent lectin-glycan interactions as a paradigm for conditional regulation by posttranslational modifications.

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