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Protein Fucosylation
- Molecular classification
- Post-translational modification, Glycosylation, Enzyme target, Glycan modification
01
Overview
Protein fucosylation is a glycosylation process involving the enzymatic attachment of fucose to proteins. It encompasses core fucosylation (α1,6-linkage to N-glycans) and O-fucosylation (direct linkage to serine or threonine). This modification regulates immune responses, cell adhesion, neuronal function, and pathogen interactions. Altered fucosylation patterns are linked to cancer, arthritis, and sickle cell disease, making it a target for therapeutic intervention. Key enzymes involved are Fut8, POFUT1, and POFUT2.
- Other names
- FucosylationProtein fucosylationCore FucosylationO-Fucosylation
02
Mechanism of action
Inhibition of fucosylation, modulation of fucosylated glycan expression
03
Biological functions
Immune responseCell adhesionCell migrationNeuronal functionSignal transductionProtein foldingAntigen recognitionReceptor for pathogens/toxins
04
Disease associations
Cancer progressionCancer metastasisRheumatoid arthritisSickle cell diseaseInfectionInflammation
05
Safety considerations
Potential for off-target effects on other glycosylation pathwaysComplexity of glycan structures and their biological rolesEfficacy and patient stratification for immunotherapies
06
Interacting drugs
Anti-PD1 checkpoint inhibitors
07
Biomarkers
Fucosylated oligosaccharides (tumor markers)
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