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Complex N-glycan promotes CD133 mono-ubiquitination and secretion
Yinan Li1, Danfang Shi1, Fan Yang1
1NHC Key Laboratory of Glycoconjugates Research, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Shanghai Medical College of Fudan University, China.
FEBS Letters
|March 16, 2019
Summary
Secreted CD133, a cancer stem cell marker, undergoes N-glycosylation. Inhibiting this glycosylation reduces CD133 secretion and promotes its endosomal accumulation, revealing a novel secretion pathway.
Area of Science:
- Cell Biology
- Glycobiology
- Cancer Research
Background:
- CD133 is a key marker for cancer stem cells, crucial for tumor initiation and metastasis.
- Evidence suggests CD133 is secreted extracellularly, but the secretion mechanism is poorly understood.
Purpose of the Study:
- To elucidate the mechanism of CD133 secretion.
- To investigate the role of N-glycosylation in CD133 secretion.
Main Methods:
- Utilized swainsonine to inhibit CD133 complex-type N-glycosylation.
- Assessed CD133 membrane localization, secretion levels, and endosomal accumulation.
- Analyzed CD133 mono-ubiquitination and interaction with Tsg101.
Main Results:
- Secreted CD133 exhibits complex-type N-glycosylation with beta1,6GlcNAc modification.
- Inhibition of N-glycosylation by swainsonine did not alter membrane localization but reduced secretion.
- Swainsonine treatment led to CD133 accumulation in early endosomes.
- Reduced secretion was linked to decreased mono-ubiquitination and impaired CD133-Tsg101 interaction.
Conclusions:
- CD133 secretion is dependent on its complex-type N-glycosylation.
- N-glycosylation regulates CD133 secretion via ubiquitination and Tsg101 interaction.
- This study uncovers a novel glycosylation-dependent pathway for CD133 secretion.
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