Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 289, Issue 2, Pages 680-695Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M113.518365
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Funding
- European Community [222992-BrainCAV]
- French Agence National de la Recherche
- E-Rare
- Fondation de France
- Association pour la Recherche sur la Sclerose Amyotrophique Laterale (ARSLa)
- Association Francaise contre les Myopathies
- Cancer Research UK
- UK Motor Neuron Disease Association
- Chemical Biology Center
- Imperial College London, UK
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The coxsackievirus and adenovirus receptor (CAR) serves as a docking factor for some adenovirus (AdV) types and group B coxsackieviruses. Its role in AdV internalization is unclear as studies suggest that its intracellular domain is dispensable for some AdV infection. We previously showed that in motor neurons, AdV induced CAR internalization and co-transport in axons, suggesting that CAR was linked to endocytic and long-range transport machineries. Here, we characterized the mechanisms of CAR endocytosis in neurons and neuronal cells. We found that CAR internalization was lipid microdomain-, actin-, and dynamin-dependent, and subsequently followed by CAR degradation in lysosomes. Moreover, ligands that disrupted the homodimeric CAR interactions in its D1 domains triggered an internalization cascade involving sequences in its intracellular tail.
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