Glycosylation signals that separate the trimerization from the mhc class II-binding domain control intracellular degradation of invariant chain.

@article{Neumann2001GlycosylationST,
  title={Glycosylation signals that separate the trimerization from the mhc class II-binding domain control intracellular degradation of invariant chain.},
  author={J{\"u}rgen Neumann and N Schach and Norbert Koch},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 16},
  pages={13469-75}
}
Invariant chain (Ii) serves as a chaperone for folding and intracellular transport of major histocompatibility complex class II (MHCII) molecules. Early in biosynthesis, Ii associates with MHCII molecules and directs their intracellular transport to endocytic compartments where vesicular proteinases sequentially release Ii from the MHCII heterodimer. The detachment of Ii makes the MHCII groove susceptible for binding of antigenic peptides. We investigated the role of N-linked glycosylation in… CONTINUE READING

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