Structural basis for recognition of phosphodiester-containing lysosomal enzymes by the cation-independent mannose 6-phosphate receptor.

@article{Olson2010StructuralBF,
  title={Structural basis for recognition of phosphodiester-containing lysosomal enzymes by the cation-independent mannose 6-phosphate receptor.},
  author={Linda J Olson and Francis C Peterson and Alicia C. Castonguay and Richard N. Bohnsack and Mariko Kudo and Russell R Gotschall and William Canfield and Brian F Volkman and Nancy M. Dahms},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 28},
  pages={12493-8}
}
Mannose 6-phosphate (Man-6-P)-dependent trafficking is vital for normal development. The biogenesis of lysosomes, a major cellular site of protein, carbohydrate, and lipid catabolism, depends on the 300-kDa cation-independent Man-6-P receptor (CI-MPR) that transports newly synthesized acid hydrolases from the Golgi. The CI-MPR recognizes lysosomal enzymes bearing the Man-6-P modification, which arises by the addition of GlcNAc-1-phosphate to mannose residues and subsequent removal of GlcNAc by… CONTINUE READING

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Mutations in the lysosomal enzyme-targeting pathway and persistent stuttering

  • C Kang
  • N Engl J Med
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