Distinctive regulation of the functional linkage between the human cation-independent mannose 6-phosphate receptor and GTP-binding proteins by insulin-like growth factor II and mannose 6-phosphate.

@article{Murayama1990DistinctiveRO,
  title={Distinctive regulation of the functional linkage between the human cation-independent mannose 6-phosphate receptor and GTP-binding proteins by insulin-like growth factor II and mannose 6-phosphate.},
  author={Y. Murayama and Takashi Okamoto and Etsuro Ogata and Tomiko Asano and Taroh Iiri and Toshiaki Katada and Michio Ui and Jeffrey H. Grubb and William S. Sly and Ikuo Nishimoto},
  journal={The Journal of biological chemistry},
  year={1990},
  volume={265 29},
  pages={17456-62}
}
The rat insulin-like growth factor II (IGF-II) receptor develops transmembrane signaling functions by directly coupling to a guanine nucleotide-binding protein (G protein) having a 40-kDa alpha subunit, Gi-2, whereas recent studies have indicated that the IGF-II receptor is a molecule identical to the cation-independent mannose 6-phosphate receptor (CI-MPR), a receptor implicated in lysosomal enzyme sorting. In this study, by using vesicles reconstituted with the clonal human CI-MPR and G… CONTINUE READING

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