Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor.

@article{Zhu2001BindingOG,
  title={Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor.},
  author={Yanli Zhu and Balraj Doray and Anssi Poussu and V. P. Lehto and Stuart Kornfeld},
  journal={Science},
  year={2001},
  volume={292 5522},
  pages={1716-8}
}
The GGAs are a multidomain protein family implicated in protein trafficking between the Golgi and endosomes. Here, the VHS domain of GGA2 was shown to bind to the acidic cluster-dileucine motif in the cytoplasmic tail of the cation-independent mannose 6-phosphate receptor (CI-MPR). Receptors with mutations in this motif were defective in lysosomal enzyme sorting. The hinge domain of GGA2 bound clathrin, suggesting that GGA2 could be a link between cargo molecules and clathrin-coated vesicle… CONTINUE READING

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