Cited by 240

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Binding of GGA2 to the Lysosomal Enzyme Sorting Motif of the Mannose 6-Phosphate Receptor

Zhu, Yunxiang, Doray, Balraj, Poussu, Anssi, Lehto, Veli-Pekka, Kornfeld, Stuart·2001·Science

Abstract

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 assembly. Thus, GGA2 binding to the CI-MPR is important for lysosomal enzyme targeting.

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Crossref · 10.1126/science.1060896

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  • GGA proteins facilitate transport of specific cargo proteins (e.g., M6PRs) from the TGN to endosomal compartments.

    “GGA proteins could also facilitate transport of specific cargo proteins [e.g., the mannose 6 phosphate receptors (M6PRs)] from the TGN to endosomal compartments and the expression of GGA1 DN inhibits this transport route (Puertollano et al., 2001;Zhu et al., 2001).”
  • Expression of GGA1 DN inhibits the transport of specific cargo proteins (e.g., M6PRs) from the TGN to endosomal compartments.

    “GGA proteins could also facilitate transport of specific cargo proteins [e.g., the mannose 6 phosphate receptors (M6PRs)] from the TGN to endosomal compartments and the expression of GGA1 DN inhibits this transport route (Puertollano et al., 2001;Zhu et al., 2001).”

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Research works printed but not linked: 16

  1. 10.1146/annurev.bi.61.070192.001515 · DOI
  2. 10.1016/0092-8674(89)90793-9 · DOI
  3. 10.1083/jcb.119.2.249 · DOI
  4. 10.1016/S0021-9258(18)41533-5 · DOI
  5. 10.1074/jbc.272.11.7003 · DOI
  6. 10.1074/jbc.275.10.7176 · DOI
  7. E. C. Dell'Angelica et al. J. Cell Biol. 149 81 (2000). · DOI
  8. 10.1083/jcb.149.1.67 · DOI · Paper page
  9. 10.1091/mbc.11.4.1241 · DOI · Paper page
  10. 10.1006/bbrc.2000.2700 · DOI
  11. 10.1002/1097-0061(200101)18:1<1::AID-YEA644>3.0.CO;2-5 · DOI
  12. 10.1083/jcb.151.3.587 · DOI · Paper page
  13. 10.1083/jcb.121.5.997 · DOI
  14. B. Doray S. Kornfeld Mol. Biol. Cell in press.
  15. 10.1073/pnas.96.16.8907 · DOI
  16. 10.1074/jbc.274.2.1164 · DOI

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Metadata

Authors
Zhu, Y., Doray, B., Poussu, A., Lehto, V.-P., & Kornfeld, S.
Affiliations
  • Department of Internal Medicine, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
  • Department of Pathology, University of Oulu, FIN-90410 Oulu, Finland.
Venue
Science
Published
2001-06
Volume
292
Issue
5522
Pages
1716-1718
ISSN
  • 0036-8075
  • 1095-9203
Cited by
240
References
0
Language
en

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