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Binding of GGA2 to the Lysosomal Enzyme Sorting Motif of the Mannose 6-Phosphate Receptor
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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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).”
From GGA1 Is Expressed in the Human Brain and Affects the Generation of Amyloid β-Peptide (2006) · cites this paper as 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).”
From GGA1 Is Expressed in the Human Brain and Affects the Generation of Amyloid β-Peptide (2006) · cites this paper as Zhu et al., 2001
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Research works printed but not linked: 16
- 10.1146/annurev.bi.61.070192.001515 · DOI
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- 10.1006/bbrc.2000.2700 · DOI
- 10.1002/1097-0061(200101)18:1<1::AID-YEA644>3.0.CO;2-5 · DOI
- 10.1083/jcb.151.3.587 · DOI · Paper page
- 10.1083/jcb.121.5.997 · DOI
- B. Doray S. Kornfeld Mol. Biol. Cell in press.
- 10.1073/pnas.96.16.8907 · DOI
- 10.1074/jbc.274.2.1164 · DOI
Cited by
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Raposo, G., & Marks, M. S. (2002) · Traffic · doi:10.1034/j.1600-0854.2002.030401.x · Cited by 161
GGA1 Is Expressed in the Human Brain and Affects the Generation of Amyloid β-Peptide
Wahle, T., Thal, D. R., Sastre, M., Rentmeister, A., Bogdanovic, N., Famulok, M., Heneka, M. T., & Walter, J. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1982-06.2006 · Cited by 88
GGA function is required for maturation of neuroendocrine secretory granules
Kakhlon, O., Sakya, P., Larijani, B., Watson, R., & Tooze, S. A. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601067 · Cited by 45
Impact of Genetic Background on Neonatal Lethality of Gga2 Gene-Trap Mice
Doray, B., Govero, J., & Kornfeld, S. (2014) · G3 Genes|Genomes|Genetics · doi:10.1534/g3.114.010355 · Cited by 9
Self-citation
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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