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Science 1 June 2001: Vol. 292. no. 5522, pp. 1716 - 1718 DOI: 10.1126/science.1060896
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Reports
Binding of GGA2 to the Lysosomal Enzyme Sorting Motif of the Mannose 6-Phosphate Receptor
Yunxiang Zhu,1
Balraj Doray,1
Anssi Poussu,2
Veli-Pekka Lehto,2
Stuart Kornfeld1*
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.
1 Department of Internal Medicine, Washington
University School of Medicine, 660 South Euclid Avenue, St. Louis, MO
63110, USA.
2 Department of Pathology, University of
Oulu, FIN-90410 Oulu, Finland.
*
To whom correspondence should be addressed. E-mail:
skornfel{at}im.wustl.edu
Read the Full Text
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