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The GGAs are a multidomain protein family implicated in
protein trafficking between the Golgi and endosomes. Here, the VHSdomain of GGA2 was shown to bind to the acidic cluster-dileucinemotif
in the cytoplasmic tail of the cation-independent mannose6-phosphate
receptor (CI-MPR). Receptors with mutations in thismotif were
defective in lysosomal enzyme sorting. The hinge domainof GGA2 bound
clathrin, suggesting that GGA2 could be a link betweencargo molecules
and clathrin-coated vesicle assembly. Thus, GGA2binding 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
The editors suggest the following Related Resources on Science sites:
In Science Magazine
PERSPECTIVES
Sharon A. Tooze (1 June 2001) Science292 (5522), 1663.
[DOI: 10.1126/science.1062239] |Summary »|Full Text »
REPORTS
Rosa Puertollano, Rubén C. Aguilar, Inna Gorshkova, Robert J. Crouch, and Juan S. Bonifacino (1 June 2001) Science292 (5522), 1712.
[DOI: 10.1126/science.1060750] |Abstract »|Full Text »|PDF »|Supplemental Data »
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