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Sorting of Mannose 6-Phosphate Receptors Mediated by the GGAs
Rosa Puertollano,1*Rubén C. Aguilar,1*Inna Gorshkova,2Robert J. Crouch,2Juan S. Bonifacino1
The delivery of soluble hydrolases to lysosomes is mediated by the
cation-independent and cation-dependent mannose 6-phosphatereceptors.
The cytosolic tails of both receptors contain acidic-cluster-dileucinesignals that direct sorting from the trans-Golgi network to theendosomal-lysosomal system. We found that these signals bind tothe VHS
domain of the Golgi-localized, -ear-containing, ARF-bindingproteins (GGAs). The receptors and the GGAs left the trans-Golginetwork on the same tubulo-vesicular carriers. A dominant-negativeGGA
mutant blocked exit of the receptors from the trans-Golginetwork.
Thus, the GGAs appear to mediate sorting of the mannose6-phosphate
receptors at the trans-Golgi network.
1 Cell Biology and Metabolism Branch, National
Institute of Child Health and Human Development, National Institutes of
Health, Bethesda, MD 20892, USA.
2 Laboratory of
Molecular Genetics, National Institute of Child Health and Human
Development, National Institutes of Health, Bethesda, MD 20892, USA.
*
These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail:
juan{at}helix.nih.gov
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In Science Magazine
PERSPECTIVES
Sharon A. Tooze (1 June 2001) Science292 (5522), 1663.
[DOI: 10.1126/science.1062239] |Summary »|Full Text »
REPORTS
Yunxiang Zhu, Balraj Doray, Anssi Poussu, Veli-Pekka Lehto, and Stuart Kornfeld (1 June 2001) Science292 (5522), 1716.
[DOI: 10.1126/science.1060896] |Abstract »|Full Text »|PDF »
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-ear-containing, ARF-binding proteins (GGAs). The receptors and the GGAs left the trans-Golgi network on the same tubulo-vesicular carriers. A dominant-negative GGA
mutant blocked exit of the receptors from the trans-Golgi network.
Thus, the GGAs appear to mediate sorting of the mannose 6-phosphate
receptors at the trans-Golgi network.
