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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5522
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pubmed:dateCreated |
2001-6-1
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pubmed:abstractText |
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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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cations,
http://linkedlifedata.com/resource/pubmed/chemical/Clathrin,
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptides,
http://linkedlifedata.com/resource/pubmed/chemical/GGA2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, IGF Type 2,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor AP-1,
http://linkedlifedata.com/resource/pubmed/chemical/leucylleucine
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
292
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1716-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11387476-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:11387476-Amino Acid Motifs,
pubmed-meshheading:11387476-Amino Acid Sequence,
pubmed-meshheading:11387476-Animals,
pubmed-meshheading:11387476-Carrier Proteins,
pubmed-meshheading:11387476-Cations,
pubmed-meshheading:11387476-Clathrin,
pubmed-meshheading:11387476-Dipeptides,
pubmed-meshheading:11387476-L Cells (Cell Line),
pubmed-meshheading:11387476-Lysosomes,
pubmed-meshheading:11387476-Mice,
pubmed-meshheading:11387476-Molecular Sequence Data,
pubmed-meshheading:11387476-Mutation,
pubmed-meshheading:11387476-Protein Sorting Signals,
pubmed-meshheading:11387476-Protein Structure, Tertiary,
pubmed-meshheading:11387476-Protein Transport,
pubmed-meshheading:11387476-Proteins,
pubmed-meshheading:11387476-Rats,
pubmed-meshheading:11387476-Receptor, IGF Type 2,
pubmed-meshheading:11387476-Recombinant Fusion Proteins,
pubmed-meshheading:11387476-Solubility,
pubmed-meshheading:11387476-Transcription Factor AP-1,
pubmed-meshheading:11387476-Transport Vesicles,
pubmed-meshheading:11387476-Two-Hybrid System Techniques,
pubmed-meshheading:11387476-trans-Golgi Network
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pubmed:year |
2001
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pubmed:articleTitle |
Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor.
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pubmed:affiliation |
Department of Internal Medicine, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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