Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor.
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.
Mesh Terms:
Adaptor Proteins, Vesicular Transport, Amino Acid Motifs, Amino Acid Sequence, Animals, Carrier Proteins, Cations, Clathrin, Dipeptides, L Cells (Cell Line), Lysosomes, Mice, Molecular Sequence Data, Mutation, Protein Sorting Signals, Protein Structure, Tertiary, Protein Transport, Proteins, Rats, Receptor, IGF Type 2, Recombinant Fusion Proteins, Solubility, Transcription Factor AP-1, Transport Vesicles, Two-Hybrid System Techniques, trans-Golgi Network
Adaptor Proteins, Vesicular Transport, Amino Acid Motifs, Amino Acid Sequence, Animals, Carrier Proteins, Cations, Clathrin, Dipeptides, L Cells (Cell Line), Lysosomes, Mice, Molecular Sequence Data, Mutation, Protein Sorting Signals, Protein Structure, Tertiary, Protein Transport, Proteins, Rats, Receptor, IGF Type 2, Recombinant Fusion Proteins, Solubility, Transcription Factor AP-1, Transport Vesicles, Two-Hybrid System Techniques, trans-Golgi Network
Science
Date: Jun. 01, 2001
PubMed ID: 11387476
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