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PMID:10459012
| Citation |
Advani, RJ, Yang, B, Prekeris, R, Lee, KC, Klumperman, J and Scheller, RH (1999) VAMP-7 mediates vesicular transport from endosomes to lysosomes. J. Cell Biol. 146:765-76 |
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| Abstract |
A more complete picture of the molecules that are critical for the organization of membrane compartments is beginning to emerge through the characterization of proteins in the vesicle-associated membrane protein (also called synaptobrevin) family of membrane trafficking proteins. To better understand the mechanisms of membrane trafficking within the endocytic pathway, we generated a series of monoclonal and polyclonal antibodies against the cytoplasmic domain of vesicle-associated membrane protein 7 (VAMP-7). The antibodies recognize a 25-kD membrane-associated protein in multiple tissues and cell lines. Immunohistochemical analysis reveals colocalization with a marker of late endosomes and lysosomes, lysosome-associated membrane protein 1 (LAMP-1), but not with other membrane markers, including p115 and transferrin receptor. Treatment with nocodozole or brefeldin A does not disrupt the colocalization of VAMP-7 and LAMP-1. Immunoelectron microscopy analysis shows that VAMP-7 is most concentrated in the trans-Golgi network region of the cell as well as late endosomes and transport vesicles that do not contain the mannose-6 phosphate receptor. In streptolysin- O-permeabilized cells, antibodies against VAMP-7 inhibit the breakdown of epidermal growth factor but not the recycling of transferrin. These data are consistent with a role for VAMP-7 in the vesicular transport of proteins from the early endosome to the lysosome. |
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| Keywords |
Animals; Antigens, CD/metabolism; Biological Transport/drug effects; Brefeldin A/pharmacology; Cell Line; Cell Membrane Permeability; Endosomes/drug effects; Endosomes/metabolism; Epidermal Growth Factor/metabolism; Gene Expression; Golgi Apparatus/drug effects; Golgi Apparatus/metabolism; Humans; Intracellular Membranes/drug effects; Intracellular Membranes/metabolism; Lysosomal-Associated Membrane Protein 1; Lysosome-Associated Membrane Glycoproteins; Lysosomes/drug effects; Lysosomes/metabolism; Membrane Glycoproteins/metabolism; Membrane Proteins/immunology; Membrane Proteins/metabolism; Mice; Microscopy, Immunoelectron; Nocodazole/pharmacology; R-SNARE Proteins; Rats; Recombinant Fusion Proteins/immunology; Recombinant Fusion Proteins/metabolism; SNARE Proteins; Transferrin/metabolism; Vesicular Transport Proteins |
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