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J. Cell Biol., Volume 146, Number 4, August 23, 1999 765-776
Copyright © 1999 by The Rockefeller University Press.

VAMP-7 Mediates Vesicular Transport from Endosomes to Lysosomes

Raj J. Advanib, Bin Yangb, Rytis Prekerisb, Kelly C. Leeb, Judith Klumpermana, and Richard H. Schellerb
a Medical School, University of Utrecht, Institute for Biomembranes, 3584CX Utrecht, The Netherlands
b Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California 94305-5428

Correspondence to: Richard H. Scheller, Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University Medical Center, B-155 Beckman Center, Stanford, CA 94305. Tel:(650) 723-9075 Fax:(650) 725-4436 E-mail:scheller{at}cmgm.stanford.edu.

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.

Key Words: VAMP-7, SNARE, endosome, lysosome, membrane trafficking


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