Vamp-7 Mediates Vesicular Transport from Endosomes to Lysosomes

doi:10.1083/jcb.146.4.765

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© The Rockefeller University Press, 0021-9525/1999//765 $5.00
The Journal of Cell Biology, Volume 146, Number 4, , 1999 765-776

Original Article

Vamp-7 Mediates Vesicular Transport from Endosomes to Lysosomes

Raj J. Advani^b, Bin Yang^b, Rytis Prekeris^b, Kelly C. Lee^b, Judith Klumperman^a, and Richard H. Scheller^b

^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
Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University Medical Center, B-155 Beckman Center, Stanford, CA 94305.(650) 725-4436(650) 723-9075

scheller{at}cmgm.stanford.edu

A more complete picture of the molecules that are critical forthe organization of membrane compartments is beginning to emergethrough the characterization of proteins in the vesicle-associatedmembrane protein (also called synaptobrevin) family of membranetrafficking proteins. To better understand the mechanisms ofmembrane trafficking within the endocytic pathway, we generateda series of monoclonal and polyclonal antibodies against thecytoplasmic domain of vesicle-associated membrane protein 7(VAMP-7). The antibodies recognize a 25-kD membrane-associatedprotein in multiple tissues and cell lines. Immunohistochemicalanalysis reveals colocalization with a marker of late endosomesand lysosomes, lysosome-associated membrane protein 1 (LAMP-1),but not with other membrane markers, including p115 and transferrinreceptor. Treatment with nocodozole or brefeldin A does notdisrupt the colocalization of VAMP-7 and LAMP-1. Immunoelectronmicroscopy analysis shows that VAMP-7 is most concentrated inthe trans-Golgi network region of the cell as well as late endosomesand transport vesicles that do not contain the mannose-6 phosphatereceptor. In streptolysin- O–permeabilized cells, antibodiesagainst VAMP-7 inhibit the breakdown of epidermal growth factorbut not the recycling of transferrin. These data are consistentwith a role for VAMP-7 in the vesicular transport of proteinsfrom the early endosome to the lysosome.

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

1.used in this paper: aa, amino acid(s); BFA, brefeldin A; EE,early endosome; GST, glutathione S-transferase; LAMP-1, lysosome-associatedmembrane protein 1; LE, late endosome; MPR, mannose-6 phosphatereceptor; NEM, N-ethylmaleimide; NSF, NEM-sensitive factor;PNS, postnuclear supernatant; RE, recycling endosome; SLO, streptolysin-O;SNAP, soluble NSF attachment protein; SNAP-25, synaptosomal-associatedprotein of 25 kD; SNARE, SNAP receptor; Tf, transferrin; TfR,Tf receptor; VAMP, vesicle-associated membrane protein

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