JCB logo
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 652K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Advani, R. J.
Right arrow Articles by Scheller, R. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Advani, R. J.
Right arrow Articles by Scheller, R. H.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

© 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. 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
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 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

© 1999 The Rockefeller University Press

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


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?




  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents