JCB logo
PeproTech: Cell Culture Supplements
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

Published 4 February 2002. doi:10.1083/jcb1563iti4
This Article
Right arrow Full Text (PDF, 317K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
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 Wells, W. A.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Wells, W. A.
Related Collections
Right arrowRelated Article
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, 0021-9525/2002/2/410-a $5.00
The Journal of Cell Biology, Volume 156, Number 3, February 4, 2002 410-a-410


In This Issue

Visualizing vesicles


Rab9 (red) and Rab7 (green) localize to distinct domains on late endosomes.

Barbero et al. have visualized the movement of individual vesicles from late endosomes to the trans Golgi by using GFP-marked Rab9 (page 511). Their results suggest that vesicles rather than tubules are used to deliver mannose 6-phosphate receptors (MPRs) in their return to the Golgi, after these proteins have transported enzymes from the Golgi to prelysosomes.

The detailed localization of the GFP-Rab9 is also telling. Rab GTPases are thought to contribute delivery address information for many trafficking vesicles, but Barbero et al. note that Rab9 is present on the endosome- derived vesicles from budding through docking. This is consistent with the group's earlier experiments suggesting that Rab9 has a function during budding. Perhaps as part of this budding process Rab9 clusters in particular regions, as the authors note that Rab9 and Rab7 (a GTPase involved in late endosome fusion) are present in largely nonoverlapping domains within a given late endosome.

Once Barbero et al. have overcome some protein engineering problems, they hope to visualize MPRs and the Rab9-binding cargo collector TIP47. They predict that MPRs will be present in the transport vesicles, and that TIP47 will be released from the vesicles after budding, perhaps to be replaced by an unknown dockingfactor. {blacksquare}



William A. Wells

wellsw{at}rockefeller.edu


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?

Related Article

Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells
Pierre Barbero, Lenka Bittova, and Suzanne R. Pfeffer
J. Cell Biol. 2002 156: 511-518. [Abstract] [Full Text] [PDF]




This Article
Right arrow Full Text (PDF, 317K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
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 Wells, W. A.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Wells, W. A.
Related Collections
Right arrowRelated Article
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?


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