JCB logo
MBL International Tel: 800.200.5459 CLICK HERE
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 1632K)
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 HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sciaky, N.
Right arrow Articles by Lippincott-Schwartz, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sciaky, N.
Right arrow Articles by Lippincott-Schwartz, J.
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, 0021-9525/1997//1137 $5.00
The Journal of Cell Biology, Volume 139, Number 5, , 1997 1137-1155

Article

Golgi Tubule Traffic and the Effects of Brefeldin A Visualized in Living Cells



Noah Sciaky*, John Presley*, Carolyn Smith{ddagger}, Kristien J.M. Zaal*, Nelson Cole*, Jorge E. Moreira*, Mark Terasaki{ddagger},§, Eric Siggia||, and Jennifer Lippincott-Schwartz*

* Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892; {ddagger} National Institute of Neurological Disorders and Stroke, NIH, Bethesda, Maryland 20892; § Department of Physiology, University of Connecticut Health Center, Farmington, Connecticut 06032; and || Department of Physics, Cornell University, Ithaca, New York 14853

The Golgi complex is a dynamic organelle engaged in both secretory and retrograde membrane traffic. Here, we use green fluorescent protein–Golgi protein chimeras to study Golgi morphology in vivo. In untreated cells, membrane tubules were a ubiquitous, prominent feature of the Golgi complex, serving both to interconnect adjacent Golgi elements and to carry membrane outward along microtubules after detaching from stable Golgi structures. Brefeldin A treatment, which reversibly disassembles the Golgi complex, accentuated tubule formation without tubule detachment. A tubule network extending throughout the cytoplasm was quickly generated and persisted for 5–10 min until rapidly emptying Golgi contents into the ER within 15–30 s. Both lipid and protein emptied from the Golgi at similar rapid rates, leaving no Golgi structure behind, indicating that Golgi membranes do not simply mix but are absorbed into the ER in BFA-treated cells. The directionality of redistribution implied Golgi membranes are at a higher free energy state than ER membranes. Analysis of its kinetics suggested a mechanism that is analogous to wetting or adsorptive phenomena in which a tension-driven membrane flow supplements diffusive transfer of Golgi membrane into the ER. Such nonselective, flow-assisted transport of Golgi membranes into ER suggests that mechanisms that regulate retrograde tubule formation and detachment from the Golgi complex are integral to the existence and maintenance of this organelle.

1. Abbreviations used in this paper: ARF, ADP-ribosylation factor; BFA, brefeldin A; FRAP, fluorescence recovery after photobleaching; GFP, green fluorescent protein; NEM, N-ethylmaleimide; ROI, region of interest.

Address all correspondence to Jennifer Lippincott-Schwartz, Cell Biology and Metabolism Branch, NICHD, NIH, Building 18T, Room 101, Bethesda, MD 20892. Tel.: (301) 496-6368. Fax: (301) 402-0078.

Noah Sciaky's current address is Department of Pediatrics, National Jewish Center, Denver, Colorado.


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?


This article has been cited by other articles:



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