spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Burkhardt, J. K.
Right arrow Articles by Argon, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Burkhardt, J. K.
Right arrow Articles by Argon, Y.

Journal of Cell Science, Vol 92, Issue 4 633-642, Copyright © 1989 by Company of Biologists

JOURNAL ARTICLES

Intracellular transport of the glycoprotein of VSV is inhibited by CCCP at a late stage of post-translational processing

JK Burkhardt and Y Argon
Department of Microbiology and Immunology, Duke University Medical Center, Durham, North Carolina 22710.

The appearance of newly synthesized glycoprotein (G) of vesicular stomatitis virus at the surface of infected BHK cells is inhibited reversibly by treatment with carbonylcyanide m-chlorophenylhydrazone (CCCP). Under the conditions used, CCCP treatment depleted the cellular ATP levels by 40-60%, consistent with inhibition of transport at energy-requiring stages. The G protein that accumulates in cells treated with CCCP is heterogeneous. Most of it is larger than the newly synthesized G protein, is acylated with palmitic acid, and is resistant to endoglycosidase H (Endo H). Most of the arrested G protein is also sensitive to digestion with neuraminidase, indicating that it has undergone at least partial sialylation. A minority of G protein accumulates under these conditions in a less-mature form, suggesting its inability to reach the mid-Golgi compartment. The oligosaccharides of this G protein are Endo-H-sensitive and seem to be partly trimmed. Whereas sialylated G protein was arrested intracellularly, fucose-labelled G protein was able to complete its transport to the cell surface, indicating that a late CCCP-sensitive step separates sialylation from fucosylation. These post-translational modifications indicate that G protein can be transported as far as the trans-Golgi in the presence of CCCP and is not merely arrested in the endoplasmic reticulum.


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
A. J. M. Verhoeven, B. P. Neve, and H. Jansen
Intracellular Activation of Rat Hepatic Lipase Requires Transport to the Golgi Compartment and Is Associated with a Decrease in Sedimentation Velocity
J. Biol. Chem., March 24, 2000; 275(13): 9332 - 9339.
[Abstract] [Full Text] [PDF]

Home page
 JCBHome page
B. Landolfi, S. Curci, L. Debellis, T. Pozzan, and A. M. Hofer
Ca2+ Homeostasis in the Agonist-sensitive Internal Store: Functional Interactions Between Mitochondria and the ER Measured In Situ in Intact Cells
J. Cell Biol., September 7, 1998; 142(5): 1235 - 1243.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 1989