JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on June 10, 2005
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
280/23/22515    most recent
M413472200v1
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 Gaigg, B.
Right arrow Articles by Schneiter, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gaigg, B.
Right arrow Articles by Schneiter, R.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print April 6, 2005
J. Biol. Chem, 10.1074/jbc.M413472200
Submitted on November 30, 2004
Revised on March 14, 2005
Accepted on April 6, 2005

Synthesis of sphingolipids with very long-chain fatty acids but not ergosterol is required for routing of newly synthesized plasma membrane ATPase to the cell surface of yeast

Barbara Gaigg, Birgit Timischl, Linda Corbino, and Roger Schneiter

Division of Biochemistry, University Fribourg, Fribourg CH-1700

Corresponding Author: roger.schneiter{at}unifr.ch

The proton pumping [H+]-ATPase, Pma1p, is an abundant and very long-lived polytopic protein of the S. cerevisiae plasma membrane. Pma1p constitutes a major cargo of the secretory pathway and thus serves as an excellent model to study plasma membrane biogenesis. We have previously shown that newly synthesized Pma1p is mistargeted to the vacuole in an elo3 mutant that affects the synthesis of the ceramide-bound C26 very long-chain fatty acid (Eisenkolb et al. (2002). Mol. Biol. Cell 13, 4414-4428) and now describe a more detailed analysis of the role of lipids in Pma1p biogenesis. Remarkably, a block at various steps of sterol biosynthesis, a complete block in sterol synthesis, or the exchange of internally synthesized ergosterol by externally supplied ergosterol or even by cholesterol does not affect Pma1p biogenesis, or its association with detergent resistant membrane domains (lipid “rafts”). However, a block in sphingolipid synthesis or any perturbation in the synthesis of the ceramide-bound C26 very long-chain fatty acid, results in mistargeting of newly synthesized Pma1p to the vacuole. Mistargeting correlates with a lack of newly synthesized Pma1p to acquire detergent resistance, suggesting that sphingolipids with very long acyl chains affect sorting of Pma1p to the cell surface.


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 Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 MicrobiologyHome page
T. Iwaki, H. Iefuji, Y. Hiraga, A. Hosomi, T. Morita, Y. Giga-Hama, and K. Takegawa
Multiple functions of ergosterol in the fission yeast Schizosaccharomyces pombe
Microbiology, March 1, 2008; 154(3): 830 - 841.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
L. Pineau, L. Bonifait, J.-M. Berjeaud, P. Alimardani-Theuil, T. Berges, and T. Ferreira
A Lipid-mediated Quality Control Process in the Golgi Apparatus in Yeast
Mol. Biol. Cell, March 1, 2008; 19(3): 807 - 821.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
E. Lauwers, G. Grossmann, and B. Andre
Evidence for Coupled Biogenesis of Yeast Gap1 Permease and Sphingolipids: Essential Role in Transport Activity and Normal Control by Ubiquitination
Mol. Biol. Cell, August 1, 2007; 18(8): 3068 - 3080.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
M. Laloi, A.-M. Perret, L. Chatre, S. Melser, C. Cantrel, M.-N. Vaultier, A. Zachowski, K. Bathany, J.-M. Schmitter, M. Vallet, et al.
Insights into the Role of Specific Lipids in the Formation and Delivery of Lipid Microdomains to the Plasma Membrane of Plant Cells
Plant Physiology, January 1, 2007; 143(1): 461 - 472.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B. Gaigg, A. Toulmay, and R. Schneiter
Very Long-chain Fatty Acid-containing Lipids rather than Sphingolipids per se Are Required for Raft Association and Stable Surface Transport of Newly Synthesized Plasma Membrane ATPase in Yeast
J. Biol. Chem., November 10, 2006; 281(45): 34135 - 34145.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
J. M. Shea, T. B. Kechichian, C. Luberto, and M. Del Poeta
The cryptococcal enzyme inositol phosphosphingolipid-phospholipase C confers resistance to the antifungal effects of macrophages and promotes fungal dissemination to the central nervous system.
Infect. Immun., October 1, 2006; 74(10): 5977 - 5988.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
R. Bosson, M. Jaquenoud, and A. Conzelmann
GUP1 of Saccharomyces cerevisiae Encodes an O-Acyltransferase Involved in Remodeling of the GPI Anchor
Mol. Biol. Cell, June 1, 2006; 17(6): 2636 - 2645.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
V. Zaremberg, C. Gajate, L. M. Cacharro, F. Mollinedo, and C. R. McMaster
Cytotoxicity of an Anti-cancer Lysophospholipid through Selective Modification of Lipid Raft Composition
J. Biol. Chem., November 11, 2005; 280(45): 38047 - 38058.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.