JCB logo
Accuri Cytometers
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

Published 28 February 2005. doi:10.1083/jcb.200409045
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 168, Number 5, 761-773
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 3704K)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
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 Boukh-Viner, T.
Right arrow Articles by Titorenko, V. I.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Boukh-Viner, T.
Right arrow Articles by Titorenko, V. I.
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?

Article

Dynamic ergosterol- and ceramide-rich domains in the peroxisomal membrane serve as an organizing platform for peroxisome fusion



Tatiana Boukh-Viner1, Tong Guo1, Alex Alexandrian1, André Cerracchio1, Christopher Gregg1, Sandra Haile1, Robert Kyskan1, Svetlana Milijevic1, Daniel Oren1, Jonathan Solomon1, Vivianne Wong1, Jean-Marc Nicaud3, Richard A. Rachubinski4, Ann M. English2, and Vladimir I. Titorenko1

1 Department of Biology, Concordia University, Montreal, Quebec H4B 1R6, Canada
2 Department of Chemistry and Biochemistry, Concordia University, Montreal, Quebec H4B 1R6, Canada
3 Laboratoire de Génétique des Microorganismes, 78850 Thiverval-Grignon, France
4 Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada

Correspondence to Vladimir I. Titorenko: VTITOR{at}vax2.concordia.ca

We describe unusual ergosterol- and ceramide-rich (ECR) domains in the membrane of yeast peroxisomes. Several key features of these detergent-resistant domains, including the nature of their sphingolipid constituent and its unusual distribution across the membrane bilayer, clearly distinguish them from well characterized detergent-insoluble lipid rafts in the plasma membrane. A distinct set of peroxisomal proteins, including two ATPases, Pex1p and Pex6p, as well as phosphoinositide- and GTP-binding proteins, transiently associates with the cytosolic face of ECR domains. All of these proteins are essential for the fusion of the immature peroxisomal vesicles P1 and P2, the earliest intermediates in a multistep pathway leading to the formation of mature, metabolically active peroxisomes. Peroxisome fusion depends on the lateral movement of Pex1p, Pex6p, and phosphatidylinositol-4,5-bisphosphate–binding proteins from ECR domains to a detergent-soluble portion of the membrane, followed by their release to the cytosol. Our data suggest a model for the multistep reorganization of the multicomponent peroxisome fusion machinery that transiently associates with ECR domains.

Abbreviations used in this paper: bp, binding proteins; ECR, ergosterol- and ceramide-rich; HLB, hydrophilic–lipophilic balance; n-OG, n-octyl-ß-D-glucopyranoside; PC, phosphatidylcholine; PE, phosphatidylethanolamine; PI, phosphatidylinositol; PS, phosphatidylserine.


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