JCB logo
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 5 January 2004. doi:10.1083/jcb.200303037
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 164, Number 1, 69-78
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 529K)
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 Ostermeyer, A. G.
Right arrow Articles by Brown, D. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ostermeyer, A. G.
Right arrow Articles by Brown, D. A.
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?

Article

Role of the hydrophobic domain in targeting caveolin-1 to lipid droplets



Anne G. Ostermeyer1, Lynne T. Ramcharan1, Youchun Zeng2, Douglas M. Lublin2 and Deborah A. Brown1

1 Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, Stony Brook, NY 11794
2 Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110

Address correspondence to D.A. Brown, Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, Stony Brook, NY 11794-5215. Tel.: (631) 632-8563. Fax: (631) 632-8575. email: deborah.brown{at}sunysb.edu

Although caveolins normally reside in caveolae, they can accumulate on the surface of cytoplasmic lipid droplets (LDs). Here, we first provided support for our model that overaccumulation of caveolins in the endoplasmic reticulum (ER) diverts the proteins to nascent LDs budding from the ER. Next, we found that a mutant H-Ras, present on the cytoplasmic surface of the ER but lacking a hydrophobic peptide domain, did not accumulate on LDs. We used the fact that wild-type caveolin-1 accumulates in LDs after brefeldin A treatment or when linked to an ER retrieval motif to search for mutants defective in LD targeting. The hydrophobic domain, but no specific sequence therein, was required for LD targeting of caveolin-1. Certain Leu insertions blocked LD targeting, independently of hydrophobic domain length, but dependent on their position in the domain. We propose that proper packing of putative hydrophobic helices may be required for LD targeting of caveolin-1.

Key Words: secondary protein structure; caveolins; hydrophobicity; protein transport; cell membrane

Abbreviations used in this paper: ADRP, adipocyte differentiation related protein; BFA, brefeldin A; DTAF, dichlorotriazinylaminofluorescein; FRT, Fischer rat thyroid; GAM, goat anti–mouse Ig(G + M); GAR, goat anti–rabbit IgG; GBV-B, GB virus-B; HCV, hepatitis C virus; IF, indirect immunofluorescence microscopy; LD, lipid droplet; PLAP, placental AP.


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