JCB logo
CountessT Automated Cell Counter
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online
doi:10.1083/jcb.200907126
The Journal of Cell Biology, Vol. 187, No. 3, 365-374
The Rockefeller University Press, 0021-9525 $30.00
© Milenkovic et al.
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 8631K)
Right arrow PDF+supp data (14870K)
Right arrow PPT slides of all figures
Right arrow Supplemental Material
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 CrossRef
Google Scholar
Right arrow Articles by Milenkovic, L.
Right arrow Articles by Rohatgi, R.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Milenkovic, L.
Right arrow Articles by Rohatgi, R.
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?

Report

Lateral transport of Smoothened from the plasma membrane to the membrane of the cilium



Ljiljana Milenkovic1, Matthew P. Scott1, and Rajat Rohatgi2

Howard Hughes Medical Institute, 1 Department of Developmental Biology, 1 Department of Genetics, 1 Department of Bioengineering, 1 Department of Medicine, 2 and Department of Biochemistry, 2 Stanford University School of Medicine, Stanford, CA 94305

Correspondence to Rajat Rohatgi: rrohatgi{at}stanford.edu; and Matthew P. Scott: mscott{at}stanford.edu

The function of primary cilia depends critically on the localization of specific proteins in the ciliary membrane. A major challenge in the field is to understand protein trafficking to cilia. The Hedgehog (Hh) pathway protein Smoothened (Smo), a 7-pass transmembrane protein, moves to cilia when a ligand is received. Using microscopy-based pulse-chase analysis, we find that Smo moves through a lateral transport pathway from the plasma membrane to the ciliary membrane. Lateral movement, either via diffusion or active transport, is quite distinct from currently studied pathways of ciliary protein transport in mammals, which emphasize directed trafficking of Golgi-derived vesicles to the base of the cilium. We anticipate that this alternative route will be used by other signaling proteins that function at cilia. The path taken by Smo may allow novel strategies for modulation of Hh signaling in cancer and regeneration.

Abbreviations used in this paper: CBG, C8 propanoic acid benzylguanine; DIP, dynamin inhibitory peptide; Fsk, Forskolin; Hh, Hedgehog; Ptc1, Patched 1; SAG, Smo agonist; Smo, Smoothened; Shh, Sonic hedgehog.

© 2009 Milenkovic et al.
This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).


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?




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