JCB logo
MBL International Tel: 800.200.5459 CLICK HERE
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 18 July 2005. doi:10.1083/jcb.200502063
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 170, Number 2, 261-272
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 2660K)
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 Goodwin, J. S.
Right arrow Articles by Kenworthy, A. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Goodwin, J. S.
Right arrow Articles by Kenworthy, A. K.
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

Depalmitoylated Ras traffics to and from the Golgi complex via a nonvesicular pathway



J. Shawn Goodwin1, Kimberly R. Drake1, Carl Rogers1, Latasha Wright3, Jennifer Lippincott-Schwartz2, Mark R. Philips3, and Anne K. Kenworthy1,2

1 Department of Molecular Physiology and Biophysics and Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232
2 Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 21218
3 Department of Cell Biology, New York University School of Medicine, New York, NY 10016

Correspondence to Anne Kenworthy: anne.kenworthy{at}vanderbilt.edu

Palmitoylation is postulated to regulate Ras signaling by modulating its intracellular trafficking and membrane microenvironment. The mechanisms by which palmitoylation contributes to these events are poorly understood. Here, we show that dynamic turnover of palmitate regulates the intracellular trafficking of HRas and NRas to and from the Golgi complex by shifting the protein between vesicular and nonvesicular modes of transport. A combination of time-lapse microscopy and photobleaching techniques reveal that in the absence of palmitoylation, GFP-tagged HRas and NRas undergo rapid exchange between the cytosol and ER/Golgi membranes, and that wild-type GFP-HRas and GFP-NRas are recycled to the Golgi complex by a nonvesicular mechanism. Our findings support a model where palmitoylation kinetically traps Ras on membranes, enabling the protein to undergo vesicular transport. We propose that a cycle of depalmitoylation and repalmitoylation regulates the time course and sites of Ras signaling by allowing the protein to be released from the cell surface and rapidly redistributed to intracellular membranes.

Abbreviations used in this paper: 2BP, 2-bromo-palmitate; CTXB, cholera toxin B subunit; FCS, fluorescence correlation spectroscopy; Mf, mobile fraction; {tau}D, correlation time; PAT, palmitoyl acyl transferase.


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