HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 282, Issue 35, 25760-25768, August 31, 2007

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 282/35/25760    most recent M700437200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Zheng, H. Articles by Buss, J. E. Search for Related Content PubMed PubMed Citation Articles by Zheng, H. Articles by Buss, J. E. Social Bookmarking                      What's this?

H-Ras Does Not Need COP I- or COP II-dependent Vesicular Transport to Reach the Plasma Membrane^*

From the Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011

Although vesicular transport of the H-Ras protein from the Golgi to the plasma membrane is well known, additional trafficking steps, both to and from the plasma membrane, have also been described. Notably, both vesicular and nonvesicular transport mechanisms have been proposed. The initial trafficking of H-Ras to the plasma membrane was therefore examined in more detail. In untreated cells, H-Ras appeared at the plasma membrane more rapidly than a protein carried by the conventional exocytic pathway, and no H-Ras was visible on Golgi membranes in >80% of the cells. H-Ras was still able to reach the plasma membrane when COP II-directed transport was disrupted by two different mutant forms of Sar1, when COP I-mediated vesicular traffic from the endoplasmic reticulum to the Golgi was inhibited with brefeldin A, or when microtubules were disrupted by nocodazole. Although some H-Ras was present in the secretory pathway, protein that reached the membranes of the endoplasmic reticulum-Golgi intermediate compartment was unable to move further in the presence of nocodozale. These results identify an alternative mechanism for H-Ras trafficking that circumvents conventional COPI-, COPII-, and microtubule-dependent vesicular transport. Thus, H-Ras has two simultaneous but distinct means of transport and need not depend on vesicular trafficking for its delivery to the plasma membrane.

Received for publication, January 16, 2007 , and in revised form, May 30, 2007.

^* This work was supported by National Science Foundation Award 0110114. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains a supplemental movie.

¹ To whom correspondence should be addressed. Tel.: 859-323-0094; E-mail: jbuss2{at}email.uky.edu.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				R. D. Pooley, K. L. Moynihan, V. Soukoulis, S. Reddy, R. Francis, C. Lo, L.-J. Ma, and D. M. Bader Murine CENPF interacts with syntaxin 4 in the regulation of vesicular transport J. Cell Sci., October 15, 2008; 121(20): 3413 - 3421. [Abstract] [Full Text] [PDF]