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

J. Biol. Chem., Vol. 283, Issue 27, 18892-18904, July 4, 2008

This Article Free via Author's Choice: AC AC Full Text Full Text (PDF) Supplemental Data AC All Versions of this Article: 283/27/18892    most recent M800986200v1 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 Shibata, Y. Articles by Voeltz, G. K. Search for Related Content PubMed PubMed Citation Articles by Shibata, Y. Articles by Voeltz, G. K. Social Bookmarking                      What's this?

The Reticulon and Dp1/Yop1p Proteins Form Immobile Oligomers in the Tubular Endoplasmic Reticulum^*

Yoko Shibata¹, Christiane Voss¹, Julia M. Rist, Junjie Hu, Tom A. Rapoport², William A. Prinz³⁴, and Gia K. Voeltz, Supported by a Searle Scholar Award^¶35

From the Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, the Laboratory of Cell Biochemistry and Biology, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, and the ^¶Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Colorado 80309

We recently identified a class of membrane proteins, the reticulons and DP1/Yop1p, which shape the tubular endoplasmic reticulum (ER) in yeast and mammalian cells. These proteins are highly enriched in the tubular portions of the ER and virtually excluded from other regions. To understand how they promote tubule formation, we characterized their behavior in cellular membranes and addressed how their localization in the ER is determined. Using fluorescence recovery after photobleaching, we found that yeast Rtn1p and Yop1p are less mobile in the membrane than normal ER proteins. Sucrose gradient centrifugation and cross-linking analyses show that they form oligomers. Mutants of yeast Rtn1p, which no longer localize exclusively to the tubular ER or are even totally inactive in inducing ER tubules, are more mobile and oligomerize less extensively. The mammalian reticulons and DP1 are also relatively immobile and can form oligomers. The conserved reticulon homology domain that includes the two membrane-embedded segments is sufficient for the localization of the reticulons to the tubular ER, as well as for their diffusional immobility and oligomerization. Finally, ATP depletion in both yeast and mammalian cells further decreases the mobilities of the reticulons and DP1. We propose that oligomerization of the reticulons and DP1/Yop1p is important for both their localization to the tubular domains of the ER and for their ability to form tubules.

Received for publication, February 6, 2008 , and in revised form, March 31, 2008.

^* This work was supported, in whole or in part, by the National Institutes of Health NIDDK intramural research program (to W. A. P. and C. V.). 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 supplemental Figs. S1–S5.

Author's Choice—Final version full access.

¹ Both authors contributed equally to this work.

² A Howard Hughes Medical Institutes Investigator.

³ Both authors contributed equally to this work.

Author's Choice

Creative Commons Attribution Non-Commercial License applies to Author Choice Articles

⁴ To whom correspondence may be addressed: Laboratory of Cell Biochemistry and Biology, NIDDK, NIH, Bethesda, MD 20892. Tel.: 301-451-4592; Fax: 301-496-9431; E-mail: wprinz{at}helix.nih.gov. ⁵ To whom correspondence may be addressed: Dept. of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309. Tel.: 303-492-3145; Fax: 303-492-7744; E-mail: gia.voeltz{at}colorado.edu.

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

This article has been cited by other articles:

				T. R. Dawson, M. D. Lazarus, M. W. Hetzer, and S. R. Wente ER membrane-bending proteins are necessary for de novo nuclear pore formation J. Cell Biol., March 9, 2009; 184(5): 659 - 675. [Abstract] [Full Text] [PDF]

				P. Benyamini, P. Webster, and D. I. Meyer Knockdown of p180 Eliminates the Terminal Differentiation of a Secretory Cell Line Mol. Biol. Cell, January 1, 2009; 20(2): 732 - 744. [Abstract] [Full Text] [PDF]

				D. J. Anderson and M. W. Hetzer Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation J. Cell Biol., September 9, 2008; 182(5): 911 - 924. [Abstract] [Full Text] [PDF]