JCB logo
PeproTech: Free Shipping at www.peprotech.com
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

Published 20 June 2005. doi:10.1083/jcb1696iti1
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 169, Number 6, 834-834
This Article
Right arrow Full Text (PDF, 613K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by LeBrasseur, N.
Right arrow Search for Related Content
PubMed
Right arrow Articles by LeBrasseur, N.
Related Collections
Right arrowRelated Article
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?

In This Issue

ER domains



Rough ER (box 1, note ribosomes aligned along the ER membrane) is replaced by smooth ER at the bud neck (box 2).

On page 897, Luedeke et al. show that, like the plasma membrane, the ER can be compartmentalized into distinct membrane domains. In budding yeast, this separation restricts the diffusion of ER membrane proteins between the bud and the mother cell.

The mRNAs of many bud-specific membrane proteins are actively transported into the bud. To keep these mRNAs and proteins in the bud, they must be kept from diffusing back into the mother cell through the ER, which traverses the bud neck. Using FRAP analyses, the authors show that proteins are kept in the bud via a diffusion barrier at the bud neck, where rough ER is replaced by a band of smooth ER.

The lumen of the ER was continuous, as shown by EM and by the exchange of lumenal ER proteins. But ER membrane proteins did not exchange—those in the bud stayed in the bud.

At the plasma membrane, mother and bud are separated by a ring of septin, which the authors show also controls ER separation. Septin mutants lost the diffusion barrier and the smooth ER band. Downstream of septin, the loss of Bud6 impaired the diffusion barrier, but did not affect smooth ER formation. Perhaps Bud6 organizes ER lipids into raft domains to create the blockade. For now, however, the contributions of lipids to this system are unknown.

In addition to its contribution to polarity, the unusual ER at the bud neck might control cytokinesis. For instance, if bud neck ER contains a higher concentration of calcium channels, it might control the localized calcium release that initiates contraction of the actomyosin ring. The domain might also pinch the ER in two at or before cytokinesis. The task now will be to determine whether ER compartmentalization exists in higher eukaryotes. {iti_end}



Nicole LeBrasseur

lebrasn{at}rockefeller.edu


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?

Related Article

Septin-dependent compartmentalization of the endoplasmic reticulum during yeast polarized growth
Cosima Luedeke, Stéphanie Buvelot Frei, Ivo Sbalzarini, Heinz Schwarz, Anne Spang, and Yves Barral
J. Cell Biol. 2005 169: 897-908. [Abstract] [Full Text] [PDF]




This Article
Right arrow Full Text (PDF, 613K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by LeBrasseur, N.
Right arrow Search for Related Content
PubMed
Right arrow Articles by LeBrasseur, N.
Related Collections
Right arrowRelated Article
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?


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