JCB logo
Quantitative Colocalization Analysis Software
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

Published online 9 August 2004. doi:10.1083/jcb1664rr4
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 166, Number 4, 445-445
This Article
Right arrow Full Text (PDF, 762K)
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 Wells, W. A.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Wells, W. A.
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?

Research Roundup

Corralled by septin



Septins (red) corral division proteins (Spa2; green) at the bud neck.

Barral/AAAS

Septin filaments in budding yeast make a corral that restricts certain division proteins to the site of cytokinesis, according to Jeroen Dobbelaere and Yves Barral (ETHZ, Zurich, Switzerland).

The corral is formed when the septin ring at the bud neck splits to form two parallel fences. The Swiss researchers had earlier noted that during this period septin becomes transiently mobile before reverting to a static organization.

They have now extended this investigation of mobility to other cytokinesis proteins. Three membrane-associated proteins involved in polarizing the actin cytoskeleton (Spa2), secretion (Sec3), and delivering cell wall to the division site (Chs2) were all extremely mobile at the division site, but did not diffuse to regions outside of the division site. Disruption of the septin barriers via a temperature-sensitive mutant led to rapid loss of the division proteins from the bud neck and cytokinesis failure.

This trapping function for septins contrasts with their function earlier in the budding yeast cell cycle, when septins act as a scaffold that recruits other division proteins. But the later, membrane-associated division proteins do not colocalize with septins. Instead, they bounce around between the two wall-like septin rings. The split rings of fission yeast septin and even the septin patches seen in mammalian cells may perform a similar function.

Dobbelaere suspects that the division proteins may be endocytosed and then delivered via vesicles to the site between the septin rings. The alternative is that membrane-associated proteins slip through the septin rings when the rings are flexible and then are trapped when the rings regain their solidity. {blacksquare}

Reference:

Dobbelaere, J., and Y. Barral. 2004. Science. 305:393–396.[Abstract/Free Full Text]



William A. Wells

wellsw{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?



This Article
Right arrow Full Text (PDF, 762K)
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 Wells, W. A.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Wells, W. A.
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