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

Published online 16 October 2006. doi:10.1083/jcb.1752rr2
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 175, Number 2, 197-197
This Article
Right arrow Full Text (PDF, 969K)
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

Spinning septins



Figure 1
Septins spin in a polarizing microscope (top) as septin rings mature (bottom).

VRABIOIU/MACMILLAN

Septin filaments in yeast do a right-angled turn in the middle of cell division, according to Alina Vrabioiu and Tim Mitchison (Harvard Medical School, Boston, MA). The filaments initially align parallel to the spindle axis but then rotate 90° to form two circumferential rings that flank the cytokinetic furrow.

Septin filaments help cells divide, but just how they do so has remained mysterious. The direction of septin-dependent striations varied between experiments, plus the striations may have been a pattern set up by proteins that bind septins, not the septins themselves.

Now, the Boston team has directly monitored the direction of septin filaments. They attached a green fluorescent protein (GFP) to septin by linking together two rigid {alpha}-helices. Polymerizing the septin–GFP molecules in a filament lined up all the GFPs. Polarized light would effectively excite these GFPs only when the light's electromagnetic oscillations were aligned with the GFPs' dipoles—the direction along which an excited electron preferentially moves to the higher energy state.

The team established in vitro what direction of polarized light best excited a filament of known orientation. Applying this to in vivo data, in which polarized light excited septin–GFP in cells whose orientation was carefully controlled, they could deduce the direction of septin filaments in vivo.

The septins are initially aligned parallel to the spindle axis, in an hourglass shape that spans the bud neck. Dephosphorylation has been implicated in reshaping the septins into two rings; if it acts selectively in the middle of the hourglass it might detach septins at one end with the other end providing a pivot point. The force driving turning might then come from membrane insertion between the two rings. Formula

Reference:

Vrabioiu, A.M., and T.J. Mitchison. 2006. Nature. 443:466–469.[CrossRef][Medline]



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, 969K)
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