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

Published online 20 October 2003. doi:10.1083/jcb1632rr3
This Article
Right arrow Full Text (PDF, 757K)
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.
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?

© The Rockefeller University Press, 0021-9525/2003/10/201 $8.00
The Journal of Cell Biology, Volume 163, Number 2, 201-201


Research Roundup

The kinase knows



Hsl1 (red), is activated at the bud neck by septin binding.

Snyder/Elsevier

CFells monitor the assembly of cytoskeletal structures via direct binding and activation of a checkpoint kinase, as shown by Jessie Hanrahan and Michael Snyder (Yale University, New Haven, CT).

Cytoskeletal reorganization is needed during various events in the cell cycle. In budding yeast, for example, a ring of septin filaments separates the mother cell from the forming bud. The ring must be completed before the cell can enter mitosis. This landmark is signaled by the Hsl1 kinase, which is activated upon ring assembly. Snyder wondered, "how do [cells] recognize when a macromolecular complex like the cytoskeleton is assembled? The thought seems daunting at first." But he found a relatively simple answer for Hsl1—it is either bound to the septin ring or is in an inactive conformation.

The authors identified a site in the large noncatalytic portion of Hsl1 that binds to and inactivates the kinase domain. This autoinhibitory domain overlaps with three sites that bind to two different septin subunits. In vitro, septins activate the kinase by displacing the inhibitory domain. In vivo, the septins have to be polymerized, as previous results showed that unassembled subunits do not activate Hsl1. This may be due to the spacing of the septin binding sites and the need for all three sites to be filled to displace the inhibitory domain.

This sensing mechanim may extend to other cytoskeletal structures. Microtubules, for instance, are bound by a relative of Hsl1 called MARK. Says Snyder, "[the Hsl1 model] is attractive as a universal mechanism to monitor assembly of cytoskeletons specifically, and maybe macromolecular complexes in general." {blacksquare}

Reference:

Hanrahan, J., et al. 2003. Mol. Cell. 12:663–673.[CrossRef][Medline]



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?



This Article
Right arrow Full Text (PDF, 757K)
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.
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