JCB logo
amgmicro.com
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online 3 January 2002. doi:10.1083/jcb1561iti2
This Article
Right arrow Full Text (PDF, 232K)
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.
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?

© The Rockefeller University Press, 0021-9525/2002/1/9 $5.00
The Journal of Cell Biology, Volume 156, Number 1, January 7, 2002 9-9

In This Issue

Polo meets the APC


Mitotic arrest results when APC and Plo1 cannot interact.

Polo kinases have been linked to activation of the anaphase promoting complex (APC) during mitosis, but the importance of this effect has been debated. Now, May et al. study this problem using polo-like kinase Plo1 from fission yeast (page 23). They show that Plo1-mediated activation is essential—a metaphase arrest results when Plo1 can no longer bind avidly to the Cdc23 subunit of the APC.

The authors came to this conclusion after identifying mutants that were dependent on high Plo1 expression for their survival. One of the mutants made a Cdc23 protein that interacted poorly with Plo1, a deficit that May et al. suggest is overcome by excess Plo1. Following up on this clue, May et al. mapped the Plo1–Cdc23 interaction to the noncatalytic domain of Plo1 and the TPR domain of Cdc23.

The APC subunit or residues that act as the Plo1 target remain unknown. In tracking down this target, May et al. plan to continue their analysis of the APC at the level of individual subunits or residues rather than as a whole complex. {blacksquare}



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?

Related Article

Polo boxes and Cut23 (Apc8) mediate an interaction between polo kinase and the anaphase-promoting complex for fission yeast mitosis
Karen M. May, Nicola Reynolds, C. Fiona Cullen, Mitsuhiro Yanagida, and Hiroyuki Ohkura
J. Cell Biol. 2002 156: 23-28. [Abstract] [Full Text] [PDF]




This Article
Right arrow Full Text (PDF, 232K)
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.
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