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

Published online 5 May 2003. doi:10.1083/jcb1613rr4
This Article
Right arrow Full Text (PDF, 816K)
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 Tuma, R. S.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Tuma, R. S.
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, 0021-9525/2003/5/457-a $5.00
The Journal of Cell Biology, Volume 161, Number 3, 457-a-457


Research Roundup

Turning RacGAP into a RhoGAP



MgcRacGAP and RhoA colocalize at the midbody during cytokinesis.

Minoshima/Elsevier

We already knew the players—MgcRacGAP, Aurora B, and RhoA—and that knocking out any one of them caused failure of cytokinesis; but it wasn't clear how they were connected. Now, it appears that Aurora B phosphorylates the GAP domain of MgcRacGAP, allowing it to turn its GAP activity toward RhoA, according to data from Yukinori Minoshima, Toshiyuki Kawashima, Toshio Kitamura (University of Tokyo, Tokyo, Japan), and colleagues.

When they first isolated MgcRacGAP, the group found that most of its activity was directed toward Rac1 and Cdc42, but there were hints—although inconsistent ones—that it also had activity toward Rho proteins. In the new work, Kitamura and colleagues found that, late in mitosis, Aurora B, RhoA, and MgcRacGAP congregate at the midbody, where Aurora B phosphorylates a serine in the GAP domain of MgcRacGAP. The phosphorylated GAP protein then stimulates the GTPase activity of RhoA, converting GTP-bound active RhoA to GDP-bound inactive RhoA, and promotes the completion of cytokinesis and cell division. Overexpression of a phosphorylation-deficient mutant of MgcRacGAP blocks RhoA activity and results in polyploid cells.

"This is the first demonstration that a modification of a GAP changes its target specificity," says Kitamura. "Biologically the interesting thing is that in the beginning of cell division MgcRacGAP probably works through Rac1 and Cdc42, which function in mitotic spindle formation. Then during the late stage of cell division and cytokinesis, MgcRacGAP converts itself to a RhoGAP and exerts itself through RhoA." {blacksquare}

Reference:

Minoshima, Y., et al. 2003. Dev. Cell. 4:549–560.[CrossRef][Medline]



Rabiya S. Tuma

rabiya{at}nasw.org


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, 816K)
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 Tuma, R. S.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Tuma, R. S.
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