JCB logo
Get More Out of Microscopy - Agilent iMIC 2000
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

Published online April 23, 2007
doi:10.1083/jcb.1773rr3
The Journal of Cell Biology, Vol. 177, No. 3, 372a-
The Rockefeller University Press, 0021-9525 $30.00
© 2007 LeBrasseur
This Article
Right arrow PDF (Full Text)
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 Reddit   Add to Technorati  
What's this?

Research Roundup

Linking division and growth


Figure 1
Vesicles delivering new surface materials in the growing bud are missing (right) when Cdk1 activity is blocked.

KELLOGG/MACMILLAN

Aprotein that pushes forward the cell cycle coordinates division with the ensuing growth of the cell surface, according to work from Derek McCusker, Douglas Kellogg (University of California, Santa Cruz, CA), and colleagues.

It's well accepted that progress through the cell cycle depends on cell growth. In contrast, says Kellogg, "general thinking held that growth is continuous and independent of the cell cycle."

But McCusker et al. now show that Cdk1, which triggers the G1 to S phase transition in budding yeast, also directly promotes the bud's growth. Bud growth quickly stalled upon blocking Cdk1 activity. The stall stemmed from a loss of polarized secretion. Normal cells placed secretory components such as vesicle tethering proteins and a myosin motor at the growing bud tip, but these proteins were rapidly delocalized when Cdk1 was inhibited.

The group then sought targets of Cdk1 that regulated cell surface growth. Several proteins that depended on Cdk1 for phosphorylation during bud growth were found in a complex that included a guanine nucleotide exchange factor and an activating protein for the Cdc42 GTPase, which is required for polarized cell growth. How phosphorylation of proteins in this complex leads to new bud membrane addition is not yet clear. The complex might orient the actin cytoskeleton in the right direction for secretion, although at least one affected secretory protein did not require actin for its polarization. Formula

Reference:

McCusker, D., et al. 2007. Nat. Cell Biol. doi: 10.1038/ncb1568



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 Reddit Reddit   Add to Technorati Technorati    What's this?



This Article
Right arrow PDF (Full Text)
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 Reddit   Add to Technorati  
What's this?


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