Molecular Biology of the Cell Call for Nominations: MBC Editor-in-Chief

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print June 7, 2006
Mol. Biol. Cell 10.1091/mbc.E06-04-0371

A more recent version of this article appeared on August 1, 2006
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E06-04-0371v1
17/8/3423    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tsang, W. Y.
Right arrow Articles by Dynlacht, B. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tsang, W. Y.
Right arrow Articles by Dynlacht, B. D.

Submitted on May 1, 2006
Revised on May 18, 2006
Accepted on May 25, 2006

CP110 Cooperates with Two Calcium-binding Proteins to Regulate Cytokinesis and Genome Stability

William Y. Tsang,* Alexander Spektor,* Daniel J. Luciano,* Vahan B. Indjeian,{dagger} Zhihong Chen,{ddagger} Jeffery L. Salisbury,{sect} Irma Sánchez,* and Brian David Dynlacht*

*Department of Pathology, New York University School of Medicine, New York, NY 10016; {dagger}Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138; {ddagger}Esai Research Institute, Andover, MA 01810; {sect}Tumor Biology Program, Mayo Clinic, Rochester, MN 55905

Monitoring Editor: Trisha Davis

The centrosome is an integral component of the eukaryotic cell cycle machinery, yet very few centrosomal proteins have been fully characterized to date. We have undertaken a series of biochemical and RNA interference (RNAi) studies to elucidate a role for CP110 in the centrosome cycle. Using a combination of yeast two-hybrid screens and biochemical analyses, we report that CP110 interacts with two different Ca2+-binding proteins, calmodulin (CaM) and centrin, in vivo. In vitro binding experiments reveal a direct, robust interaction between CP110 and CaM and the existence of multiple high-affinity CaM-binding domains in CP110. Native CP110 exists in large (~300 kDa to 3 MDa) complexes that contain both centrin and CaM. We investigated a role for CP110 in CaM-mediated events using RNAi and show that its depletion leads to a failure at a late stage of cytokinesis and the formation of binucleate cells, mirroring the defects resulting from ablation of either CaM or centrin function. Importantly, expression of a CP110 mutant unable to bind CaM also promotes cytokinesis failure and binucleate cell formation. Taken together, our data demonstrate a functional role for CaM-binding to CP110 and suggest that CP110 cooperates with CaM and centrin to regulate progression through cytokinesis.

Address correspondence to: Brian David Dynlacht (brian.dynlacht{at}med.nyu.edu)




This article has been cited by other articles:


Home page
 Mol. Biol. CellHome page
A. Selvapandiyan, P. Kumar, J. C. Morris, J. L. Salisbury, C. C. Wang, and H. L. Nakhasi
Centrin1 Is Required for Organelle Segregation and Cytokinesis in Trypanosoma brucei
Mol. Biol. Cell, September 1, 2007; 18(9): 3290 - 3301.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
J. Azimzadeh and M. Bornens
Structure and duplication of the centrosome
J. Cell Sci., July 1, 2007; 120(13): 2139 - 2142.
[Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2006 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.