Tsang, William Y; Spektor, Alexander; Luciano, Daniel J; Indjeian, Vahan B; Chen, Zhihong; Salisbury, Jeffery L; Sanchez, Irma; Dynlacht, Brian David
"CP110 Cooperates with Two Calcium-binding Proteins to Regulate Cytokinesis and Genome Stability"
Molecular biology of the cell 2006 Aug; 17(8):3423-3434
- 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 Ca(2+)-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 ( approximately 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
Check for full text:
# 66471 (MEDL:16760425)
This publication list a product of the NYU Faculty Bibliography.