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CP110 cooperates with two calcium-binding proteins to regulate cytokinesis and genome stability.

http://www.ncbi.nlm.nih.gov/pubmed/16760425

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 (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.

Pubmed ID: 16760425 RIS Download

Mesh terms: Calcium-Binding Proteins | Calmodulin | Cell Cycle Proteins | Cytokinesis | Gene Expression | Genomic Instability | HeLa Cells | Humans | Microtubule-Associated Proteins | Molecular Weight | Multiprotein Complexes | Mutation | Phenotype | Phosphoproteins | Polyploidy | Protein Binding | Protein Structure, Tertiary | Protein Transport | RNA Interference

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