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Updated: Aug 23, 2026

Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
Calmodulin-binding domains in Alzheimer's disease proteins: extending the calcium hypothesis
Danton H O'Day1, Michael A Myre
1Department of Biology, University of Toronto at Mississauga, 3359 Mississauga Rd., Mississauga, Ont., Canada L5L 1C6. doday@utm.utoronto.ca
Abstract:
The calcium hypothesis of Alzheimer's disease (AD) invokes the disruption of calcium signaling as the underlying cause of neuronal dysfunction and ultimately apoptosis. As a primary calcium signal transducer, calmodulin (CaM) responds to cytosolic calcium fluxes by binding to and regulating the activity of target CaM-binding proteins (CaMBPs). Ca(2+)-dependent CaMBPs primarily contain domains (CaMBDs) that can be classified into motifs based upon variations on the basic amphiphilic alpha-helix domain involving conserved hydrophobic residues at positions 1-10, 1-14 or 1-16. In contrast, an IQ or IQ-like domain often mediates Ca(2+)-independent CaM-binding. Based on these attributes, a search for CaMBDs reveals that many of the proteins intimately linked to AD may be calmodulin-binding proteins, opening new avenues for research on this devastating disease.
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