Abstract
Caldendrin and recoverin are Ca(2+)-sensor proteins operating in neuronal systems. In a search for novel binding partners of recoverin, we employed an affinity column and identified caldendrin as a possible interaction partner. Caldendrin and recoverin co-localized in the retina in a subset of bipolar cells and in the pineal gland as revealed by immunofluorescence studies. The binding process was controlled by Ca(2+) as revealed by pull-down assays, and surface plasmon resonance studies. Importantly, caldendrin existed as a Ca(2+)-independent homodimer whereas a complex of recoverin and caldendrin formed with low to moderate affinity in the presence of Ca(2+). Co-transfection of COS-7 cells with plasmids harboring the gene for fluorescently labeled recoverin and caldendrin was used to study the cellular distribution by time-lapse fluorescence microscopy. Apparently, the increase of intracellular Ca(2+) facilitates the translocation of caldendrin to intracellular membranes, which is under control of complex formation with recoverin.