Abstract
Caldendrin is the first member of a novel family of Ca2+-binding proteins (CaBPs). Its unique two-domain structure is composed of a calmodulin-homologous C-terminus and an unrelated N-terminal part. The latter is thought to mediate the tight association of caldendrin with the subsynaptic cytoskeleton. Caldendrin is expressed in forebrain regions with a laminar cytoarchitecture as well as in the inner retina where it is localized to OFF cone bipolar and a subset of amacrine and ganglion cells. In addition, caldendrin is prominently present in processes and synapses of the inner plexiform layer. Thus, caldendrin-immunoreactivity is displayed by subpopulations of most retinal cell classes, with the exception of glial cells. Caldendrin is most likely involved in dendritic Ca2+-signaling, one of the functions of its close relative, calmodulin. However, several lines of evidence suggest that due to its unique properties caldendrin might not merely substitute for calmodulin. It is speculated that either the specific enrichment in cellular micro-compartments like the postsynaptic cytomatrix, the unique two-domain structure or the altered distribution of surface charges renders caldendrin specific for distinct binding partners or certain Ca2+-triggered signaling events.
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Seidenbecher, C.I., Reissner, C., Kreutz, M.R. (2002). Caldendrins in the Inner Retina. In: Baehr, W., Palczewski, K. (eds) Photoreceptors and Calcium. Advances in Experimental Medicine and Biology, vol 514. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0121-3_27
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DOI: https://doi.org/10.1007/978-1-4615-0121-3_27
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