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• W2034656159 abstract "The hexa-EF-hand Ca2+-binding protein calretinin (CR) is predominantly expressed in specific neurons of the central and peripheral nervous system. However, CR expression is also observed in non-neuronal cells, e.g. during embryonic development and in mesothelioma cells. Of the 6 EF-hand domains, 5 are functional; the first 4 domains form 2 pairs showing high cooperativity within a pair that results in non-linear modulation of intracellular Ca2+ signals by CR. EF-hand domain 5 has a low affinity and represents the identified interaction site with CR-binding partners present in mouse cerebellar granule cells. CR binding to other targets including the pore-forming α1 subunit of the Ca2+ channel CaV2.1, as well as to huntingtin indicates additional Ca2+ sensor functions besides the well-known Ca2+-buffering functions. The absence of CR in cerebellar granule cells of CR-/- mice results in increased excitability and altered firing of Purkinje cells and promotes cerebellar 160-Hz oscillations impairing motor coordination. The putative role of CR in neuroprotection is still highly discussed. Altogether, CR emerges as a multi-functional protein also associated with development, i.e. cell proliferation, differentiation and cell death." @default.
• W2034656159 created "2016-06-24" @default.
• W2034656159 creator A5087948193 @default.
• W2034656159 date "2014-01-01" @default.
• W2034656159 modified "2023-10-17" @default.
• W2034656159 title "Calretinin: from a “simple” Ca2+ buffer to a multifunctional protein implicated in many biological processes" @default.
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• W2034656159 doi "https://doi.org/10.3389/fnana.2014.00003" @default.
• W2034656159 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3913827" @default.
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