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• W2086044657 startingPage "14514" @default.
• W2086044657 abstract "Ca(2+) in neurons is vital to processes such as neurotransmission, neurotoxicity, synaptic development, and gene expression. Disruption of Ca(2+) homeostasis occurs in brain aging and in neurodegenerative disorders. Membrane transporters, among them the calmodulin (CaM)-activated plasma membrane Ca(2+) ATPases (PMCAs) that extrude Ca(2+) from the cell, play a key role in neuronal Ca(2+) homeostasis. Using X-exome sequencing we have identified a missense mutation (G1107D) in the CaM-binding domain of isoform 3 of the PMCAs in a family with X-linked congenital cerebellar ataxia. PMCA3 is highly expressed in the cerebellum, particularly in the presynaptic terminals of parallel fibers-Purkinje neurons. To study the effects of the mutation on Ca(2+) extrusion by the pump, model cells (HeLa) were cotransfected with expression plasmids encoding its mutant or wild-type (wt) variants and with the Ca(2+)-sensing probe aequorin. The mutation reduced the ability of the PMCA3 pump to control the cellular homeostasis of Ca(2+). It significantly slowed the return to baseline of the Ca(2+) transient induced by an inositol-trisphosphate (InsP(3))-linked plasma membrane agonist. It also compromised the ability of the pump to oppose the influx of Ca(2+) through the plasma membrane capacitative channels." @default.
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• W2086044657 date "2012-08-21" @default.
• W2086044657 modified "2023-10-14" @default.
• W2086044657 title "Mutation of plasma membrane Ca ²⁺ ATPase isoform 3 in a family with X-linked congenital cerebellar ataxia impairs Ca ²⁺ homeostasis" @default.
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• W2086044657 doi "https://doi.org/10.1073/pnas.1207488109" @default.
• W2086044657 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3437887" @default.
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