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1000
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Abstract/Summary
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Neurons express more genes than any other cell type and it is therefore unlikely that synapto–nuclear Ca2+ signaling alone can explain the specific genomic response to the plethora of extracellular stimuli that control gene expression. Possible candidates for encoding of signals at the origin and later decoding at a nuclear destination are synapto–nuclear protein messenger. These proteins translocate to the nucleus in a stimulus-dependent manner, where they can regulate via their nuclear target interactions very specific aspects of gene expression (Jordan and Kreutz, 2009). However, this type of signaling is challenged by space and time constraints. Synapses are localized far away from the nucleus and synaptic signals are very labile and rapidly degraded. On top the minute quantities of signaling molecules that can be released from synaptic sites are greatly diluted in relation to the entire volume of the dendritic arborization or nucleus. A precise machinery is therefore required to deliver the signal to nuclear target sites, but unfortunately very little is known on just how protein messenger can translocate several hundred micrometers, avoid degradation, retain signal and do this in a reliable manner.
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