HspB5/αB-crystallin phosphorylation at S45 and S59 is essential for protection of the dendritic tree of rat hippocampal neurons.

Journal of Neurochemistry
Britta Bartelt-KirbachNikola Golenhofen

Abstract

Rarefaction of the dendritic tree leading to neuronal dysfunction is a hallmark of many neurodegenerative diseases and we have shown previously that heat shock protein B5 (HspB5)/αB-crystallin is able to increase dendritic complexity in vitro. The aim of this study was to investigate if this effect is also present in vivo, if HspB5 can counteract dendritic rarefaction under pathophysiological conditions and the impact of phosphorylation of HspB5 in this process. HspB5 and eight mutants inhibiting or mimicking phosphorylation at the three phosphorylation sites serine (S)19, S45, and S59 were over-expressed in cultured rat hippocampal neurons with subsequent investigation of the complexity of the dendritic tree. Sholl analysis revealed significant higher complexity of the dendritic tree after over-expression of wild-type HspB5 and the mutant HspB5-AEE. All other mutants showed no or minor effects. For in vivo investigation in utero electroporation of mouse embryos was applied. At embryonal day E15.5 the respective plasmids were injected, cornu ammonis 1 (CA1) pyramidal cells transfected by electroporation and their basal dendritic trees were analyzed at post-natal day P15. In vivo, HspB5 and HspB5-AEE led to an increase of total ...Continue Reading

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