HspB5/αB-crystallin phosphorylation at S45 and S59 is essential for protection of the dendritic tree of rat hippocampal neurons.
Dendritic branching
HspB5/αB-crystallin
hippocampus
neurodegenerative diseases
neuroprotection
phosphorylation
Journal
Journal of neurochemistry
ISSN: 1471-4159
Titre abrégé: J Neurochem
Pays: England
ID NLM: 2985190R
Informations de publication
Date de publication:
06 2021
06 2021
Historique:
revised:
26
10
2020
received:
10
07
2020
accepted:
18
11
2020
pubmed:
22
11
2020
medline:
25
8
2021
entrez:
21
11
2020
Statut:
ppublish
Résumé
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 dendritic length as well as a higher complexity. Finally, the dendritic effect of HspB5 was investigated under a pathophysiological condition, that is, iron deficiency which reportedly results in dendritic rarefaction. HspB5 and HspB5-AEE but not the non-phosphorylatable mutant HspB5-AAA significantly counteracted the dendritic rarefaction. Thus, our data suggest that up-regulation and selective phosphorylation of HspB5 in neurodegenerative diseases may preserve dendritic morphology and counteract neuronal dysfunction.
Substances chimiques
Crystallins
0
Microtubule-Associated Proteins
0
cryaB protein, rat
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2055-2069Informations de copyright
© 2020 The Authors. Journal of Neurochemistry published by John Wiley & Sons Ltd on behalf of International Society for Neurochemistry.
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