Memory Decline and Its Reversal in Aging and Neurodegeneration Involve miR-183/96/182 Biogenesis.
Aging
/ pathology
Amyotrophic Lateral Sclerosis
/ genetics
Animals
Cell Line, Tumor
Cell Nucleus
/ metabolism
Cognition Disorders
/ genetics
Frontotemporal Lobar Degeneration
/ genetics
Hippocampus
/ metabolism
Humans
Memory Disorders
/ complications
Mice, Inbred C57BL
MicroRNAs
/ biosynthesis
Nerve Degeneration
/ complications
Protein Phosphatase 1
/ metabolism
RNA-Binding Protein FUS
/ metabolism
Smad Proteins
/ metabolism
Dementia
FUS
Memory
Protein phosphatase 1
TDP-43
microRNA
Journal
Molecular neurobiology
ISSN: 1559-1182
Titre abrégé: Mol Neurobiol
Pays: United States
ID NLM: 8900963
Informations de publication
Date de publication:
May 2019
May 2019
Historique:
received:
11
05
2018
accepted:
09
08
2018
pubmed:
22
8
2018
medline:
14
8
2019
entrez:
22
8
2018
Statut:
ppublish
Résumé
Aging is characterized by progressive memory decline that can lead to dementia when associated with neurodegeneration. Here, we show in mice that aging-related memory decline involves defective biogenesis of microRNAs (miRNAs), in particular miR-183/96/182 cluster, resulting from increased protein phosphatase 1 (PP1) and altered receptor SMAD (R-SMAD) signaling. Correction of the defect by miR-183/96/182 overexpression in hippocampus or by environmental enrichment that normalizes PP1 activity restores memory in aged animals. Regulation of miR-183/96/182 biogenesis is shown to involve the neurodegeneration-related RNA-binding proteins TDP-43 and FUS. Similar alterations in miR-183/96/182, PP1, and R-SMADs are observed in the brains of patients with amyotrophic lateral sclerosis (ALS) or frontotemporal lobar degeneration (FTLD), two neurodegenerative diseases with pathological aggregation of TDP-43. Overall, these results identify new mechanistic links between miR-183/96/182, PP1, TDP-43, and FUS in age-related memory deficits and their reversal.
Identifiants
pubmed: 30128653
doi: 10.1007/s12035-018-1314-3
pii: 10.1007/s12035-018-1314-3
doi:
Substances chimiques
MicroRNAs
0
RNA-Binding Protein FUS
0
Smad Proteins
0
Protein Phosphatase 1
EC 3.1.3.16
Types de publication
Journal Article
Langues
eng
Pagination
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