Tumor suppressor protein CYLD regulates morphogenesis of dendrites and spines.
Acetylation
Animals
Cell Differentiation
Cells, Cultured
Dendrites
/ ultrastructure
Dendritic Spines
/ ultrastructure
Deubiquitinating Enzyme CYLD
/ genetics
Gene Knockdown Techniques
Hippocampus
/ ultrastructure
Mice
Microtubules
/ metabolism
Morphogenesis
/ genetics
Primary Cell Culture
Protein Binding
Tubulin
/ metabolism
dendritic morphogenesis
hippocampal neuron
microtubule
spine formation
tubulin acetylation
Journal
The European journal of neuroscience
ISSN: 1460-9568
Titre abrégé: Eur J Neurosci
Pays: France
ID NLM: 8918110
Informations de publication
Date de publication:
08 2019
08 2019
Historique:
received:
26
09
2018
accepted:
01
04
2019
pubmed:
20
4
2019
medline:
12
8
2020
entrez:
20
4
2019
Statut:
ppublish
Résumé
Cylindromatosis tumor suppressor protein (CYLD) was initially identified as a tumor suppressor deubiquitylating protein in familial cylindromatosis patients. Proteomic analyses using rodent brain samples revealed enrichment of CYLD in purified postsynaptic density fractions. Here, we report that CYLD regulates dendritic growth and postsynaptic differentiation in mouse hippocampal neurons. CYLD showed diffuse localization in rapidly growing dendrites, but was gradually concentrated in spines. Overexpression and knockdown of CYLD in the early stage of cultured neurons demonstrated that CYLD positively regulated dendritic growth. Phenotypes in dendritic morphogenesis induced by CYLD overexpression and knockdown could be reversed by manipulation of the critical acetylation site of α-tubulin, suggesting tubulin acetylation is a downstream pathway of CYLD-dependent dendritic growth. Overexpression and knockdown of CYLD in the later stage of cultured neurons revealed that CYLD promoted formation of postsynaptic spines. Influence of CYLD on spines was not affected by co-expression of acetylation mutant forms of α-tubulin, indicating that CYLD regulates dendritic growth and spine formation through different molecular mechanisms. Analyses with the truncated and mutated forms of CYLD demonstrated that the first microtubule-binding domain of CYLD was critical for spine formation. These results suggest important roles of CYLD in sequential promotion of dendritic growth and postsynaptic spine maturation.
Substances chimiques
Tubulin
0
CYLD protein, mouse
EC 3.4.19.12
Deubiquitinating Enzyme CYLD
EC 3.4.19.12
Banques de données
GENBANK
['NM_173369']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2722-2739Informations de copyright
© 2019 Federation of European Neuroscience Societies and John Wiley & Sons Ltd.
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