Phosphorylation of Focal Adhesion Kinase at Y925: Role in Glia-Dependent and Independent Migration through Regulating Cofilin and N-Cadherin.
Cofilin
Focal adhesion kinase
Locomotion
N-Cadherin
Reelin
Translocation
Journal
Molecular neurobiology
ISSN: 1559-1182
Titre abrégé: Mol Neurobiol
Pays: United States
ID NLM: 8900963
Informations de publication
Date de publication:
Jun 2022
Jun 2022
Historique:
received:
11
11
2021
accepted:
16
02
2022
pubmed:
25
3
2022
medline:
1
6
2022
entrez:
24
3
2022
Statut:
ppublish
Résumé
The adult neocortex is a six-layered structure, consisting of nearly continuous layers of neurons that are generated in a temporally strictly coordinated order. During development, cortical neurons originating from the ventricular zone migrate toward the Reelin-containing marginal zone in an inside-out arrangement. Focal adhesion kinase (FAK), one tyrosine kinase localizing to focal adhesions, has been shown to be phosphorylated at tyrosine 925 (Y925) by Src, an important downstream molecule of Reelin signaling. Up to date, the precise molecular mechanisms of FAK and its phosphorylation at Y925 during neuronal migration are still unclear. Combining in utero electroporation with immunohistochemistry and live imaging, we examined the function of FAK in regulating neuronal migration. We show that phosphorylated FAK is colocalized with Reelin positive Cajal-Retzius cells in the developing neocortex and hippocampus. Phosphorylation of FAK at Y925 is significantly reduced in reeler mice. Overexpression and dephosphorylation of FAK impair locomotion and translocation, resulting in migration inhibition and dislocation of both late-born and early-born neurons. These migration defects are highly correlated to the function of FAK in regulating cofilin phosphorylation and N-Cadherin expression, both are involved in Reelin signaling pathway. Thus, fine-tuned phosphorylation of focal adhesion kinase at Y925 is crucial for both glia-dependent and independent neuronal migration.
Identifiants
pubmed: 35325397
doi: 10.1007/s12035-022-02773-y
pii: 10.1007/s12035-022-02773-y
doi:
Substances chimiques
Actin Depolymerizing Factors
0
Cadherins
0
Focal Adhesion Protein-Tyrosine Kinases
EC 2.7.10.2
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
3467-3484Subventions
Organisme : Top talent recruitment of Xi'an Medical University
ID : 2018RCYJ04
Organisme : General project of basic research of Shaanxi Province
ID : 2020JM-603
Organisme : National Key Research and Development Program of China
ID : 2018YFE0127000
Organisme : Deutsche Forschungsgemeinschaft
ID : FR 620/13-1
Informations de copyright
© 2022. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
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