Gamma‐protocadherin localization at the synapse is associated with parameters of synaptic maturation

2021 ◽  
Author(s):  
Nicole LaMassa ◽  
Hanna Sverdlov ◽  
Aliya Mambetalieva ◽  
Stacy Shapiro ◽  
Michael Bucaro ◽  
...  
Keyword(s):  
Synaptic Maturation

scholarly journals Self-amplified BDNF transcription is a regulatory system for synaptic maturation in cultured cortical neurons

2015 ◽  
Vol 91 ◽  
pp. 55-61 ◽  
Author(s):  
Shingo Nakajima ◽  
Tadahiro Numakawa ◽  
Naoki Adachi ◽  
Yoshiko Ooshima ◽  
Haruki Odaka ◽  
...  
Keyword(s):  
Cortical Neurons ◽  
Regulatory System ◽  
Cultured Cortical Neurons ◽  
Synaptic Maturation ◽  
Bdnf Transcription

scholarly journals CBP and SRF co-regulate dendritic growth and synaptic maturation

2019 ◽  
Vol 26 (11) ◽  
pp. 2208-2222 ◽  
Author(s):  
Beatriz del Blanco ◽  
Deisy Guiretti ◽  
Romana Tomasoni ◽  
María T. Lopez-Cascales ◽  
Rafael Muñoz-Viana ◽  
...  
Keyword(s):  
Dendritic Growth ◽  
Synaptic Maturation

scholarly journals Synaptic maturation of theXenopusretinotectal system: Effects of brain-derived neurotrophic factor on synapse ultrastructure

2010 ◽  
Vol 518 (7) ◽  
pp. 972-989 ◽  
Author(s):  
Angeliki Maria Nikolakopoulou ◽  
Margarita M. Meynard ◽  
Sonya Marshak ◽  
Susana Cohen-Cory
Keyword(s):  
Neurotrophic Factor ◽  
Brain Derived Neurotrophic Factor ◽  
Synapse Ultrastructure ◽  
Synaptic Maturation

Disturbance of cerebellar synaptic maturation in mutant mice lacking BSRPs, a novel brain-specific receptor-like protein family

FEBS Letters ◽  
2006 ◽  
Vol 580 (17) ◽  
pp. 4057-4064 ◽  
Author(s):  
Taisuke Miyazaki ◽  
Kouichi Hashimoto ◽  
Atsushi Uda ◽  
Hiroyuki Sakagami ◽  
Yoshitaka Nakamura ◽  
...  
Keyword(s):  
Protein Family ◽  
Mutant Mice ◽  
Specific Receptor ◽  
Synaptic Maturation

scholarly journals PKN1 Is a Novel Regulator of Hippocampal GluA1 Levels

2021 ◽  
Vol 13 ◽  
Author(s):  
Motahareh Solina Safari ◽  
Dido Obexer ◽  
Gabriele Baier-Bitterlich ◽  
Stephanie zur Nedden
Keyword(s):  
Synaptic Proteins ◽  
The Novel ◽  
Serine Threonine Kinase ◽  
Expression Levels ◽  
Akt Phosphorylation ◽  
Protein Levels ◽  
Subunit Expression ◽  
Enhanced Expression ◽  
Synaptic Maturation ◽  
Specific Regulation

Alterations in the processes that control α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) expression, assembly and trafficking are closely linked to psychiatric and neurodegenerative disorders. We have recently shown that the serine/threonine kinase Protein kinase N1 (PKN1) is a developmentally active regulator of cerebellar synaptic maturation by inhibiting AKT and the neurogenic transcription factor neurogenic differentiation factor-2 (NeuroD2). NeuroD2 is involved in glutamatergic synaptic maturation by regulating expression levels of various synaptic proteins. Here we aimed to study the effect of Pkn1 knockout on AKT phosphorylation and NeuroD2 levels in the hippocampus and the subsequent expression levels of the NeuroD2 targets and AMPAR subunits: glutamate receptor 1 (GluA1) and GluA2/3. We show that PKN1 is expressed throughout the hippocampus. Interestingly, not only postnatal but also adult hippocampal phospho-AKT and NeuroD2 levels were significantly elevated upon Pkn1 knockout. Postnatal and adult Pkn1–/– hippocampi showed enhanced expression of the AMPAR subunit GluA1, particularly in area CA1. Surprisingly, GluA2/3 levels were not different between both genotypes. In addition to higher protein levels, we also found an enhanced GluA1 content in the membrane fraction of postnatal and adult Pkn1–/– animals, while GluA2/3 levels remained unchanged. This points toward a very specific regulation of GluA1 expression and/or trafficking by the novel PKN1-AKT-NeuroD2 axis. Considering the important role of GluA1 in hippocampal development as well as the pathophysiology of several disorders, ranging from Alzheimer’s, to depression and schizophrenia, our results validate PKN1 for future studies into neurological disorders related to altered AMPAR subunit expression in the hippocampus.

scholarly journals Neuroligin-1 mediates presynaptic maturation through brain-derived neurotrophic factor signaling

BMC Biology ◽  
2021 ◽  
Vol 19 (1) ◽  
Author(s):  
Andonia Petkova-Tuffy ◽  
Nina Gödecke ◽  
Julio Viotti ◽  
Martin Korte ◽  
Thomas Dresbach
Keyword(s):  
Cell Adhesion ◽  
Synaptic Vesicle ◽  
Neurotrophic Factor ◽  
Neurodevelopmental Disorders ◽  
Active Zone ◽  
Brain Derived Neurotrophic Factor ◽  
Synaptic Vesicle Recycling ◽  
Vesicle Recycling ◽  
Synapse Maturation ◽  
Synaptic Maturation

Abstract Background Maturation is a process that allows synapses to acquire full functionality, optimizing their activity to diverse neural circuits, and defects in synaptic maturation may contribute to neurodevelopmental disorders. Neuroligin-1 (NL1) is a postsynaptic cell adhesion molecule essential for synapse maturation, a role typically attributed to binding to pre-synaptic ligands, the neurexins. However, the pathways underlying the action of NL1 in synaptic maturation are incompletely understood, and some of its previously observed effects seem reminiscent of those described for the neurotrophin brain-derived neurotrophic factor (BDNF). Here, we show that maturational increases in active zone stability and synaptic vesicle recycling rely on the joint action of NL1 and brain-derived neurotrophic factor (BDNF). Results Applying BDNF to hippocampal neurons in primary cultures or organotypical slice cultures mimicked the effects of overexpressing NL1 on both structural and functional maturation. Overexpressing a NL1 mutant deficient in neurexin binding still induced presynaptic maturation. Like NL1, BDNF increased synaptic vesicle recycling and the augmentation of transmitter release by phorbol esters, both hallmarks of presynaptic maturation. Mimicking the effects of NL1, BDNF also increased the half-life of the active zone marker bassoon at synapses, reflecting increased active zone stability. Overexpressing NL1 increased the expression and synaptic accumulation of BDNF. Inhibiting BDNF signaling pharmacologically or genetically prevented the effects of NL1 on presynaptic maturation. Applying BDNF to NL1-knockout mouse cultures rescued defective presynaptic maturation, indicating that BDNF acts downstream of NL1 and can restore presynaptic maturation at late stages of network development. Conclusions Our data introduce BDNF as a novel and essential component in a transsynaptic pathway linking NL1-mediated cell adhesion, neurotrophin action, and presynaptic maturation. Our findings connect synaptic cell adhesion and neurotrophin signaling and may provide a therapeutic approach to neurodevelopmental disorders by targeting synapse maturation.

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