Phosphorylated septin 3 delocalizes from the spine base and facilitates endoplasmic reticulum extension into spines via myosin-Va DOI Creative Commons
Natsumi Ageta‐Ishihara, Makoto Mizukami,

I. Kinoshita

и другие.

Molecular Brain, Год журнала: 2025, Номер 18(1)

Опубликована: Май 15, 2025

Abstract Cytoskeletal remodeling drives morphological changes. Septin cytoskeleton assembles into hetero-oligomers. We previously demonstrated that late-phase long-term potentiation (L-LTP) induces smooth endoplasmic reticulum (sER) extension dendritic spines via septin 3 (SEPT3), contributing to greater postsynaptic Ca 2+ responses and enhanced activation of synaptically induced signaling. Sept3 −/− mice exhibit a reduced number sER-containing show impaired spatial/object memory despite normal short-term memory. Additionally, SEPT3 binds the motor protein myosin-Va (MYO5A) upon elevated Ca²⁺ concentrations, facilitating sER from shaft spine. MYO5A localizes on membrane, while remains at spine base, accumulating electroconvulsive stimulation (ECS). However, mechanism underlying SEPT3’s delocalization base its cooperative role with in unclear. In this study, we demonstrate is phosphorylated stimulation-dependent manner. Phosphorylation Thr211 releases enabling constitutively active mutant (MYO5A-CCtr). These findings provide molecular insight phosphorylation regulating dynamics sustain activation.

Язык: Английский

Phosphorylated septin 3 delocalizes from the spine base and facilitates endoplasmic reticulum extension into spines via myosin-Va DOI Creative Commons
Natsumi Ageta‐Ishihara, Makoto Mizukami,

I. Kinoshita

и другие.

Molecular Brain, Год журнала: 2025, Номер 18(1)

Опубликована: Май 15, 2025

Abstract Cytoskeletal remodeling drives morphological changes. Septin cytoskeleton assembles into hetero-oligomers. We previously demonstrated that late-phase long-term potentiation (L-LTP) induces smooth endoplasmic reticulum (sER) extension dendritic spines via septin 3 (SEPT3), contributing to greater postsynaptic Ca 2+ responses and enhanced activation of synaptically induced signaling. Sept3 −/− mice exhibit a reduced number sER-containing show impaired spatial/object memory despite normal short-term memory. Additionally, SEPT3 binds the motor protein myosin-Va (MYO5A) upon elevated Ca²⁺ concentrations, facilitating sER from shaft spine. MYO5A localizes on membrane, while remains at spine base, accumulating electroconvulsive stimulation (ECS). However, mechanism underlying SEPT3’s delocalization base its cooperative role with in unclear. In this study, we demonstrate is phosphorylated stimulation-dependent manner. Phosphorylation Thr211 releases enabling constitutively active mutant (MYO5A-CCtr). These findings provide molecular insight phosphorylation regulating dynamics sustain activation.

Язык: Английский

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