Dynamic bi-directional phosphorylation events associated with the reciprocal 
regulation of synapses during homeostatic up- and down-scaling

Desch, Kristina; Langer, Julian David; Schuman, Erin M.

doi:10.1016/j.celrep.2021.109583

アイテム詳細

登録内容を編集ファイル形式で保存

一時保存へ追加

タグ情報を表示リリース履歴を表示詳細要約

公開

学術論文

Dynamic bi-directional phosphorylation events associated with the reciprocal regulation of synapses during homeostatic up- and down-scaling

MPS-Authors

Desch, Kristina
Proteomics (Scientific Service Group), Max Planck Institute for Brain Research, Max Planck Society;

/persons/resource/persons137770

Langer, Julian David
Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society;
Proteomics (Scientific Service Group), Max Planck Institute for Brain Research, Max Planck Society;

Schuman, Erin M.
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

External Resource

There are no locators available

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

フルテキスト (公開)

公開されているフルテキストはありません

付随資料 (公開)

There is no public supplementary material available

引用

Desch, K., Langer, J. D., & Schuman, E. M. (2021). Dynamic bi-directional phosphorylation events associated with the reciprocal regulation of synapses during homeostatic up- and down-scaling. Cell Reports, 36(8):. doi:10.1016/j.celrep.2021.109583.

引用: https://hdl.handle.net/21.11116/0000-0009-4946-7

要旨

Homeostatic synaptic scaling allows for bi-directional adjustment of the strength of synaptic connections in response to changes in their input. Protein phosphorylation modulates many neuronal processes, but it has not been studied on a global scale during synaptic scaling. Here, we use liquid chromatography-tandem mass spectrometry (LC-MS/MS) analyses to measure changes in the phosphoproteome in response to up- or down-scaling in cultured cortical neurons over minutes to 24 h. Of ~45,000 phosphorylation events, ~3,300 (associated with 1,285 phosphoproteins) are regulated by homeostatic scaling. Activity-sensitive phosphoproteins are predominantly located at synapses and involved in cytoskeletal reorganization. We identify many early phosphorylation events that could serve as sensors for the activity offset as well as late and/or persistent phosphoregulation that could represent effector mechanisms driving the homeostatic response. Much of the persistent phosphorylation is reciprocally regulated by up- or down-scaling, suggesting that mechanisms underlying these two poles of synaptic regulation make use of a common signaling axis.