CaMKII activation persistently segregates postsynaptic proteins via liquid phase separation

Autor:	Tomohisa, Hosokawa, Pin-Wu, Liu, Qixu, Cai, Joana S, Ferreira, Florian, Levet, Corey, Butler, Jean-Baptiste, Sibarita, Daniel, Choquet, Laurent, Groc, Eric, Hosy, Mingjie, Zhang, Yasunori, Hayashi
Rok vydání:	2020
Předmět:	Enzyme Activation Male Rats Sprague-Dawley Mice Liquid-Liquid Extraction Animals Membrane Proteins Female Amino Acid Sequence Receptors AMPA Calcium-Calmodulin-Dependent Protein Kinase Type 2 Receptors N-Methyl-D-Aspartate Rats
Zdroj:	Nature neuroscience. 24(6)
ISSN:	1546-1726
Popis:	Transient information input to the brain leads to persistent changes in synaptic circuits, contributing to the formation of memory engrams. Pre- and postsynaptic structures undergo coordinated functional and structural changes during this process, but how such changes are achieved by their component molecules remains largely unknown. We found that activated CaMKII, a central player of synaptic plasticity, undergoes liquid-liquid phase separation with the NMDA-type glutamate receptor subunit GluN2B. Due to CaMKII autophosphorylation, the condensate stably persists even after Ca
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::62bddfbf8c5c8da8f44085b5b8371e69 https://pubmed.ncbi.nlm.nih.gov/34075223 Zobrazit plný text záznamu Full text from SpringerLink