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- W4225539576 endingPage "110168" @default.
- W4225539576 startingPage "110168" @default.
- W4225539576 abstract "Neuronal CaMKII holoenzymes (α and β isoforms) enable molecular signal computation underlying learning and memory but also mediate excitotoxic neuronal death. Here, we provide a comparative analysis of these signaling devices, using single-particle electron microscopy (EM) in combination with biochemical and live-cell imaging studies. In the basal state, both isoforms assemble mainly as 12-mers (but also 14-mers and even 16-mers for the β isoform). CaMKIIα and β isoforms adopt an ensemble of extended activatable states (with average radius of 12.6 versus 16.8 nm, respectively), characterized by multiple transient intra- and inter-holoenzyme interactions associated with distinct functional properties. The extended state of CaMKIIβ allows direct resolution of intra-holoenzyme kinase domain dimers. These dimers could enable cooperative activation by calmodulin, which is observed for both isoforms. High-order CaMKII clustering mediated by inter-holoenzyme kinase domain dimerization is reduced for the β isoform for both basal and excitotoxicity-induced clusters, both in vitro and in neurons." @default.
- W4225539576 created "2022-05-05" @default.
- W4225539576 creator A5010162864 @default.
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- W4225539576 creator A5075109560 @default.
- W4225539576 creator A5086445291 @default.
- W4225539576 date "2021-12-01" @default.
- W4225539576 modified "2023-10-16" @default.
- W4225539576 title "Conserved and divergent features of neuronal CaMKII holoenzyme structure, function, and high-order assembly" @default.
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- W4225539576 doi "https://doi.org/10.1016/j.celrep.2021.110168" @default.
- W4225539576 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34965414" @default.
- W4225539576 hasPublicationYear "2021" @default.
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