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• W4210366040 startingPage "49" @default.
• W4210366040 abstract "Lamins are the major constituent of the nuclear lamina, a protein meshwork underlying the inner nuclear membrane. Nuclear lamins are type V intermediate filaments that assemble into ~3.5 nm thick filaments. To date, only the conditions for the in vitro assembly of Caenorhabditis elegans lamin (Ce-lamin) are known. Here, we investigated the assembly of Ce-lamin filaments by cryo-electron microscopy and tomography. We show that Ce-lamin is composed of ~3.5 nm protofilaments that further interact in vitro and are often seen as 6-8 nm thick filaments. We show that the assembly of lamin filaments is undisturbed by the removal of flexible domains, that is, the intrinsically unstructured head and tail domains. In contrast, much of the coiled-coil domains are scaffold elements that are essential for filament assembly. Moreover, our results suggest that Ce-lamin helix 1A has a minor scaffolding role but is important to the lateral assembly regulation of lamin protofilaments." @default.
• W4210366040 created "2022-02-08" @default.
• W4210366040 creator A5011519979 @default.
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• W4210366040 date "2022-02-07" @default.
• W4210366040 modified "2023-10-11" @default.
• W4210366040 title "Filament assembly of the <i>C. elegans</i> lamin in the absence of helix 1A" @default.
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• W4210366040 doi "https://doi.org/10.1080/19491034.2022.2032917" @default.
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