Biomimetic nuclear lamin fibers with remarkable toughness and stiffness

Khayat, Maayan; Deri, Shani; Wolf, D.; Trigano, Tom; Medalia, Ohad; Ben‐Harush, Kfir

doi:10.1016/j.ijbiomac.2020.09.113

Cited by 6 publications

(2 citation statements)

References 26 publications

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“…Insight into the assembly and 3D structure of the lamin filaments is therefore of major importance. The Ce -lamin can be expressed in high quantities in bacteria, although it is localized to inclusion bodies [ 37 ]. Following a two-step dialysis, lamins were assembled into filaments.…”

Section: Resultsmentioning

confidence: 99%

Filament assembly of the C. elegans lamin in the absence of helix 1A

Leeuw

Kronenberg-Tenga

Eibauer

et al. 2022

Nucleus

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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.

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Section: Resultsmentioning

confidence: 99%

Filament assembly of the C. elegans lamin in the absence of helix 1A

Leeuw

Kronenberg-Tenga

Eibauer

et al. 2022

Nucleus

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“…The mechanical properties of filaments in paracrystals could be wildly different from those in vivo, where lamin dimers form thin filaments and a mesh-like network [54,129]. Nevertheless, paracrystalline assemblies provide an alternative approach to decipher the biophysical properties of lamins [12,130].…”

Section: Interrogating Single Lamin Filaments In Vitro In Silico and In Situmentioning

confidence: 99%

Bend, Push, Stretch: Remarkable Structure and Mechanics of Single Intermediate Filaments and Meshworks

Sapra

Medalia

2021

Cells

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The cytoskeleton of the eukaryotic cell provides a structural and functional scaffold enabling biochemical and cellular functions. While actin and microtubules form the main framework of the cell, intermediate filament networks provide unique mechanical properties that increase the resilience of both the cytoplasm and the nucleus, thereby maintaining cellular function while under mechanical pressure. Intermediate filaments (IFs) are imperative to a plethora of regulatory and signaling functions in mechanotransduction. Mutations in all types of IF proteins are known to affect the architectural integrity and function of cellular processes, leading to debilitating diseases. The basic building block of all IFs are elongated α-helical coiled-coils that assemble hierarchically into complex meshworks. A remarkable mechanical feature of IFs is the capability of coiled-coils to metamorphize into β-sheets under stress, making them one of the strongest and most resilient mechanical entities in nature. Here, we discuss structural and mechanical aspects of IFs with a focus on nuclear lamins and vimentin.

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From reductionism to synthesis: The case of hagfish slime

Bressman¹,

Fudge²

2021

Comparative Biochemistry and Physiology Part B: Biochemistry an

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Biomimetic nuclear lamin fibers with remarkable toughness and stiffness

Cited by 6 publications

References 26 publications

Filament assembly of the C. elegans lamin in the absence of helix 1A

Filament assembly of the C. elegans lamin in the absence of helix 1A

Bend, Push, Stretch: Remarkable Structure and Mechanics of Single Intermediate Filaments and Meshworks

From reductionism to synthesis: The case of hagfish slime

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