Structural, Mechanical and Functional Properties of Intermediate Filaments from the Atomistic to the Cellular Scales

Qin, Zhao; Chou, Chia; Kreplak, Laurent; Buehler, Markus J.

doi:10.1007/978-3-642-17590-9_4

Cited by 6 publications

(7 citation statements)

References 136 publications

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“…The normal filament elasticity is α = 0.345 × 10 −8 N/µm which corresponds to 22 MPa. This lies in the range of experimentally measured values [31,32,33] and compares well with values used in [34]. In the simulations we use three values for fiber elasticity -less stiff filaments with 0.001α, normal filaments with α, and stiff filaments with 1000α.…”

Section: The Modelsupporting

confidence: 71%

“…Using Hooke's law, F = α∆L, we get a relationship between the spring constant α and the Young's modulus given by α = YA L . The elastic modulus of vimentin has been estimated to be 8-9 MPa [31], 900 MPa by [32], and 6.5 MPa for another keratin-like based filament [33]. For a 10 percent change of length with forces on the order of 0.18 pN a Young's modulus of 22 MPa is needed.…”

Section: Parametersmentioning

confidence: 99%

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Stochastic modeling reveals how motor protein and filament properties affect intermediate filament transport

Dallon

Leduc

Etienne-Manneville

et al. 2019

Journal of Theoretical Biology

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Intermediate filaments are a key component of the cytoskeleton. Their transport along microtubules plays an essential role in the control of the shape and structural organization of cells. To identify the key parameters responsible for the control of intermediate filament transport, we generated a model of elastic filament transport by microtubule-associated dynein and kinesin. The model is also applicable to the transport of any elastically-coupled cargoes. We investigate the effect of filament properties such as number of motor binding sites, length, and elasticity on motion of filaments. Additionally, we consider the effect of motor properties, i.e. off rates, on filament transport. When one motor has a catch bond off rate it dictates the motion, whereas when motors have the same type of off rate filaments can alternate between retrograde and anterograde motions. The elasticity of filaments optimizes the filament transport and the coordination of motors along the length of the filament.

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Section: The Modelsupporting

confidence: 71%

Section: Parametersmentioning

confidence: 99%

Stochastic modeling reveals how motor protein and filament properties affect intermediate filament transport

Dallon

Leduc

Etienne-Manneville

et al. 2019

Journal of Theoretical Biology

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“…Molecular dynamics (MD) simulation offers an approach to model chemical interactions and can potentially yield physically-reasonable full structure predictions of IF proteins. Results of such molecular simulations have been reported previously for both the vimentin homodimer system [ 28 – 32 ], and recently, the trichocyte keratin heterodimer [ 33 , 34 ] (found in hair). These previous studies chiefly focused on the mechanical properties of the IF sub-units, rather than the structural details, and did not report local structural properties of the dimer at the residue level, nor did they provide any specific details on the structure and behavior of the head or tail domains.…”

Section: Introductionsupporting

confidence: 57%

Complete Structure of an Epithelial Keratin Dimer: Implications for Intermediate Filament Assembly

et al. 2015

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Keratins are cytoskeletal proteins that hierarchically arrange into filaments, starting with the dimer sub-unit. They are integral to the structural support of cells, in skin, hair and nails. In skin, keratin is thought to play a critical role in conferring the barrier properties and elasticity of skin. In general, the keratin dimer is broadly described by a tri-domain structure: a head, a central rod and a tail. As yet, no atomistic-scale picture of the entire dimer structure exists; this information is pivotal for establishing molecular-level connections between structure and function in intermediate filament proteins. The roles of the head and tail domains in facilitating keratin filament assembly and function remain as open questions. To address these, we report results of molecular dynamics simulations of the entire epithelial human K1/K10 keratin dimer. Our findings comprise: (1) the first three-dimensional structural models of the complete dimer unit, comprising of the head, rod and tail domains; (2) new insights into the chirality of the rod-domain twist gained from analysis of the full domain structure; (3) evidence for tri-subdomain partitioning in the head and tail domains; and, (4) identification of the residue characteristics that mediate non-covalent contact between the chains in the dimer. Our findings are immediately applicable to other epithelial keratins, such as K8/K18 and K5/K14, and to intermediate filament proteins in general.

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“…To fully capture the hierarchical structure of keratin, computational models have been developed for each length scale. Starting with the fundamental building blocks of amino acids, these models aim to analyze the mechanical properties and arrangement of molecules in IFs at the sub-nanoscale ( Chou and Buehler, 2012 ; Qin et al, 2009 , 2011 ; Qin and Buehler, 2011 ). Chou and Buehler (2012) pioneered this effort by reconstructing heterodimers from an entire amino acid sequence of keratin proteins using molecular dynamics simulations.…”

Section: Introductionmentioning

confidence: 99%

Engineering with keratin: A functional material and a source of bioinspiration

et al. 2021

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Summary Keratin is a highly multifunctional biopolymer serving various roles in nature due to its diverse material properties, wide spectrum of structural designs, and impressive performance. Keratin-based materials are mechanically robust, thermally insulating, lightweight, capable of undergoing reversible adhesion through van der Waals forces, and exhibit structural coloration and hydrophobic surfaces. Thus, they have become templates for bioinspired designs and have even been applied as a functional material for biomedical applications and environmentally sustainable fiber-reinforced composites. This review aims to highlight keratin's remarkable capabilities as a biological component, a source of design inspiration, and an engineering material. We conclude with future directions for the exploration of keratinous materials.

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Structural, Mechanical and Functional Properties of Intermediate Filaments from the Atomistic to the Cellular Scales

Cited by 6 publications

References 136 publications

Stochastic modeling reveals how motor protein and filament properties affect intermediate filament transport

Stochastic modeling reveals how motor protein and filament properties affect intermediate filament transport

Complete Structure of an Epithelial Keratin Dimer: Implications for Intermediate Filament Assembly

Engineering with keratin: A functional material and a source of bioinspiration

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