Recent insight into intermediate filament structure

Eldirany, Sherif A.; Lomakin, Ivan B.; Ho, Minh; Bunick, Christopher G.

doi:10.1016/j.ceb.2020.10.001

Cited by 66 publications

(68 citation statements)

References 75 publications

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“…These stages of stepwise assembly appear analogous to SYCE2-TEX12’s 2:2 building-blocks, 4:4 assembly intermediates and 10-nm fibres. Further, IF proteins consist of coiled-coil cores flanked by assembly motifs 63 , their 10-nm fibres can assemble into meshwork and bundled networks 64,65 , and lamin forms 3.5-nm fibres that are reminiscent of SYCE2-TEX12’s 4-nm fibres 56,66 . Thus, hierarchical assembly of SYCE2-TEX12 bears striking resemblance to IF assembly, suggesting that SYCE2-TEX12 fibres may acquire the longitudinal strength, with flexion and torsional freedom, that is typical of the cytoskeleton by exploiting the same structural principles as molecules such as keratin.…”

Section: Discussionmentioning

confidence: 99%

Structural basis of meiotic chromosome synaptic elongation through hierarchical fibrous assembly of SYCE2-TEX12

Dunce

Salmon

Davies

2020

Preprint

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The supramolecular structure of the synaptonemal complex (SC) mediates homologous chromosome synapsis and facilitates the formation of genetic crossovers during meiosis. The mammalian SC is formed of eight coiled-coil proteins which interact in specific subcomplexes and self-assemble into distinct macromolecular arrays that fulfil specific aspects of the SC’s dynamic functional architecture. Here, we report the structure of SC subcomplex SYCE2-TEX12 and its mechanism of self-assembly into fibres that define the SC’s midline longitudinal structure. X-ray crystal structures, electron microscopy, biophysical and mutational analyses reveal that SYCE2-TEX12 is assembled from 2:2 complexes in which TEX12 chains are positioned at either end of a rod-like SYCE2 dimer. These molecular building-blocks assemble laterally into 4:4 complexes, and longitudinally into fibres of potentially limitless length, which acts as string-like threads that wind around one another in intertwined fibres of up to 40-nm in width and several micrometres in length. This hierarchical assembly mechanism is reminiscent of intermediate filament proteins and results in SYCE2-TEX12 fibres that can span the entire chromosome length, thereby providing the underpinning structural support for SC elongation during meiotic chromosome synapsis.

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Section: Discussionmentioning

confidence: 99%

Structural basis of meiotic chromosome synaptic elongation through hierarchical fibrous assembly of SYCE2-TEX12

Dunce

Salmon

Davies

2020

Preprint

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“…Information collected through these approaches has been integrated with molecular modeling studies providing our current view of vimentin assembly 14, 24 (reviewed in 25 ). Moreover, information from various intermediate filament proteins has contributed to the understanding of filament structure 26, 27 . Most available models of the vimentin tetramer adopt the A11 configuration, in which an anchoring knob–hydrophobic pocket mechanism involving the 1B segment, identified in several intermediate filament proteins including vimentin, provides stability 28 (see 27 for review).…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, information from various intermediate filament proteins has contributed to the understanding of filament structure 26, 27 . Most available models of the vimentin tetramer adopt the A11 configuration, in which an anchoring knob–hydrophobic pocket mechanism involving the 1B segment, identified in several intermediate filament proteins including vimentin, provides stability 28 (see 27 for review). In turn, in ULF or filaments, a parallel stacking of tetramers is proposed, usually represented as a tubular structure 14, 29, 30 (Figure 1B), although their exact disposition and relative positions with respect to the longitudinal axis, are not understood.…”

Section: Introductionmentioning

confidence: 99%

“…). Moreover, information from various intermediate filament proteins has contributed to the understanding of filament structure 26,27 . Most available models of the vimentin tetramer adopt the A11 configuration, in which an anchoring knob-hydrophobic pocket mechanism involving the 1B segment, identified in several intermediate filament proteins…”

Section: Introductionmentioning

confidence: 99%

“…including vimentin, provides stability 28 (see 27 for review). In turn, in ULF or filaments, a parallel stacking of tetramers is proposed, usually represented as a tubular structure 14, 29, 30 (Figure 1B), although their exact disposition and relative positions with respect to the longitudinal axis, are not understood.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Elucidating vimentin interaction with zinc ions and its interplay with oxidative modifications through crosslinking assays and molecular dynamics simulations

Mónico

Guzmán-Caldentey

et al. 2021

Preprint

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The intermediate filament protein vimentin is involved in essential cellular processes, including cell division and stress responses. Vimentin oxidative modifications impact network reorganization and its single cysteine residue, Cys328, acts as a redox sensor. Vimentin binds zinc, which influences its assembly by undefined mechanisms. Here, results from combined biochemical and molecular dynamics studies support that zinc ions interact with Cys328 in its thiolate form, whereas Glu329 and Asp331 stabilize zinc coordination. Vimentin oxidation can induce disulfide crosslinking, implying a close proximity of cysteine residues in certain vimentin associations, validated by our computational models. Notably, micromolar zinc concentrations selectively prevent Cys328 alkylation and crosslinking. These effects are not mimicked by magnesium, consistent with the fewer magnesium ions hosted at the cysteine region. Altogether, our results pinpoint the region surrounding Cys328, highly conserved in type III intermediate filaments, as a hot spot for zinc binding, which modulates Cys328 reactivity and vimentin assembly.

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Genetic Blistering Diseases

McGrath

2024

Rook's Textbook of Dermatology

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The integrity of the skin is maintained by complex networks of structural and non‐structural proteins within the epidermis, epidermal basement membrane zone and upper dermis. Disruption to the function of any one of these integral proteins through inherited gene mutations can make the skin less resilient to trauma and more prone to blister formation. This chapter provides an overview of key proteins involved in skin integrity and outlines the spectrum of blistering diseases linked to abnormalities therein. The text also describes approaches to diagnosis of inherited blistering diseases, as well as innovative therapies which try to reduce blistering and improve skin function.

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Recent insight into intermediate filament structure

Cited by 66 publications

References 75 publications

Structural basis of meiotic chromosome synaptic elongation through hierarchical fibrous assembly of SYCE2-TEX12

Structural basis of meiotic chromosome synaptic elongation through hierarchical fibrous assembly of SYCE2-TEX12

Elucidating vimentin interaction with zinc ions and its interplay with oxidative modifications through crosslinking assays and molecular dynamics simulations

Genetic Blistering Diseases

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