A Review of Mechanics-Based Mesoscopic Membrane Remodeling Methods: Capturing Both the Physics and the Chemical Diversity

Kumar, Gaurav; Duggisetty, Satya Chaithanya; Srivastava, Anand

doi:10.1007/s00232-022-00268-4

Cited by 14 publications

(11 citation statements)

References 167 publications

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“… Kumar et al (2019 , 2022 ) have pointed out from their Monte Carlo simulations that the intrinsic curvatures of filaments imposing anisotropic membrane curvatures (both longitudinal and orthogonal to the direction of the filaments) can drive either concave or convex deformations of liposomes, with the filaments ordered in a nematic fashion. We imposed negative intrinsic curvature for human septin filaments along their length because in yeast, septin filaments were also found to have negative intrinsic curvature of similar magnitude.…”

Section: Discussionmentioning

confidence: 99%

A human septin octamer complex sensitive to membrane curvature drives membrane deformation with a specific mesh-like organization

Nakazawa

Kumar

Chauvin

et al. 2023

Journal of Cell Science

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Septins are cytoskeletal proteins interacting with the inner plasma membrane and other cytoskeletal partners. Being key in membrane remodeling processes, they often localize at specific micrometric curvatures. To analyze the behavior of human septins at the membrane and decouple their role from other partners, we used a combination of bottom-up in vitro methods. We assayed their ultrastructural organization, their curvature sensitivity, as well as their role in membrane reshaping. On membranes, human septins organize into a two-layered mesh of orthogonal filaments, instead of generating parallel sheets of filaments observed for budding yeast septins. This peculiar mesh organization is sensitive to micrometric curvature and drives membrane reshaping as well. The observed membrane deformations together with the filamentous organization are recapitulated in a coarse-grained computed simulation to understand their mechanisms. Our results highlight the specific organization and behavior of animal septins at the membrane as opposed to those of fungal proteins.

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Section: Discussionmentioning

confidence: 99%

A human septin octamer complex sensitive to membrane curvature drives membrane deformation with a specific mesh-like organization

Nakazawa

Kumar

Chauvin

et al. 2023

Journal of Cell Science

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“…Kumar et al 31,44 have pointed out from their Monte Carlo simulations that the intrinsic curvatures of filaments imposing anisotropic membrane curvatures (both longitudinal and orthogonal to the direction of the filaments) can drive either concave or convex deformations of liposomes, with the filaments ordered in a nematic fashion. We have specifically chosen negative intrinsic curvature for human septin filaments along their length because in Yeast, also, they were found to have negative intrinsic curvature of similar magnitude.…”

Section: Discussionmentioning

confidence: 99%

A specific mesh-like organization of human septin octameric complex drives membrane reshaping and curvature sensitivity

Nakazawa

Kumar

Chauvin

et al. 2022

Preprint

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Septins are cytoskeletal proteins interacting with the inner plasma membrane and other cytoskeletal partners. Being key in membrane remodeling processes, they often localize at specific micrometric curvatures. To analyze the behavior of human septins at the membrane, we have used a combination of methods to assay their ultrastructural organization, their curvature sensitivity as well as their role in membrane reshaping. In contrast to budding yeast septins, on membranes, human septins systematically organize into a two-layered mesh of orthogonal filaments instead of generating parallel sheets of filaments observed for budding yeast septins. This peculiar mesh organization is curvature sensitive and drives membrane reshaping as well. The observed membrane deformations together with the filamentous organization are recapitulated in a coarse-grained computed simulation to understand their mechanisms. Our results highlight the specificity of animal septins as opposed to fungal proteins.

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“…In this paper, we systematically investigate the threshold coverages for membrane tubulation by arc-shaped particles via coarse-grained modeling and simulations. Membrane-shaping by arc-shaped proteins or particles has been previously modeled in a variety of ways ,,− (for recent reviews, see refs and ). In our coarse-grained model of membrane shaping, the membrane is described as a triangulated elastic surface, and the particles, as segmented arcs that induce membrane curvature by binding to the membrane.…”

Section: Introductionmentioning

confidence: 99%

Which Coverages of Arc-Shaped Proteins Are Required for Membrane Tubulation?

Gao,

Hou,

et al. 2024

J. Phys. Chem. B

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Arc-shaped BIN/Amphiphysin/Rvs (BAR) domain proteins generate curvature by binding to membranes and induce membrane tubulation at sufficiently large protein coverages. For the amphiphysin N-BAR domain, Le Roux et al., Nat. Commun. 2021, 12, 6550, measured a threshold coverage of 0.44 ± 0.097 for nanotubules emerging from the supported lipid bilayer. In this article, we systematically investigate membrane tubulation induced by arc-shaped protein-like particles with coarse-grained modeling and simulations and determine the threshold coverages at different particle−particle interaction strengths and membrane spontaneous curvatures. In our simulations, the binding of arc-shaped particles induces a membrane shape transition from spherical vesicles to tubules at a particle threshold coverage of about 0.5, which is rather robust to variations of the direct attractive particle interactions or spontaneous membrane curvature in the coarse-grained model. Our study suggests that threshold coverages of around or slightly below 0.5 are a general requirement for membrane tubulation by arc-shaped BAR domain proteins.

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A Review of Mechanics-Based Mesoscopic Membrane Remodeling Methods: Capturing Both the Physics and the Chemical Diversity

Cited by 14 publications

References 167 publications

A human septin octamer complex sensitive to membrane curvature drives membrane deformation with a specific mesh-like organization

A human septin octamer complex sensitive to membrane curvature drives membrane deformation with a specific mesh-like organization

A specific mesh-like organization of human septin octameric complex drives membrane reshaping and curvature sensitivity

Which Coverages of Arc-Shaped Proteins Are Required for Membrane Tubulation?

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