Curvature-sensing and generation by membrane proteins: a review

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Auteur principal: Noguchi, Hiroshi
Format: Preprint
Publié: 2025
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author Noguchi, Hiroshi
author_facet Noguchi, Hiroshi
contents Membrane proteins are crucial in regulating biomembrane shapes and controlling the dynamic changes in membrane morphology during essential cellular processes. These proteins can localize to regions with their preferred curvatures (curvature sensing) and induce localized membrane curvature. Thus, this review describes the recent theoretical development in membrane remodeling performed by membrane proteins. The mean-field theories of protein binding and the resulting membrane deformations are reviewed. The effects of hydrophobic insertions on the area-difference elasticity energy and that of intrinsically disordered protein domains on the membrane bending energy are discussed. For the crescent-shaped proteins, such as Bin/Amphiphysin/Rvs superfamily proteins, anisotropic protein bending energy and orientation-dependent excluded volume significantly contribute to curvature sensing and generation. Moreover, simulation studies of membrane deformations caused by protein binding are reviewed, including domain formation, budding, and tubulation.
format Preprint
id arxiv_https___arxiv_org_abs_2501_18311
institution arXiv
publishDate 2025
record_format arxiv
spellingShingle Curvature-sensing and generation by membrane proteins: a review
Noguchi, Hiroshi
Soft Condensed Matter
Biological Physics
Membrane proteins are crucial in regulating biomembrane shapes and controlling the dynamic changes in membrane morphology during essential cellular processes. These proteins can localize to regions with their preferred curvatures (curvature sensing) and induce localized membrane curvature. Thus, this review describes the recent theoretical development in membrane remodeling performed by membrane proteins. The mean-field theories of protein binding and the resulting membrane deformations are reviewed. The effects of hydrophobic insertions on the area-difference elasticity energy and that of intrinsically disordered protein domains on the membrane bending energy are discussed. For the crescent-shaped proteins, such as Bin/Amphiphysin/Rvs superfamily proteins, anisotropic protein bending energy and orientation-dependent excluded volume significantly contribute to curvature sensing and generation. Moreover, simulation studies of membrane deformations caused by protein binding are reviewed, including domain formation, budding, and tubulation.
title Curvature-sensing and generation by membrane proteins: a review
topic Soft Condensed Matter
Biological Physics
url https://arxiv.org/abs/2501.18311