Skip to Main content Skip to Navigation
Journal articles

Comparing physical mechanisms for membrane curvature-driven sorting of BAR-domain proteins

Abstract : Protein enrichment at specific membrane locations in cells is crucial for many cellular functions. It is well-recognized that the ability of some proteins to sense membrane curvature contributes partly to their enrichment in highly curved cellular membranes. In the past, different theoretical models have been developed to reveal the physical mechanisms underlying curvature-driven protein sorting. This review aims to provide a detailed discussion of the two continuous models that are based on the Helfrich elasticity energy, (1) the spontaneous curvature model and (2) the curvature mismatch model. These two models are commonly applied to describe experimental observations of protein sorting. We discuss how they can be used to explain the curvature-induced sorting data of two BAR proteins, amphiphysin and centaurin. We further discuss how membrane rigidity, and consequently the membrane curvature generated by BAR proteins, could influence protein organization on the curved membranes. Finally, we address future directions in extending these models to describe some cellular phenomena involving protein sorting.
Complete list of metadata

https://hal.archives-ouvertes.fr/hal-03281035
Contributor : Aurélie Bertin <>
Submitted on : Wednesday, July 7, 2021 - 7:00:35 PM
Last modification on : Wednesday, July 14, 2021 - 3:39:48 AM

File

soft_matter_version_author.pdf
Files produced by the author(s)

Identifiers

Citation

Feng-Ching Tsai, Mijo Simunovic, Benoit Sorre, Aurélie Bertin, John Manzi, et al.. Comparing physical mechanisms for membrane curvature-driven sorting of BAR-domain proteins. Soft Matter, Royal Society of Chemistry, 2021, 17 (16), pp.4254-4265. ⟨10.1039/d0sm01573c⟩. ⟨hal-03281035⟩

Share

Metrics

Record views

12

Files downloads

25