Display options
Cite
Tsai FC, Simunovic M, Sorre B, et al. Comparing physical mechanisms for membrane curvature-driven sorting of BAR-domain proteins. Soft Matter. 2021;17(16):4254-4265doi: 10.1039/d0sm01573c.
Tsai, F. C., Simunovic, M., Sorre, B., Bertin, A., Manzi, J., Callan-Jones, A., & Bassereau, P. (2021). Comparing physical mechanisms for membrane curvature-driven sorting of BAR-domain proteins. Soft matter, 17(16), 4254-4265. https://doi.org/10.1039/d0sm01573c
Tsai, Feng-Ching, et al. "Comparing physical mechanisms for membrane curvature-driven sorting of BAR-domain proteins." Soft matter vol. 17,16 (2021): 4254-4265. doi: https://doi.org/10.1039/d0sm01573c
Tsai FC, Simunovic M, Sorre B, Bertin A, Manzi J, Callan-Jones A, Bassereau P. Comparing physical mechanisms for membrane curvature-driven sorting of BAR-domain proteins. Soft Matter. 2021 Apr 28;17(16):4254-4265. doi: 10.1039/d0sm01573c. PMID: 33870384.
Copy Download .nbib Format: NLM
Share it on

Soft Matter. 2021 Apr 28;17(16):4254-4265. doi: 10.1039/d0sm01573c.

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

Soft matter

Feng-Ching Tsai, Mijo Simunovic, Benoit Sorre, Aurélie Bertin, John Manzi, Andrew Callan-Jones, Patricia Bassereau

Affiliations

  1. Institut Curie, Université PSL, CNRS UMR168, Sorbonne Université, Laboratoire Physico Chimie Curie, 75005 Paris, France. [email protected] [email protected].
  2. Department of Chemical Engineering, Columbia University, New York, NY 10027, USA and Department of Genetics and Development, Columbia Stem Cell Initiative, Columbia University Irving Medical Center, NY 10032, USA.
  3. Institut Curie, Université PSL, CNRS UMR168, Sorbonne Université, Laboratoire Physico Chimie Curie, 75005 Paris, France. [email protected] [email protected] and Laboratoire Matière et Systèmes Complexes, UMR 7057 CNRS, Université de Paris, Paris, France. [email protected].
  4. Laboratoire Matière et Systèmes Complexes, UMR 7057 CNRS, Université de Paris, Paris, France. [email protected].

PMID: 33870384 DOI: 10.1039/d0sm01573c

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.

MeSH terms

Publication Types