Issue 32, 2013
From the journal:

Soft Matter

The mechanics of membrane proteins is a signature of biological function†

Felix Rico,a   Laura Picas,b   Adai Colom,a   Nikolay Buzhynskyya  and  Simon Scheuring*a  

* Corresponding authors

a U1006 INSERM, Aix-Marseille Université, Parc Scientifique de Luminy, 13009 Marseille, France
E-mail: simon.scheuring@inserm.fr
Fax: +33 (0)4 91 82 87 01
Tel: +33 (0)4 91 82 87 00

b Institut Curie, UMR144 CNRS, 26 rue d'Ulm, 75005 Paris, France

Abstract

Beyond structure, the mechanics of plasma membrane components is of key importance to biological function. Nanoscale mechanics is however poorly described due to the lack of suitable experimental tools. Here, we combined atomic force microscopy and nanomechanical mapping to analyze the structure and mechanical properties of native eye lens cell membranes. Lens membranes mainly comprise two proteins; aquaporin 0 and connexin, forming respectively thin and gap intercellular junctions that sustain mechanical stress during accommodation. Our results reveal the mechanical heterogeneity of the plasma membrane, allowing examination of the mechanical nanoenvironment of individual proteins and the flexibility of supramolecular assemblies. The remarkable rigidity of gap junctions suggests their role as stable intercellular adhesion complexes ensuring maintenance of thin junctions, which form more flexible supramolecular complexes capable of sustaining pressure differences between cells. Our work proposes the mechanical properties of individual proteins and protein domains directly related to biological function as a novel molecular signature.

Graphical abstract: The mechanics of membrane proteins is a signature of biological function

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Article information

DOI
https://doi.org/10.1039/C3SM50967B
Article type
Paper
Submitted
08 Apr 2013
Accepted
24 Jun 2013
First published
25 Jun 2013

Soft Matter, 2013,9, 7866-7873

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The mechanics of membrane proteins is a signature of biological function

F. Rico, L. Picas, A. Colom, N. Buzhynskyy and S. Scheuring, Soft Matter, 2013, 9, 7866 DOI: 10.1039/C3SM50967B

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