Physical basis of some membrane shaping mechanisms.
In vesicular transport pathways, membrane proteins and lipids are internalized, externalized or transported within cells, not by bulk diffusion of single molecules, but embedded in the membrane of small vesicles or thin tubules. The formation of these 'transport carriers' follows sequential events: membrane bending, fission from the donor compartment, transport and eventually fusion with the acceptor membrane. A similar sequence is involved during the internalization of drug or gene carriers inside cells. These membrane-shaping events are generally mediated by proteins binding to membranes. The mechanisms behind these biological processes are actively studied both in the context of cell biology and biophysics. Bin/amphiphysin/Rvs (BAR) domain proteins are ideally suited for illustrating how simple soft matter principles can account for membrane deformation by proteins. We review here some experimental methods and corresponding theoretical models to measure how these proteins affect the mechanics and the shape of membranes. In more detail, we show how an experimental method employing optical tweezers to pull a tube from a giant vesicle may give important quantitative insights into the mechanism by which proteins sense and generate membrane curvature and the mechanism of membrane scission.This article is part of the themed issue 'Soft interfacial materials: from fundamentals to formulation'.
Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005 Paris, France The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA.
Mijo
http://orcid.org/0000-0001-9394-1552
M
Simunovic
Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005 Paris, France Sorbonne Universités, UPMC Univ Paris 06, 75005 Paris, France.
Coline
http://orcid.org/0000-0002-5632-3250
C
Prévost
Laboratoire Matière et Systèmes Complexes, CNRS, UMR 7057, 75205 Paris Cedex 13, France.
Andrew
http://orcid.org/0000-0001-8769-687X
A
Callan-Jones
Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005 Paris, France Sorbonne Universités, UPMC Univ Paris 06, 75005 Paris, France patricia.bassereau@curie.fr.
Patricia
http://orcid.org/0000-0002-8544-6778
P
Bassereau
D002462:Cell Membrane / Q000737:chemistry / Q000502:physiology; D004705:Endocytosis; D008051:Lipid Bilayers / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology; D043942:Nanotubes; D017434:Protein Structure, Tertiary
D008051:Lipid Bilayers; D008565:Membrane Proteins
Bin/amphiphysin/Rvs-domain proteins; curvature; lipid membranes; membrane nanotube; scaffold; scission