When Physics Takes Over: BAR Proteins and Membrane Curvature

被引:217
作者
Simunovic, Mijo [1 ,2 ,3 ]
Voth, Gregory A. [1 ,2 ]
Callan-Jones, Andrew [4 ,5 ]
Bassereau, Patricia [3 ,6 ,7 ]
机构
[1] Univ Chicago, James Franck Inst, Inst Biophys Dynam, Dept Chem, Chicago, IL 60637 USA
[2] Univ Chicago, Computat Inst, Chicago, IL 60637 USA
[3] Inst Curie, Ctr Rech, F-75248 Paris, France
[4] Univ Paris Diderot, F-75205 Paris, France
[5] CNRS, UMR 7057, Matiere & Syst Complexes, F-75205 Paris, France
[6] CNRS, PhysicoChim Curie, UMR 168, F-75248 Paris, France
[7] Univ Paris 06, F-75252 Paris, France
基金
美国国家卫生研究院;
关键词
CLATHRIN-INDEPENDENT ENDOCYTOSIS; MEDIATED INTERACTIONS; AMPHIPATHIC HELICES; TUBULAR MEMBRANES; STRUCTURAL BASIS; LIPID-MEMBRANES; N-BAR; ENDOPHILIN; DOMAINS; AGGREGATION;
D O I
10.1016/j.tcb.2015.09.005
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Cell membranes become highly curved during membrane trafficking, cytokinesis, infection, immune response, or cell motion. Bin/amphiphysin/Rvs (BAR) domain proteins with their intrinsically curved and anisotropic shape are involved in many of these processes, but with a large spectrum of modes of action. In vitro experiments and multiscale computer simulations have contributed in identifying a minimal set of physical parameters, namely protein density on the membrane, membrane tension, and membrane shape, that control how bound BAR domain proteins behave on the membrane. In this review, we summarize the multifaceted coupling of BAR proteins to membrane mechanics and propose a simple phase diagram that recapitulates the effects of these parameters.
引用
收藏
页码:780 / 792
页数:13
相关论文
共 63 条
[1]   Endophilin A1 induces different membrane shapes using a conformational switch that is regulated by phosphorylation [J].
Ambroso, Mark R. ;
Hegde, Balachandra G. ;
Langen, Ralf .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2014, 111 (19) :6982-6987
[2]  
Atkins P.W., 2014, PHYS CHEM THERMODYNA
[3]   New Insights into BAR Domain-Induced Membrane Remodeling [J].
Ayton, Gary S. ;
Lyman, Edward ;
Krishna, Vinod ;
Swenson, Richard D. ;
Mim, Carsten ;
Unger, Vinzenz M. ;
Voth, Gregory A. .
BIOPHYSICAL JOURNAL, 2009, 97 (06) :1616-1625
[4]   Endophilin Functions as a Membrane-Bending Molecule and Is Delivered to Endocytic Zones by Exocytosis [J].
Bai, Jihong ;
Hu, Zhitao ;
Dittman, Jeremy S. ;
Pym, Edward C. G. ;
Kaplan, Joshua M. .
CELL, 2010, 143 (03) :430-441
[5]   Thermodynamics and Mechanics of Membrane Curvature Generation and Sensing by Proteins and Lipids [J].
Baumgart, Tobias ;
Capraro, Benjamin R. ;
Zhu, Chen ;
Das, Sovan L. .
ANNUAL REVIEW OF PHYSICAL CHEMISTRY, VOL 62, 2011, 62 :483-506
[6]   A unifying mechanism accounts for sensing of membrane curvature by BAR domains, amphipathic helices and membrane-anchored proteins [J].
Bhatia, Vikram Kjoller ;
Hatzakis, Nikos S. ;
Stamou, Dimitrios .
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY, 2010, 21 (04) :381-390
[7]   Direct observation of Bin/amphiphysin/Rvs (BAR) domain-induced membrane curvature by means of molecular dynamics simulations [J].
Blood, Philip D. ;
Voth, Gregory A. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (41) :15068-15072
[8]   Endophilin marks and controls a clathrin-independent endocytic pathway [J].
Boucrot, Emmanuel ;
Ferreira, Antonio P. A. ;
Almeida-Souza, Leonardo ;
Debard, Sylvain ;
Vallis, Yvonne ;
Howard, Gillian ;
Bertot, Laetitia ;
Sauvonnet, Nathalie ;
McMahon, Harvey T. .
NATURE, 2015, 517 (7535) :460-+
[9]   Membrane Fission Is Promoted by Insertion of Amphipathic Helices and Is Restricted by Crescent BAR Domains [J].
Boucrot, Emmanuel ;
Pick, Adi ;
Camdere, Gamze ;
Liska, Nicole ;
Evergren, Emma ;
McMahon, Harvey T. ;
Kozlov, Michael M. .
CELL, 2012, 149 (01) :124-136
[10]   Curvature-driven membrane lipid and protein distribution [J].
Callan-Jones, Andrew ;
Bassereau, Patricia .
CURRENT OPINION IN SOLID STATE & MATERIALS SCIENCE, 2013, 17 (04) :143-150