Biological Membrane Organization and Cellular Signaling

被引:134
作者
Cheng, Xiaolin [1 ]
Smith, Jeremy C. [2 ,3 ]
机构
[1] Ohio State Univ, Div Med Chem & Pharmacognosy, Biophys Grad Program, Translat Data Analyt Inst, Columbus, OH 43210 USA
[2] Oak Ridge Natl Lab, Biosci Div, UT ORNL Ctr Mol Biophys, Oak Ridge, TN 37831 USA
[3] Univ Tennessee, Dept Biochem & Cellular & Mol Biol, Knoxville, TN 37996 USA
关键词
GPI-ANCHORED PROTEINS; NICOTINIC ACETYLCHOLINE-RECEPTOR; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE BINDING; 2-PHOTON FLUORESCENCE MICROSCOPY; DETERGENT-RESISTANT MEMBRANES; NUCLEAR-MAGNETIC-RESONANCE; LATERAL PHASE-SEPARATION; LIQUID-ORDERED PHASE; ALPHA-HELIX DIPOLE; ZETA PKC-ZETA;
D O I
10.1021/acs.chemrev.8b00439
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
To execute their many vital functions, cell membranes are highly organized. Here, we review how membrane structure shapes signal transduction across membranes. Recent experimental and computational advances have shed significant light on mechanisms linking the function of membrane signaling proteins to the composition and physical properties of the membrane lateral structures in which they are embedded. We provide an overview of the structural characteristics of membranes containing heterogeneous mixtures of lipids and other molecules and summarize work on "raft" domains in model and cell membranes, as determined by microscopy, spectroscopy, neutron scattering, and computer simulations. We discuss the principles of partitioning of proteins into membranes and how the structure, dynamics, and function of membrane-embedded and peripheral proteins can be modulated by specific membrane components and physical properties of membranes and raft domains. Finally, we discuss challenges and future directions toward a molecular-level understanding of how membrane organization gives rise to various context-dependent cellular signaling.
引用
收藏
页码:5849 / 5880
页数:32
相关论文
共 336 条
[81]   Electron spin resonance characterization of liquid ordered phase of detergent-resistant membranes from RBL-2H3 cells [J].
Ge, MT ;
Field, KA ;
Aneja, R ;
Holowka, D ;
Baird, B ;
Freed, JH .
BIOPHYSICAL JOURNAL, 1999, 77 (02) :925-933
[82]   Interaction of G protein coupled receptors and cholesterol [J].
Gimpl, Gerald .
CHEMISTRY AND PHYSICS OF LIPIDS, 2016, 199 :61-73
[83]   Characterizing the interactions between GPI-anchored alkaline phosphatases and membrane domains by AFM [J].
Giocondi, Marie-Cecile ;
Seantier, Bastien ;
Dosset, Patrice ;
Milhiet, Pierre-Emmanuel ;
Le Grimellec, Christian .
PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY, 2008, 456 (01) :179-188
[84]   On bimolecular layers of lipoids on the chromocytes of the blood. [J].
Gorter, E ;
Grendel, F .
JOURNAL OF EXPERIMENTAL MEDICINE, 1925, 41 (04) :439-443
[85]   A study of the membrane-water interface region of membrane proteins [J].
Granseth, E ;
von Heijne, G ;
Elofsson, A .
JOURNAL OF MOLECULAR BIOLOGY, 2005, 346 (01) :377-385
[86]   Ceramide-rich membrane rafts mediate CD40 clustering [J].
Grassmé, H ;
Jendrossek, V ;
Bock, J ;
Riehle, A ;
Gulbins, E .
JOURNAL OF IMMUNOLOGY, 2002, 168 (01) :298-307
[87]   CD95 signaling via ceramide-rich membrane rafts [J].
Grassmé, H ;
Jekle, A ;
Riehle, A ;
Schwarz, H ;
Berger, J ;
Sandhoff, K ;
Kolesnick, R ;
Gulbins, E .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (23) :20589-20596
[88]   The influence of cholesterol on membrane protein structure, function, and dynamics studied by molecular dynamics simulations [J].
Grouleff, Julie ;
Irudayam, Sheeba Jem ;
Skeby, Katrine K. ;
Schiott, Birgit .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2015, 1848 (09) :1783-1795
[89]   Do sterols reduce proton and sodium leaks through lipid bilayers? [J].
Haines, TH .
PROGRESS IN LIPID RESEARCH, 2001, 40 (04) :299-324
[90]   Accelerated molecular dynamics: A promising and efficient simulation method for biomolecules [J].
Hamelberg, D ;
Mongan, J ;
McCammon, JA .
JOURNAL OF CHEMICAL PHYSICS, 2004, 120 (24) :11919-11929