Protein modulation of lipids, and vice-versa, in membranes

Biochimica et Biophysica Acta - Biomembranes

Volumn 1778, Issue 7-8, 2008, Pages 1545-1575

  Marsh, Derek ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

Annular lipid; Boundary lipid; Elastic bending fluctuations; Hydrophobic matching; Intrinsic curvature; Non lamellar lipid

Indexed keywords

ALAMETHICIN; LIPID; MEMBRANE PROTEIN; OLIGOMER; PROTEIN;

CONFORMATION; CRYSTAL STRUCTURE; ELASTICITY; ENERGY TRANSFER; GENETIC POLYMORPHISM; HYDROPHOBICITY; MELTING POINT; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN LIPID INTERACTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; REVIEW; STOICHIOMETRY;

ANIMALS; BIOPHYSICS; ELASTICITY; ELECTRON SPIN RESONANCE SPECTROSCOPY; HYDROPHOBICITY; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE LIPIDS; MEMBRANE MICRODOMAINS; MEMBRANE PROTEINS; MODELS, MOLECULAR; THERMODYNAMICS;

EID: 45449105164     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.01.015     Document Type: Review

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112. Watts A., Marsh D., and Knowles P.F. Lipid-substituted cytochrome oxidase: no absolute requirement of cardiolipin for activity. Biochem. Biophys. Res. Commun. 81 (1978) 397-402
113. Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H., Shinzawa-Itoh K., Nakashima R., Yaono R., and Yoshikawa S. The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272 (1996) 1136-1144
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116. Powl A.M., East J.M., and Lee A.G. Heterogeneity in the binding of lipid molecules to the surface of a membrane protein: hot spots for anionic lipids on the mechanosensitive channel of large conductance MscL and effects on conformation. Biochemistry 44 (2005) 5873-5883
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118. Tanford C. The Hydrophobic Effect (1980), Wiley, New York
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120. +-ATPase membranes from Squalus acanthias. Biochemistry 24 (1985) 3572-3578
121. Miyazaki J., Hideg K., and Marsh D. Interfacial ionization and partitioning of membrane-bound local anaesthetics. Biochim. Biophys. Acta 1103 (1992) 62-68
122. Horváth L.I., Arias H.R., Hankovszky H.O., Hideg K., Barrantes F.J., and Marsh D. Association of spin-labeled local anaesthetics at the hydrophobic surface of acetylcholine receptor in native membranes from Torpedo marmorata. Biochemistry 29 (1990) 8707-8713
123. +-ATPase enzymes. Org. Biomol. Chem. 1 (2003) 4361-4363
124. Dixon N., Páli T., Kee T.P., and Marsh D. Spin-labelled vacuolar-ATPase inhibitors in lipid membranes. Biochim. Biophys. Acta 1665 (2004) 177-183
125. 0-sector. Biophys. J. 94 (2008) 506-514
126. Ryba N.J.P., and Marsh D. Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation transfer electron spin resonance. Biochemistry 31 (1992) 7511-7518
127. Ryba N.J.P., Marsh D., and Uhl R. The kinetics and thermodynamics of bleaching of rhodopsin in dimyristoylphosphatidylcholine. Identification of meta-I, meta-II, and meta-III intermediates. Biophys. J. 64 (1993) 1801-1812
128. Caffrey M., and Feigenson G.W. Fluorescence quenching in model membranes. 3. Relationship between calcium adenosinetriphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics. Biochemistry 20 (1981) 1949-1961
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132. Marsh D. Lateral pressure profile, spontaneous curvature frustration, and the incorporation and conformation of proteins in membranes. Biophys. J. 93 (2007) 3884-3899
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138. Marsh D., Kurad D., and Livshits V.A. High-field electron spin resonance of spin labels in membranes. Chem. Phys. Lipids 116 (2002) 93-114
139. Sachse J.-H., King M.D., and Marsh D. ESR determination of lipid diffusion coefficients at low spin-label concentrations in biological membranes, using exchange broadening, exchange narrowing, and dipole-dipole interactions. J. Magn. Reson. 71 (1987) 385-404
140. King M.D., Sachse J.-H., and Marsh D. Unconstrained optimization method for interpreting the concentration and temperature dependence of the linewidths of interacting nitroxide spin labels. Application to the measurement of translational diffusion coefficients of spin-labeled phospholipids in membranes. J. Magn. Reson. 72 (1987) 257-267
141. Horváth L.I., Brophy P.J., and Marsh D. Exchange rates at the lipid-protein interface of myelin proteolipid protein studied by spin-label electron spin resonance. Biochemistry 27 (1988) 46-52
142. East J.M., Melville D., and Lee A.G. Exchange rates and numbers of annular lipids for the calcium and magnesium ion dependent adenosinetriphosphatase. Biochemistry 24 (1985) 2615-2623
143. Páli T., Finbow M.E., and Marsh D. Membrane assembly of the 16-kDa proteolipid channel from Nephrops norvegicus studied by relaxation enhancements in spin-label ESR. Biochemistry 38 (1999) 14311-14319
144. Páli T., Kleinschmidt J.H., Powell G.L., and Marsh D. Nonlinear electron paramagnetic rsonance studies of the interaction of cytochrome c oxidase with spin-labeled lipids in gel-phase membranes. Biochemistry 39 (2000) 2355-2361
145. Arora A., and Marsh D. Protein-induced vertical lipid dislocation in a model membrane system: spin-label relaxation studies on avidin-biotinylphosphatidylethanolamine interactions. Biophys. J. 75 (1998) 2915-2922
146. Arora A., Esmann M., and Marsh D. Microsecond motions of the lipids associated with trypsinized Na,K-ATPase membranes. Progressive saturation spin-label electron spin resonance studies. Biochemistry 38 (1999) 10084-10091
147. Horváth L.I., Brophy P.J., and Marsh D. Exchange rates at the lipid-protein interface of the myelin proteolipid protein determined by saturation transfer electron spin resonance and continuous wave saturation studies. Biophys. J. 64 (1993) 622-631
148. Horváth L.I., Brophy P.J., and Marsh D. Spin label saturation transfer EPR determinations of the stoichiometry and selectivity of lipid-protein interactions in the gel phase. Biochim. Biophys. Acta 1147 (1993) 277-280
149. Meier P., Sachse J.-H., Brophy P.J., Marsh D., and Kothe G. Integral membrane proteins significantly decrease the molecular motion in lipid bilayers: a deuteron NMR relaxation study of membranes containing myelin proteolipid apoprotein. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 3704-3708
150. 31P NMR spectroscopy. Biochemistry 32 (1993) 9709-9713
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156. Marsh D., Watts A., and Smith I.C.P. Dynamic structure and phase behaviour of dimyristoylphosphatidylethanolamine bilayers studied by deuterium nuclear magnetic resonance. Biochemistry 22 (1983) 3023-3026
157. 2H-NMR studies. Biophys. J. 71 (1996) 3320-3329
158. Pates R.D., and Marsh D. Lipid mobility and order in bovine rod outer segment disk membranes. A spin-label study of lipid-protein interactions. Biochemistry 26 (1987) 29-39
159. Marsh D., and Páli T. Lipid conformation in crystalline bilayers and in crystals of transmembrane proteins. Chem. Phys. Lipids 141 (2006) 48-65
160. Marsh D. Lipid-binding proteins: structure of the phospholipid ligands. Protein Sci. 12 (2003) 2109-2117
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179. Cevc G., and Marsh D. Phospholipid Bilayers. Physical Principles and Models (1987), Wiley-Interscience, New York
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182. Pocanschi C.L., Apell H.J., Puntervoll P., Hogh B., Jensen H.B., Welte W., and Kleinschmidt J.H. The major outer membrane protein of Fusobacterium nucleatum (FomA) folds and inserts into lipid bilayers via parallel folding pathways. J. Mol. Biol. 355 (2006) 548-561
183. Ramakrishnan M., Qu J., Pocanschi C.L., Kleinschmidt J.H., and Marsh D. Orientation of β-barrel proteins OmpA and FhuA in lipid membranes. Chainlength dependence from infrared dichroism. Biochemistry 44 (2005) 3515-3523
184. 2H NMR. Biophys. J. 83 (2002) 1479-1488
185. 2H NMR study. Biochemistry 44 (2005) 1004-1012
186. Marsh D., Jost M., Peggion C., and Toniolo C. Lipid chainlength dependence for incorporation of alamethicin in membranes: EPR studies on TOAC-spin labelled analogues. Biophys. J. 92 (2007) 4002-4011
187. Marsh D., Jost M., Peggion C., and Toniolo C. TOAC spin labels in the backbone of alamethicin: EPR studies in lipid membranes. Biophys. J. 92 (2007) 473-481
188. Marsh D., Shanmugavadivu B., and Kleinschmidt J.H. Membrane elastic fluctuations and the insertion and tilt of β-barrel proteins. Biophys. J. 91 (2006) 227-232
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191. Seddon J.M., Cevc G., Kaye R.D., and Marsh D. X-ray diffraction study of the polymorphism of hydrated diacyl- and dialkylphosphatidylethanolamines. Biochemistry 23 (1984) 2634-2644
192. Cullis P.R., and De Kruijff B. Lipid polymorphism and the functional roles of lipids in biological membranes. Biochim. Biophys. Acta 559 (1979) 399-420
193. Marsh D. General features of phospholipid phase transitions. Chem. Phys. Lipids 57 (1991) 109-120
194. Marsh D. Handbook of Lipid Bilayers (1990), CRC Press, Boca Raton FL
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197. Marsh D. Intrinsic curvature in normal and inverted lipid structures and in membranes. Biophys. J. 70 (1996) 2248-2255
198. Marsh D. Nonlamellar packing parameters for diacylglycerols. Biophys. J. 72 (1997) 2834-2836
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201. 31P NMR and X-ray diffraction. Biochemistry 24 (1985) 2902-2908
202. Seddon J.M., Kaye R.D., and Marsh D. Induction of the lamellar-inverted hexagonal phase transition in cardiolipin by protons and monovalent cations. Biochim. Biophys. Acta 734 (1983) 347-352
203. Sankaram M.B., Powell G.L., and Marsh D. Effect of acyl chain composition on salt-induced lamellar to inverted hexagonal phase transitions in cardiolipin. Biochim. Biophys. Acta 980 (1989) 389-392
204. 31P NMR spectroscopy and X-ray diffraction. Biochim. Biophys. Acta 690 (1982) 117-123
205. Cevc G., Seddon J.M., and Marsh D. The mechanism of regulation of membrane phase behaviour, structure and interactions by lipid headgroups and electrolyte solution. Faraday Discuss. Chem. Soc. 81 (1986) 179-189
206. II) phases. Biochim. Biophys. Acta 1327 (1997) 131-147
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208. Heimburg T., Ryba N.J.P., Würz U., and Marsh D. Phase transition from a gel to a fluid phase of cubic symmetry in dimyristoylphosphatidylcholine/myristic acid (1:2, mol/mol) bilayers. Biochim. Biophys. Acta 1025 (1990) 77-81
209. Heimburg T., Würz U., and Marsh D. Binary phase diagram of hydrated dimyristoylglycerol-dimyristoyl phosphatidylcholine mixtures. Biophys. J. 63 (1992) 1369-1378
210. Swamy M.J., Ramakrishnan M., Marsh D., and Würz U. Miscibility and phase behaviour of binary mixtures of N-palmitoylethanolamine and dipalmitoylphosphatidylcholine. Biochim. Biophys. Acta 1616 (2003) 174-183
211. Kamlekar R., Satyanarayana S., Marsh D., and Swamy M.J. Miscibility and phase behavior of N-acylethanolamine/diacylphosphatidylethanolamine binary mixtures of matched acyl chainlengths (n = 14, 16). Biophys. J. 92 (2007) 3968-3977
212. 31P NMR studies of N-biotinyl phosphatidylethanolamines. Biochemistry 32 (1993) 9960-9967
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216. King M.D., and Marsh D. Polymorphic phase behaviour of lysopalmitoylphosphatidylcholine in poly(ethylene glycol)-water mixtures. Biochemistry 28 (1989) 5643-5647
217. Marsh D. Scaling and mean-field theories applied to polymer brushes. Biophys. J. 86 (2004) 2630-2633
218. M. Esmann, N.U. Fedosova, D. Marsh, Osmotic stress and viscous retardation of the Na,K-ATPase ion pump, Biophys. J. (in press). doi:10.1529/biophysj.106.101774
219. Marsh D. Water adsorption isotherms and hydration forces for lysolipids and diacyl phospholipids. Biophys. J. 55 (1989) 1093-1100
220. 31P NMR study. Biochim. Biophys. Acta 685 (1982) 153-161
221. 2+ system. Eur. J. Biochem. 129 (1983) 621-625
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223. Powell G.L., Knowles P.F., and Marsh D. Incorporation of cytochrome oxidase into cardiolipin bilayers and induction of non-lamellar phases. Biochemistry 29 (1990) 5127-5132
224. de Grip W.J., Drenthe E.H.S., Van Echteld C.J.A., De Kruijff B., and Verkleij A.J. Possible role of rhodopsin in maintaining bilayer structure in the photoreceptor membrane. Biochim. Biophys. Acta 558 (1979) 330-337
225. Mollevanger L.C.P.J., and de Grip W.J. Phase behavior of isolated photoreceptor membrane lipids is modulated by bivalent cations. FEBS Lett. 169 (1984) 256-260
226. M. Esmann, D. Marsh, Influence of Na,K-ATPase on membrane lipid polymorphism, (in press).
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228. Killian J.A., Salemink I., de Planque M.R.R., Lindblom G., Koeppe II R.E., and Greathouse D.V. Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane α-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans. Biochemistry 35 (1996) 1037-1045
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234. Heimburg T., and Biltonen R.L. Thermotropic behavior of dimyristoylphopshatidylglycerol and its interaction with cytochrome c,. Biochemistry 33 (1994) 9477-9488
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236. Mariani P., Luzzati V., and Delacroix H. Cubic phases of lipid-containing systems-structure analysis and biological implications. J. Mol. Biol. 204 (1988) 165-188
237. Hildebrandt P., Heimburg T., and Marsh D. Quantitative conformational analysis of cytochrome c bound to phospholipid vesicles studied by resonance Raman spectroscopy. Eur. Biophys. J. 18 (1990) 193-201
238. Heimburg T., and Marsh D. Investigation of secondary and tertiary structural changes of cytochrome c in complexes with anionic lipids using amide hydrogen exchange measurements: an FTIR study. Biophys. J. 65 (1993) 2408-2417
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244. Perozo E., Kloda A., Cortes D.M., and Martinac B. Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating. Nat. Struct. Biol. 9 (2002) 696-703
245. Marsh D. Energetics of hydrophobic matching in lipid-protein interactions. Biophys. J. 94 (2008) 3996-4013
246. Williamson I.M., Alvis S.J., East J.M., and Lee A.G. Interactions of phospholipids with the potassium channel KcsA. Biophys. J. 83 (2002) 2026-2038
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248. Kučerka N., Tristram-Nagle S., and Nagle J.F. Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains. J. Membr. Biol. 208 (2005) 193-202
249. Marsh D. Comment on interpretation of mechanochemical properties of lipid bilayer vesicles from the equation of state or pressure-area measurement of the monolayer at the air-water or oil-water interface. Langmuir 22 (2006) 2916-2919
250. King M.D., and Marsh D. Headgroup and chain length dependence of phospholipid self-assembly studied by spin-label electron spin resonance. Biochemistry 26 (1987) 1224-1231
251. Sperotto M.M., and Mouritsen O.G. Dependence of lipid-membrane phase transition temperature on the mismatch of protein and lipid hydrophobic thickness. Eur. Biophys. J. Biophys. Lett. 16 (1988) 1-10
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258. Lewis R.N.A.H., Mak N., and McElhaney R.N. A differential scanning calorimetric study of the thermotropic phase behavior of model membranes composed of phosphatidylcholines containing linear saturated fatty acyl chains. Biochemistry 26 (1987) 6118-6126
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265. Attard G.S., Templer R.H., Smith W.S., Hunt A.N., and Jackowski S. Modulation of CTP:phosphocholine cytidylyltransferase by membrane curvature elastic stress. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 9032-9036
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270. Cantor C.R. Lateral pressures in cell membranes: a mechanism for modulation of protein function. J. Phys. Chem., B 101 (1997) 1723-1725
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275. Allen S.J., Curran A.R., Templer R.H., Meijberg W., and Booth P.J. Controlling the folding efficiency of an integral membrane protein. J. Mol. Biol. 342 (2004) 1293-1304
276. Marsh D. Elastic curvature constants of lipid monolayers and bilayers. Chem. Phys. Lipids 144 (2006) 146-159
277. Moe P., and Blount P. Assessment of potential stimuli for mechano-dependent gating of MscL: effects of pressure, tension, and lipid headgroups. Biochemistry 44 (2005) 12239-12244
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279. Liu Y.F., and Nagle J.F. Diffuse scattering provides material parameters and electron density profiles of biomembranes. Phys. Rev. E 69 (2004) 040901-1-040901-4
280. Marsh D., Watts A., Maschke W., and Knowles P.F. Protein-immobilized lipid in dimyristoylphosphatidylcholine-substituted cytochrome oxidase: evidence for both boundary and trapped-bilayer lipid. Biochem. Biophys. Res. Commun. 81 (1978) 403-409
281. Marsh D., and Páli T. Infrared dichroism from the x-ray structure of bacteriorhodopsin. Biophys. J. 80 (2001) 305-312
282. Stenkamp R.E., Filipek S., Driessen C.A.G.G., Teller D.C., and Palczewski K. Crystal structure of rhodopsin: a template for cone visual pigments and other G protein-coupled receptors. Biochim. Biophys. Acta 1565 (2002) 168-182
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