Parameters modulating the maximum insertion pressure of proteins and peptides in lipid monolayers

Biochimie

Volumn 91, Issue 6, 2009, Pages 718-733

  Calvez, Philippe ^a   Bussières, Sylvain ^a   Eric Demers ^a   Salesse, Christian ^a  

^a LAVAL UNIVERSITY   (Canada)

Author keywords

Air water interface; Critical exclusion surface pressure; Critical surface pressure; Exclusion pressure; Limiting surface pressure; Maximum insertion pressure; Membrane lateral pressure; Membrane associated proteins; Monolayer; Packing pressure protein; Peptides; Peripheral proteins; Surface pressure cut off

Indexed keywords

ALKALINE PHOSPHATASE; AMYLOID; APOLIPOPROTEIN; CHOLINE PHOSPHATE CYTIDYLYLTRANSFERASE; GLYCOLIPID; GLYCOSYLPHOSPHATIDYLINOSITOL; NEUROPEPTIDE Y; TRIACYLGLYCEROL LIPASE;

ACYLATION; LIPID MONOLAYER; PEPTIDE ANALYSIS; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW;

AMINO ACID SEQUENCE; LIPID BILAYERS; MEMBRANE LIPIDS; MEMBRANE PROTEINS; MODELS, THEORETICAL; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY;

EID: 67349258550     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2009.03.018     Document Type: Review

References (140)

1. Hunte C., and Richers S. Lipids and membrane protein structures. Curr. Opin. Struct. Biol. 18 (2008) 406-411
2. De Vries L., and Gist Farquhar M. RGS proteins: more than just GAPs for heterotrimeric G proteins. Trends Cell. Biol. 9 (1999) 138-144
3. Wensel T.G. Signal transducing membrane complexes of photoreceptor outer segments. Vis. Res. 48 (2008) 2052-2061
4. Cho W., and Stahelin R.V. Membrane-protein interaction in cell signaling and membrane trafficking. Annu. Rev. Biophys. Biomol. Struct. 34 (2005) 119-151
5. Van Den Brink-van der Laan E., Killian A.J., and de Kruijff B. Nonbilayer lipids affect peripheral and integral membrane proteins via changes in the lateral pressure profile. Biochim. Biophys. Acta 1666 (2004) 275-288
6. Lemmon M.A. Membrane recognition by phospholipid-binding domains. Nat. Rev. Mol. Cell. Biol. 9 (2008) 99-111
7. Sackmann E. Supported membranes: scientific and practical applications. Science 271 (1996) 43-48
8. Dynarowicz-Latka P., Dhanabalan A., and Oliveira Jr. O.N. Modern physicochemical research on Langmuir monolayers. Adv. Colloid Interface Sci. 91 (2001) 221-293
9. Brezesinski G., and Möhwald H. Langmuir monolayers to study interactions at model membrane surfaces. Adv. Colloid Interface Sci. 100-102 (2003) 563-584
10. Maget-Dana R. The monolayer technique: a potent tool for studying the interfacial properties of antimicrobial and membrane-lytic peptides and their interactions with lipid membranes. Biochim. Biophys. Acta 1462 (1999) 109-140
11. Brockman H. Lipid monolayers: why use half a membrane to characterize protein-membrane interactions?. Curr. Opin. Struct. Biol. 9 (1999) 438-443
12. 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
13. Feng S.S. 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 15 (1999) 998-1010
14. MacDonald R.C., and Simon S.A. Lipid monolayer states and their relationships to bilayers. Proc. Natl. Acad. Sci. U.S.A 84 (1987) 4089-4093
15. Baszkin A. Molecular recognition on the supported and on the air/water interface-spread protein monolayers. Adv. Colloid Interface Sci. 128-130 (2006) 111-120
16. Winget J.M., Pan Y.H., and Bahnson B.J. The interfacial binding surface of phospholipase A2s. Biochim. Biophys. Acta 1761 (2006) 1260-1269
17. Boucher J., Trudel E., Méthot M., Desmeules P., and Salesse C. Organization, structure and activity of proteins in monolayers. Colloids Surf. B. Biointerfaces 58 (2007) 73-90
18. Verger R., and Pattus F. Lipid-protein interactions in monolayers. Chem. Phys. Lipids 30 (1982) 189-227
19. Phillips M., and Sparks C. Properties of apolipoproteins at the air/water interface. Ann. N.Y. Acad. Sci. 348 (1980) 122-137
20. Bringezu F., Majerowicz M., Maltseva E., Wen S., Brezesinski G., and Waring A.J. Penetration of the antimicrobial peptide dicynthaurin into phospholipid monolayers at the liquid/air interface. Chembiochem 8 (2007) 1038-1047
21. Kennedy M.T., Brockman H., and Rusnak F. Determinants of calcineurin binding to model membranes. Biochemistry 36 (1997) 13579-13585
22. Wang S.X., Cai G.P., and Sui S.F. The insertion of human apolipoprotein H into phospholipid membranes: a monolayer study. Biochem. J. 335 (1998) 225-232
23. Weinberg R.B., Ibdah J.A., and Phillips M.C. Adsorption of apolipoprotein A-IV to phospholipid monolayers spread at the air/water interface. A model for its labile binding to high density lipoproteins. J. Biol. Chem. 267 (1992) 8977-8983
24. Eeman M., Berquand A., Dufrene Y.F., Paquot M., Dufour S., and Deleu M. Penetration of surfactin into phospholipid monolayers: nanoscale interfacial organization. Langmuir 22 (2006) 11337-11345
25. Gillotte K.L., Zaiou M., Lund-Katz S., Anantharamaiah G.M., Holvoet P., Dhoest A., Palgunachari M.N., Segrest J.P., Weisgraber K.H., Rothblat G.H., and Phillips M.C. Apolipoprotein-mediated plasma membrane microsolubilization. Role of the lipid affinity and membrane penetration in the efflux of cellular cholesterol and phospholipid. J. Biol. Chem. 274 (1999) 2021-2028
26. Varas M., Sanchez-Borzone M., Sanchez J.M., Barioglio S.R., and Perillo M.A. Surface behavior and peptide-lipid interactions of the cyclic neuropeptide melanin concentrating hormone. J. Phys. Chem. B. 112 (2008) 7330-7337
27. Lahdo R., and De La Fournière-Bessueille L. Insertion of the amyloid precursor protein into lipid monolayers: effects of cholesterol and apolipoprotein E. Biochem. J. 382 (2004) 987-994
28. Malkova S., Long F., Stahelin R.V., Pingali S.V., Murray D., Cho W., and Schlossman M.L. X-ray reflectivity studies of cPLA2α-C2 domains adsorbed onto Langmuir monolayers of SOPC. Biophys. J. 89 (2005) 1861-1873
29. Nylund M., Fortelius C., Palonen E.K., Molotkovsky J.G., and Mattjus P. Membrane curvature effects on glycolipid transfer protein activity. Langmuir 23 (2007) 11726-11733
30. Vernoux N., Maniti O., Besson F., Granjon T., Marcillat O., and Vial C. Mitochondrial creatine kinase adsorption to biomimetic membranes: a Langmuir monolayer study. J. Colloid Interface Sci. 310 (2007) 436-445
31. Kouzayha A., and Besson F. GPI-alkaline phosphatase insertion into phosphatidylcholine monolayers: phase behavior and morphology changes. Biochem. Biophys. Res. Commun. 333 (2005) 1315-1321
32. Lahdo R., Coillet-Matillon S., Chauvet J.P., and De La Fournière-Bessueille L. The amyloid precursor protein interacts with neutral lipids. Eur. J. Biochem. 269 (2002) 2238-2246
33. Thuduppathy G.R., Terrones O., Craig J.W., Basanez G., and Hill R.B. The N-terminal domain of Bcl-xL reversibly binds membranes in a pH-dependent manner. Biochemistry 45 (2006) 14533-14542
34. Lichtenbergova L., Yoon E.T., and Cho W. Membrane penetration of cytosolic phospholipase A2 is necessary for its interfacial catalysis and arachidonate specificity. Biochemistry 37 (1998) 14128-14136
35. Wijewickrama G.T., Albanese A., Kim Y.J., Oh Y.S., Murray P.S., Takayanagi R., Tobe T., Masuda S., Murakami M., Kudo I., Ucker D.S., Murray D., and Cho W. Unique membrane interaction mode of group IIF phospholipase A2. J. Biol. Chem. 281 (2006) 32741-32754
36. Johnson J.E., Rao N.M., Hui S.W., and Cornell R.B. Conformation and lipid binding properties of four peptides derived from the membrane-binding domain of CTP:phosphocholine cytidylyltransferase. Biochemistry 37 (1998) 9509-9519
37. Engel M.F., Yigittop H., Elgersma R.C., Rijkers D.T., Liskamp R.M.J., de Kruijff B., Hôppener J.W., and Killian A.J. Islet amyloid polypeptide inserts into phospholipid monolayers as monomer. J. Mol. Biol. 356 (2006) 783-789
38. Sood R., Domanov Y., Pietiäinen M., Kontinen V.P., and Kinnunen P.K.J. Binding of LL-37 to model biomembranes: insight into target vs host cell recognition. Biochim. Biophys. Acta 1778 (2008) 983-996
39. Demel R.A., Geurts van Kessel W.S., Zwaal R.F., Roelofsen B., and van Deenen L.L. Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayers. Biochim. Biophys. Acta 406 (1975) 97-107
40. Blume A., and Eibl H. The influence of charge on bilayer membranes. Calorimetric investigations of phosphatidic acid bilayers. Biochim. Biophys. Acta 558 (1979) 13-21
41. Moreau H., Pieroni G., Jolivet-Reynaud C., Alouf J.E., and Verger R. A new kinetic approach for studying phospholipase C (Clostridium perfringens α toxin) activity on phospholipid monolayers. Biochemistry 27 (1988) 2319-2323
42. Seelig A. Local anesthetics and pressure: a comparison of dibucaine binding to lipid monolayers and bilayers. Biochim. Biophys. Acta 899 (1987) 196-204
43. Silvius J.R. Role of cholesterol in lipid raft formation: lessons from lipid model systems. Biochim. Biophys. Acta 1610 (2003) 174-183
44. Boguslavsky V., Rebecchi M., Morris A.J., Jhon D.Y., Rhee S.G., and McLaughlin S. Effect of monolayer surface pressure on the activities of phosphoinositide-specific phospholipase C-β1, -γ1, and -δ1. Biochemistry 33 (1994) 3032-3037
45. Marsh D. Lateral pressure in membranes. Biochim. Biophys. Acta 1286 (1996) 183-223
46. Albrecht O., Gruler H., and Sackmann E. Polymorphism of phospholipid monolayers. J. Physique 39 (1978) 301
47. Hui S.W., Cowden M., Papahadjopoulos D., and Parsons D.F. Electron diffraction study of hydrated phospholipid single bilayers. Effects of temperature hydration and surface pressure of the "precursor" monolayer. Biochim. Biophys. Acta 382 (1975) 265-275
48. Steinmetz A. Intestinal apolipoprotein metabolism. Klin. Wochenschr 68 (1990) 12-18
49. Gordon D.J., and Rifkind B.M. Treating high blood cholesterol in the older patient. Am. J. Cardiol. 63 (1989) 48H-52H
50. Oram J.F., and Yokoyama S. Apolipoprotein-mediated removal of cellular cholesterol and phospholipids. J. Lipid. Res. 37 (1996) 2473-2491
51. Fielding C.J., and Fielding P.E. Molecular physiology of reverse cholesterol transport. J. Lipid Res. 36 (1995) 211-228
52. Segrest J.P., Garber D.W., Brouillette C.G., Harvey S.C., and Anantharamaiah G.M. The amphipathic alpha helix: a multifunctional structural motif in plasma apolipoproteins. Adv. Protein Chem. 45 (1994) 303-369
53. Segrest J.P., Jones M.K., De Loof H., Brouillette C.G., Venkatachalapathi Y.V., and Anantharamaiah G.M. The amphipathic helix in the exchangeable apolipoproteins: a review of secondary structure and function. J. Lipid Res. 33 (1992) 141-166
54. Rall Jr. S.C., Weisgraber K.H., and Mahley R.W. Human apolipoprotein E. The complete amino acid sequence. J. Biol. Chem. 257 (1982) 4171-4178
55. Ghiselli G., Krishnan S., Beigel Y., and Gotto Jr. A.M. Plasma metabolism of apolipoprotein A-IV in humans. J. Lipid Res. 27 (1986) 813-827
56. Weinberg R.B., and Jordan M.K. Effects of phospholipid on the structure of human apolipoprotein A-IV. J. Biol. Chem. 265 (1990) 8081-8086
57. Kertesz Z., Yu B.B., Steinkasserer A., Haupt H., Benham A., and Sim R.B. Characterization of binding of human beta 2-glycoprotein I to cardiolipin. Biochem. J. 310 (1995) 315-321
58. Hagihara Y., Goto Y., Kato H., and Yoshimura T. Role of the N- and C-terminal domains of bovine beta 2-glycoprotein I in its interaction with cardiolipin. J. Biochem. 118 (1995) 129-136
59. Willems G.M., Janssen M.P., Pelsers M.M., Comfurius P., Galli M., Zwaal R.F., and Bevers E.M. Role of divalency in the high-affinity binding of anticardiolipin antibody-beta 2-glycoprotein I complexes to lipid membranes. Biochemistry 35 (1996) 13833-13842
60. Palgunachari M.N., Mishra V.K., Lund-Katz S., Phillips M.C., Adeyeye S.O., Alluri S., Anantharamaiah G.M., and Segrest J.P. Only the two end helixes of eight tandem amphipathic helical domains of human Apo A-I have Significant lipid affinity: implications for HDL assembly. Arterioscler. Thromb. Vasc. Biol. 16 (1996) 328-338
61. Marcillat O., Goldschmidt D., Eichenberger D., and Vial C. Only one of the two interconvertible forms of mitochondrial creatine kinase binds to heart mitoplasts. Biochim. Biophys. Acta 890 (1987) 233-241
62. Schlegel J., Zurbriggen B., Wegmann G., Wyss M., Eppenberger H.M., and Wallimann T. Native mitochondrial creatine kinase forms octameric structures. Isolation of two interconvertible mitochondrial creatine kinase forms, dimeric and octameric mitochondrial creatine kinase: characterization, localization, and structure-function relationships. J. Biol. Chem. 263 (1988) 16942-16953
63. Vacheron M.J., Clottes E., Chautard C., and Vial C. Mitochondrial creatine kinase interaction with phospholipid vesicles. Arch. Biochem. Biophys. 344 (1997) 316-324
64. Yamada K., Abe A., and Sasaki T. Glycolipid transfer protein from pig brain transfers glycolipids with beta-linked sugars but not with alpha-linked sugars at the sugar-lipid linkage. Biochim. Biophys. Acta 879 (1986) 345-349
65. Malinina L., Malakhova M.L., Teplov A., Brown R.E., and Patel D.J. Structural basis for glycosphingolipid transfer specificity. Nature 430 (2004) 1048-1053
66. Ikezawa H. Glycosylphosphatidylinositol (GPI)-anchored proteins. Biol. Pharm. Bull. 25 (2002) 409-417
67. Simons K., and Ikonen E. Functional rafts in cell membranes. Nature 387 (1997) 569-572
68. Shenolikar S., and Nairn A.C. Protein phosphatases: recent progress. Adv. Second Messenger Phosphoprotein Res. 23 (1991) 1-121
69. Towler D.A., Gordon J.I., Adams S.P., and Glaser L. The biology and enzymology of eukaryotic protein acylation. Annu. Rev. Biochem. 57 (1988) 69-99
70. Ames J.B., Tanaka T., Stryer L., and Ikura M. Portrait of a myristoyl switch protein. Curr. Opin. Struct. Biol. 6 (1996) 432-438
71. Braunewell K.H., and Szanto A.J. Visinin-like proteins (VSNLs): interaction partners and emerging functions in signal transduction of a subfamily of neuronal Ca2+ -sensor proteins. Cell. Tissue Res. 335 (2009) 301-316
72. 2+-sensor proteins: multitalented regulators of neuronal function. Trends Neurosci. 27 (2004) 203-209
73. Iwasaki Y., and Yamane T. Enzymatic synthesis of structured lipids. Adv. Biochem. Eng. Biotechnol. 90 (2004) 151-171
74. Six D.A., and Dennis E.A. The expanding superfamily of phospholipase A2 enzymes: classification and characterization. Biochim. Biophys. Acta 1488 (2000) 1-19
75. Burke J.E., and Dennis E.A. Phospholipase A2 structure/function, mechanism, and signaling. J. Lipid Res. 50 (2009) S237-S242
76. Shimizu T., Ohto T., and Kita Y. Cytosolic phospholipase A2: biochemical properties and physiological roles. IUBMB Life 58 (2006) 328-333
77. Hirabayashi T., Murayama T., and Shimizu T. Regulatory mechanism and physiological role of cytosolic phospholipase A2. Biol. Pharm. Bull. 27 (2004) 1168-1173
78. Simkhada J.R., Cho S.S., Lee H.J., and Yoo J.C. Purification and biochemical properties of phospholipase D (PLD57) produced by Streptomyces sp. CS-57. Arch. Pharm. Res. 30 (2007) 1302-1308
79. El Kirat K., Besson F., Prigent A.F., Chauvet J.P., and Roux B. Role of calcium and membrane organization on phospholipase D localization and activity. Competition between a soluble and an insoluble substrate. J. Biol. Chem. 277 (2002) 21231-21236
80. Yamamoto I., Konto A., Handa T., and Miyajima K. Regulation of phospholipase D activity by neutral lipids in egg-yolk phosphatidylcholine small unilamellar vesicles and by calcium ion in aqueous medium. Biochim. Biophys. Acta 1233 (1995) 21-26
81. El Kirat K., Chauvet J.P., Roux B., and Besson F. Streptomyces chromofuscus phospholipase D interaction with lipidic activators at the air/water interface. Biochim. Biophys. Acta 1661 (2004) 144-153
82. Noinville S., Revault M., Baron M.H., Tiss A., Yapoudjian S., Ivanova M., and Verger R. Conformational changes and orientation of Humicola lanuginosa lipase on a solid hydrophobic surface: an in situ interface Fourier transform infrared-attenuated total reflection study. Biophys. J. 82 (2002) 2709-2719
83. Chahinian H., Bezzine S., Ferrato F., Ivanova M.G., Perez B., Lowe M.E., and Carriere F. The β5' loop of the pancreatic lipase C2-like domain plays a critical role in the lipase-lipid interactions. Biochemistry 41 (2002) 13725-13735
84. Hermoso J., Pignol D., Penel S., Roth M., Chapus C., and Fontecilla-Camps J.C. Neutron crystallographic evidence of lipase-colipase complex activation by a micelle. EMBO J. 16 (1997) 5531-5536
85. Pignol D., Ayvazian L., Kerfelec B., Timmins P., Crenon I., Hermoso J., Fontecilla-Camps J.C., and Chapus C. Critical role of micelles in pancreatic lipase activation revealed by small angle neutron scattering. J. Biol. Chem. 275 (2000) 4220-4224
86. Bezzine S., Carriere F., De Caro J., Verger R., and De Caro A. Human pancreatic lipase: an exposed hydrophobic loop from the C-terminal domain may contribute to interfacial binding. Biochemistry 37 (1998) 11846-11855
87. Thomas L., Scheidt H.A., Bettio A., Huster D., Beck-Sickinger A.G., Arnold K., and Zschörnig O. Membrane interaction of neuropeptide Y detected by EPR and NMR spectroscopy. Biochim. Biophys. Acta 1714 (2005) 103-113
88. Dyck M., and Lösche M. Interaction of the neurotransmitter, neuropeptide Y, with phospholipid membranes: film balance and fluorescence microscopy studies. J. Phys. Chem. B. 110 (2006) 22143-22151
89. Monks S.A., Karagianis G., Howlett G.J., and Norton R.S. Solution structure of human neuropeptide Y. J. Biomol. NMR 8 (1996) 379-390
90. Bader R., Bettio A., Beck-Sickinger A.G., and Zerbe O. Structure and dynamics of micelle-bound neuropeptide Y: comparison with unligated NPY and implications for receptor selection. J. Mol. Biol. 305 (2001) 307-329
91. Dyck M., Kerth A., Blume A., and Lösche M. Interaction of the neurotransmitter, neuropeptide Y, with phospholipid membranes: infrared spectroscopic characterization at the air/water interface. J. Phys. Chem. B 110 (2006) 22151
92. Kopitar M., Ritonja A., Popovic T., Gabrijelcic D., Krizaj I., and Turk V. A new type of low-molecular mass cysteine proteinase inhibitor from pig leukocytes. Biol. Chem. Hoppe Seyler 370 (1989) 1145-1151
93. Matsuzaki K., Sugishita K.I., Ishibe N., Ueha M., Nakata S., Miyajima K., and Epand R.M. Relationship of membrane curvature to the formation of pores by magainin 2. Biochemistry 37 (1998) 11856-11863
94. Yang D., Chertov O., and Oppenheim J.J. Participation of mammalian defensins and cathelicidins in anti-microbial immunity: receptors and activities of human defensins and cathelicidin (LL-37). J. Leukoc. Biol. 69 (2001) 691-697
95. Zanetti M., Del Sal G., Storici P., Schneider C., and Romeo D. The cDNA of the neutrophil antibiotic Bac5 predicts a pro-sequence homologous to a cysteine proteinase inhibitor that is common to other neutrophil antibiotics. J. Biol. Chem. 268 (1993) 522-526
96. Agerberth B., Charo J., Werr J., Olsson B., Idali F., Lindbom L., Kiessling R., Jornvall H., Wigzell H., and Gudmundsson G.H. The human antimicrobial and chemotactic peptides LL-37 and α-defensins are expressed by specific lymphocyte and monocyte populations. Blood 96 (2000) 3086-3093
97. Ritonja A., Kopitar M., Jerala R., and Turk V. Primary structure of a new cysteine proteinase inhibitor from pig leucocytes. FEBS Lett. 255 (1989) 211-214
98. Frohm M., Agerberth B., Ahangari G., Stahle-Backdahl M., Liden S., Wigzell H., and Gudmundsson G.H. The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J. Biol. Chem. 272 (1997) 15258-15263
99. Sevcsik E., Pabst G., Richter W., Danner S., Amenitsch H., and Lohner K. Interaction of LL-37 with model membrane systems of different complexity: influence of the lipid matrix. Biophys. J. 94 (2008) 4688-4699
100. Bernheimer A.W., and Avigad L.S. Nature and properties of a cytolytic agent produced by Bacillus subtilis. J. Gen. Microbiol. 61 (1970) 361-369
101. Vollenbroich D., Özel M., Vater J., Kamp R.M., and Pauli G. Mechanism of inactivation of enveloped viruses by the biosurfactants surfactin from Bacillus subtilis. Biologicals 25 (1997) 289-297
102. Lee I.H., Lee Y.S., Kim C.H., Kim C.R., Hong T., Menzel L., Boo L.M., Pohl J., Sherman M.A., Waring A., and Lehrer R.I. Dicynthaurin: an antimicrobial peptide from hemocytes of the solitary tunicate, Halocynthia aurantium. Biochim. Biophys. Acta 1527 (2001) 141-148
103. Blaudez D., Turlet J.M., Dufourcq J., Bard D., Buffeteau T., and Desbat B. Investigations at the air/water interface using polarization modulation IR spectroscopy. J. Chem. Soc. 92 (1996) 525-530
104. Kerth A., Erbr A., Dathe M., and Blume A. Infrared reflection absorption spectroscopy of amphipathic model peptides at the air/water interface. Biophys. J. 86 (2004) 3750-3758
105. Kajava A.V., Aebi U., and Steven A.C. The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin. J. Mol. Biol. 348 (2005) 247-252
106. Lorenzo A., Razzaboni B., Weir G.C., and Yankner B.A. Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus. Nature 368 (1994) 756-760
107. Jayasinghe S.A., and Langen R. Lipid membranes modulate the structure of islet amyloid polypeptide β. Biochemistry 44 (2005) 12113-12119
108. Ancelin M.L., and Vial H.J. Regulation of phosphatidylcholine biosynthesis in Plasmodium-infected erythrocytes. Biochim. Biophys. Acta 1001 (1989) 82-89
109. Carman G.M., and Henry S.A. Phospholipid biosynthesis in yeast. Annu. Rev. Biochem. 58 (1989) 635-669
110. Dunne S.J., Cornell R.B., Johnson J.E., Glover N.R., and Tracey A.S. Structure of the membrane binding domain of CTP: phosphocholine cytidylyltransferase. Biochemistry 35 (1996) 11975-11984
111. Calvert P.D., Govardovskii V.I., Krasnoperova N., Anderson R.E., Lem J., and Makino C.L. Membrane protein diffusion sets the speed of rod phototransduction. Nature 411 (2001) 90-94
112. Feller S.E., and Gawrisch K. Properties of docosahexaenoic-acid-containing lipids and their influence on the function of rhodopsin. Curr. Opin. Struct. Biol. 15 (2005) 416-422
113. Lamb T.D. Gain and kinetics of activation in the G-protein cascade of phototransduction. Proc. Natl. Acad. Sci. U.S.A 93 (1996) 566-570
114. Arshavsky V.Y., Lamb T.D., and Pugh E.N. G proteins and phototransduction. Annu. Rev. Physiol. 64 (2002) 153-187
115. Segrest J.P., Jackson R.L., Morrisett J.D., and Gotto A.M. A molecular theory of lipid-protein interactions in the plasma lipoproteins. FEBS Lett. 38 (1974) 247-253
116. Atkinson D., and Small D.M. Recombinant lipoproteins: implications for structure and assembly of native lipoproteins. Annu. Rev. Biophys. Biophys. Chem. 15 (1986) 403-456
117. Mattjus P. Glycolipid transfer proteins and membrane interaction. Biochim. Biophys. Acta 1788 (2009) 267-272
118. Maniti O. La créatine kinase mitochondriale-organisatrice de la membrane mitochondriale? Ségrégation de la cardiolipine sur des monocouches phospholipidiques. Perturbations induites par un agent issu de la peroxidation lipidique, le 4-hydroxynonénal (2008), Université Claude Bernard, Lyon p. 147
119. Bi X., Flach C.R., Perez-Gil J., Plasencia I., Andreu D., Oliveira E., and Mendelsohn R. Secondary structure and lipid interactions of the N-terminal segment of pulmonary surfactant SP-C in Langmuir films: IR reflection-absorption spectroscopy and surface pressure studies. Biochemistry 41 (2002) 8385-8395
120. Desmeules P., Penney S.E., Desbat B., and Salesse C. Determination of the contribution of the myristoyl group and hydrophobic amino acids of recoverin on its dynamics of binding to lipid monolayers. Biophys. J. 93 (2007) 2069-2082
121. Meister A., Nicolini C., Waldmann H., Kuhlmann J., Kerth A., Winter R., and Blume A. Insertion of lipidated ras proteins into lipid monolayers studied by infrared reflection absorption spectroscopy (IRRAS). Biophys. J. 91 (2006) 1388-1401
122. Muenter A.H., Hentschel J., Borner H.G., and Brezesinski G. Characterization of peptide-guided polymer assembly at the air/water interface. Langmuir 24 (2008) 3306-3316
123. Wang L., Cai P., Galla H.J., He H., Flach C.R., and Mendelsohn R. Monolayer-multilayer transitions in a lung surfactant model: IR reflection-absorption spectroscopy and atomic force microscopy. Eur. Biophys. J. 34 (2005) 243-254
124. Lavoie H., Blaudez D., Vaknin D., Desbat B., Ocko B.M., and Salesse C. Spectroscopic and structural properties of valine gramicidin A in monolayers at the air/water interface. Biophys. J. 83 (2002) 3558-3569
125. Martin B.A., Oxhorn B.C., Rossow C.R., and Perrino B.A. A cluster of basic amino acid residues in calcineurin B participates in the binding of calcineurin to phosphatidylserine vesicles. J. Biochem. 129 (2001) 843-849
126. Perisic O., Fong S., Lynch D.E., Bycroft M., and Williams R.L. Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2. J. Biol. Chem. 273 (1998) 1596-1604
127. Resh M.D. Membrane targeting of lipid modified signal transduction proteins. Subcell. Biochem. 37 (2004) 217-232
128. McLaughlin S., and Aderem A. The myrstoyl electrostatic switch: a modulator of reversible protein-membrane interactions. Trends Biochem. Sci. 20 (1995) 272-276
129. Nosjean O., Briolay A., and Roux B. Mammalian GPI proteins: sorting, membrane residence and functions. Biochim. Biophys. Acta 1331 (1997) 153-186
130. Fergusson M.A. The structure, biosynthesis and functions of glycosylphosphatidyl-inositol anchors, and the contributions of trypanosome research. J. Cell. Sci. 112 (1999) 2799-2809
131. Cross B., Ronzon F., Roux B., and Rieu J.P. Measurement of the anchorage force between GPI-anchored alkaline phosphatase and supported membranes by AFM force spectroscopy. Langmuir 21 (2005) 5149-5153
132. Giocondi M.C., Seantier B., Dosset P., Milhiet P.E., and Le Grimellec C. Characterizing the interactions between GPI-anchored alkaline phosphatases and membrane domains by AFM. Pflugers Arch. 456 (2008) 179-188
133. Kenworthy A.K., and Edidin M. Imaging fluorescence resonance energy transfer as probe of membrane organization and molecular associations of GPI-anchored proteins. Methods Mol. Biol. 116 (1999) 37-49
134. Kennedy M.T., Brockman H., and Rusnak F. Contributions of myristoylation to calcineurin structure/function. J. Biol. Chem. 271 (1996) 26517-26521
135. Desmeules P., Grandbois M., Bondarenko V.A., Yamazaki A., and Salesse C. Measurement of membrane binding between recoverin, a calcium-myristoyl switch protein, and lipid bilayers by AFM-based force spectroscopy. Biophys. J. 82 (2002) 3343-3350
136. Lange C., and Koch K.W. Calcium-dependent binding of recoverin to membranes monitored by surface plasmon resonance spectroscopy in real time. Biochemistry 36 (1997) 12019-12026
137. Lamarche F., Téchy F., Aghion J., and Leblanc R.M. Surface pressure, surface potential and ellipsometric study of cytochrome c binding to dioleoylphosphatidylcholine monolayer at the air-water interface. Colloids Surf. B. Biointerfaces 30 (1988) 209-222
138. Chapple J.P., Grayson C., Hardcastle A.J., Bailey T.A., Matter K., Adamson P., Graham C.H., Willison K.R., and Cheetham M.E. Organization on the plasma membrane of the retinitis pigmentosa protein RP2: investigation of association with detergent-resistant membranes and polarized sorting. Biochem. J. 372 (2003) 427-433
139. Mingotaud A.F., Mingotaud C., and Patterson L.K. Handbook of Monolayers (1993), Academic Press, London
140. Jnet. http://www.compbio.dundee.ac.uk/∼www-jpred/