Specific anchoring modes of two distinct dystrophin rod sub-domains interacting in phospholipid Langmuir films studied by atomic force microscopy and PM-IRRAS

Biochimica et Biophysica Acta - Biomembranes

Volumn 1798, Issue 8, 2010, Pages 1503-1511

  Vie V ^a   Legardinier, S ^b   Chieze, L ^a   Le Bihan, O ^a   Qin, Y ^a   Sarkis, J ^a,b   Hubert, J F ^b   Renault, A ^a   Desbat, B ^c   Le Rumeur, E ^b  

^a UNIVERSITÉ DE RENNES 1   (France)

^b UNIVERSITÉ DE RENNES 1   (France)

^c UNIVERSITÉ DE BORDEAUX   (France)

Author keywords

Atomic force microscopy; Dystrophin rod domain; Langmuir films; Polarization modulation infrared spectroscopy; Spectrin like repeats

Indexed keywords

1,2 DIOLEYL SN GLYCERO 3 PHOSPHOCHOLINE; DYSTROPHIN; MINIDYSTROPHIN; PHOSPHOLIPID; PHOSPHORYLCHOLINE; THREO 3,4 DIHYDROXYPHENYLSERINE; UNCLASSIFIED DRUG;

ABSORPTION SPECTROSCOPY; ADSORPTION; AIR; ALPHA HELIX; ARTICLE; ATOMIC FORCE MICROSCOPY; DRUG BINDING; DRUG STRUCTURE; HYDROPHOBICITY; LIQUID; MEMBRANE BINDING; POLARIZATION MODULATED INFRARED REFLECTION ABSORPTION SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DEFICIENCY; PROTEIN DOMAIN; PROTEIN LIPID INTERACTION; PROTEIN SECONDARY STRUCTURE; STRUCTURAL HOMOLOGY;

EID: 77953692026     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.04.005     Document Type: Article

References (43)

1. Koenig M., Monaco A.P., Kunkel L.M. The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein. Cell 1988, 53:219-226.
2. Ohlendieck K., Campbell K. Dystrophin constitutes 5% of membrane cytoskeleton in skeletal muscle. FEBS Lett. 1991, 283:30-234.
3. Ervasti J.M. Dystrophin, its interactions with other proteins, and implications for muscular dystrophy. Biochim. Biophys. Acta 2007, 1772:108-117.
4. DeWolf C., McCauley P., Sikorski A.F., Winlove C.P., Bailey A.I., Kahana E., Pinder J.C., Gratzer W.B. Interaction of dystrophin fragments with model membranes. Biophys. J. 1997, 72:2599-2604.
5. Le Rumeur E., Fichou Y., Pottier S., Gaboriau F., Rondeau-Mouro C., Vincent M., Gallay J., Bondon A. Interaction of dystrophin rod domain with membrane phospholipids: evidence of a close proximity between tryptophan residues and lipids. J. Biol. Chem. 2003, 278:5993-6001.
6. Legardinier S., Raguénès-Nicol C., Tascon C., Rocher C., Hardy S., Hubert J.F., Le Rumeur E. Mapping of the lipid-binding and stability properties of the central rod domain of human dystrophin. J. Mol. Biol. 2009, 389:546-558.
7. Petrof B.J., Shrager J.B., Stedmann H.H., Kelly A.M., Sweeney H.L. Dystrophin protects the sarcolemma from stresses developed during muscle contraction. Proc. Natl. Acad. Sci. U. S. A. 1993, 90:3710-3714.
8. Straub V., Rafael J.A., Chamberlain J.S., Campbell K.P. Animal models for muscular dystrophy show different patterns of sarcolemmal disruption. J. Cell Biol. 1997, 139:375-385.
9. Nguyen F., Chérel Y., Guigand L., Goubault-Leroux I., Wyers M. Muscle lesions associated with dystrophin deficiency in neonatal golden retriever puppies. J. Comp. Pathol. 2002, 126:100-108.
10. Koenig M., Kunkel L.M. Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility. J. Biol. Chem. 1990, 265:4560-4566.
11. Winder S., Gibson T., Kendrick-Jones J. Dystrophin and utrophin: the missing links!. FEBS Lett. 1995, 369:27-33.
12. Legardinier S., Hubert J.-F., Le Bihan O., Tascon C., Rocher C., Raguénès-Nicol C., Bondon A., Hardy S., Le Test E. Sub-domains of the dystrophin rod domain display contrasting lipid-binding and stability properties. Biochim. Biophys. Acta 2008, 1784:672-682.
13. Brockman H. Lipid monolayers: why use half a membrane to characterize protein-membrane interactions?. Curr. Opin. Struct. Biol. 1999, 9:438-443.
14. Diakowski W., Sikorski A. Brain spectrin exerts much stronger effect on anionic phospholipid monolayers than erythroid spectrin. Biochim. Biophys. Acta 2002, 1564:403-411.
15. Grzybek M., Chorzalska A., Bok E., Hryniewicz-Jankowska A., Czogalla A., Diakowski W., Sikorski A.F. Spectrin-phospholipid interactions. Existence of multiple kinds of binding sites?. Chem. Phys. Lipids 2006, 141:133-141.
16. Blaudez D., Buffeteau T., Cornut J.-C., Desbat B., Escafre N., Pézolet M., Turlet J.-M. Polarization-modulated FT-IR spectroscopy of a spread monolayer at the air/water interface. Appl. Spectrosc. 1993, 47:869-874.
17. Bellet-Amalric E., Blaudez D., Desbat B., Graner F., Gauthier F., Renault A. Interaction of the third helix of Antennapedia homeodomain and a phospholipid monolayer, studied by ellipsometry and PM-IRRAS at the air-water interface. Biochim. Biophys. Acta 2000, 1467:131-143.
18. Vié V., Van Mau N., Chaloin L., Lesniewska E., Le Grimellec C., Heitz F. Detection of peptide-lipid interactions in mixed monolayers, using isotherms, atomic force microscopy, and fourier transform infrared analyses. Biophys. J. 2000, 78(2000):846-856.
19. Dubreil L., Vie V., Beaufils S., Marion D., Renault A. Aggregation of puroindoline in phospholipid monolayers spread at the air-liquid interface. Biophys. J. 2003, 85:2650-2660.
20. Bottier C., Gean J., Desbat B., Renault A., Marion D., Vie V. Structure and orientation of puroindolines into wheat galactolipid monolayers. Langmuir 2008, 24:10901-10909.
21. Blaudez D., Turlet J.-M., Dufourcq J., Bard D., Buffeteau T., Desbat B. Investigations at the air/water interface using polarization modulation IR spectroscopy. J. Chem. Soc. Faraday Trans. 1996, 92:525-530.
22. Castano S., Desbat B., Laguerre M., Dufourcq J. Structure, orientation and affinity for interfaces and lipids of ideally amphipathic lytic LiKj(i=2j) peptides. Biochim. Biophys. Acta 1999, 1416:176-194.
23. Buffeteau T., Calvez E.L., Castano S., Desbat B., Blaudez D., Dufourcq J. Anisotropic optical constants of α-helix and β-sheet secondary structures in the infrared. J. Phys. Chem. B 2000, 104:4537-4544.
24. Lavoie H., Desbat B., Vaknin D., Salesse C. Structure of rhodopsin in monolayers at the air-water interface: a PM-IRRAS and X-Ray Reflectivity study. Biochemistry 2002, 41:13424-13434.
25. Picard F., Buffeteau T., Desbat B., Auger M., Pezolet M. Quantitative orientation measurements in thin lipid films by attenuated total reflection infrared spectroscopy. Biophys. J. 1999, 76:539-551.
26. Ronzon F., Desbat B., Chauvet J.P., Roux B. Behavior of a GPI-anchored protein in phospholipid monolayers at the air-water interface. Biochim. Biophys. Acta 2002, 1560:1-13.
27. Estrela-Lopis I., Brezesinski G., Möhwald H. Dipalmitoyl phosphatidylcholine/phospholipase D interactions investigated with polarization-modulated infrared reflection absorption spectroscopy. Biophys. J. 2001, 80:749-754.
28. Castano S., Blaudez D., Desbat B., Dufourcq J., Wroblewski H. Secondary structure of spiralin in solution, at the air/water interface, and in interaction with lipid monolayers. Biochim. Biophys. Acta 2002, 1562(2002):45-56.
29. Saccani J., Castano S., Desbat B., Blaudez D. A phospholipid bilayer supported under a polymerized Langmuir film. Biophys. J. 2003, 85:3781-3787.
30. Le Calvez E., Blaudez D., Buffeteau T., Desbat B. Effect of cations on the dissociation of arachidonic acid monolayers on water studied by polarization-modulated infrared reflection-absorption spectroscopy. Langmuir 2001, 17:670-674.
31. Calvert R., Kahana E., Gratzer W.B. Stability of the dystrophin rod domain fold: evidence for nested repeating units. Biophys. J. 1996, 71:1605-1610.
32. Phillips M.C., Williams R.M., Chapman D. On the nature of hydrocarbon chain motions in lipid liquid crystals. Chem. Phys. Lipids 1969, 3:234-244.
33. Demel R.A., Geurts van Kessel W.S., Zwaal R.F., Roelofsen B., van Deenen L.L. Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayers. Biochim. Biophys. Acta 1975, 406:97-107.
34. Nagle J.F. Theory of lipid monolayer and bilayer phase transitions: effect of headgroup interactions. J. Membr. Biol. 1976, 27:233-250.
35. Blume A. A comparative study of the phase transitions of phospholipid bilayers and monolayers. Biochim. Biophys. Acta 1979, 557:32-44.
36. Banks G.B., Chamberlain J.S. The value of mammalian models for Duchenne muscular dystrophy in developing therapeutic strategies. Curr. Top. Dev. Biol. 2008, 84:431-453.
37. Prins K.W., Humston J.L., Mehta A., Tate V., Ralston E., Ervasti J.M. Dystrophin is a microtubule-associated protein. J. Cell Biol. 2009, 186:363-369.
38. Deconinck N., Dan B. Pathophysiology of Duchenne muscular dystrophy: current hypotheses. Pediatr. Neurol. 2007, 36:1-7.
39. Etard C., Behra M., Ertzer R., Fischer N., Jesuthasan S., Blader P., Geisler R., Strahle U. Mutation in the delta-subunit of the nAChR suppresses the muscle defects caused by lack of Dystrophin. Dev. Dyn. 2005, 234:1016-1025.
40. Hamill O., Martinac B. Molecular basis of mechanotransduction in living cells. Physiol. Rev. 2001, 81:685-740.
41. Sheetz M.P., Sable J.E., Dobereiner H.G. Continuous membrane-cytoskeleton adhesion requires continuous accommodation to lipid and cytoskeleton dynamics. Annu. Rev. Biophys. Biomol. Struct. 2006, 35:417-434.
42. Harper S.Q., Hauser M.A., DelloRusso C., Duan D., Crawford R.W., Phelps S.F., Harper H.A., Robinson A.S., Engelhardt J.F., Brooks S.V., Chamberlain J.S. Modular flexibility of dystrophin: implications for gene therapy of Duchenne muscular dystrophy. Nature Med. 2002, 8:253-261.
43. Liu M., Yue Y., Harper S., Grange R., Chamberlain J., Duan D. Adeno-associated virus-mediated microdystrophin expression protects young mdx muscle from contraction-induced injury. Mol. Ther. 2005, 11:245-256.