Utility of surface-supported bilayers in studies of transmembrane helix dimerization

Journal of Structural Biology

Volumn 168, Issue 1, 2009, Pages 53-60

  Li, Edwin ^a   Merzlyakov, Mikhail ^a   Lin, Janice ^a   Searson, Peter ^a   Hristova, Kalina ^a  

^a Johns Hopkins University   (United States)

Author keywords

Supported bilayers; Thermodynamics; Transmembrane helix dimerization

Indexed keywords

MEMBRANE PROTEIN;

ARTICLE; BACTERIAL MEMBRANE; CELL MEMBRANE; DIMERIZATION; EUKARYOTE; LIPID BILAYER; PRIORITY JOURNAL;

ANIMALS; HUMANS; LIPID BILAYERS; MEMBRANE PROTEINS; MODELS, THEORETICAL; PROTEIN MULTIMERIZATION;

BACTERIA (MICROORGANISMS); EUKARYOTA;

EID: 69249219030     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2009.03.005     Document Type: Article

References (57)

1. Artemenko E.O., Egorova N.S., Arseniev A.S., and Feofanov A.V. Transmembrane domain of EphA1 receptor forms dimers in membrane-like environment. Biochim. Biophys. Acta 1778 (2008) 2361-2367
2. Bormann B.J., and Engelman D.M. Intramembrane helix-helix association in oligomerization and transmembrane signaling. Annu. Rev. Biophys. Biomol. Struc. 21 (1992) 223-242
3. Chang W.K., Wimley W.C., Searson P.C., Hristova K., and Merzlyakov M. Characterization of antimicrobial peptide activity by electrochemical impedance spectroscopy. Biochim. Biophys. Acta 1778 (2008) 2430-2436
4. Chen, L., Merzlyakov, M., Cohen, T., Shai, Y., Hristova, K., 2009. Energetics of ErbB1 transmembrane domain dimerization in lipid bilayers. Biophys. J. 96.
5. Crane J.M., Kiessling V., and Tamm L.K. Measuring lipid asymmetry in planar supported bilayers by fluorescence interference contrast microscopy. Langmuir 21 (2005) 1377-1388
6. Cristian L., Lear J.D., and DeGrado W.F. Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers. Proc. Nat. Acad. Sci. USA 100 (2003) 14772-14777
7. Duong M.T., Jaszewski T.M., Fleming K.G., and MacKenzie K.R. Changes in apparent free energy of helix-helix dimerization in a biological membrane due to point mutations. J. Mol. Biol. 371 (2007) 422-434
8. Fantl W.J., Johnson D.E., and Williams L.T. Signaling by receptor tyrosine kinases. Annu. Rev. Biochem. 62 (1993) 453-481
9. Finger C., Volkmer T., Prodohl A., Otzen D.E., Engelman D.M., and Schneider D. The stability of transmembrane helix interactions measured in a biological membrane. J. Mol. Biol. 358 (2006) 1221-1228
10. Gerber D., Sal-Man N., and Shai Y. Two motifs within a transmembrane domain, one for homodimerization and the other for heterodimerization. J. Biol. Chem. 279 (2004) 21177-21182
11. Gurezka R., and Langosch D. In vitro selection of membrane-spanning leucine zipper protein-protein interaction motifs using POSSYCCAT. J. Biol. Chem. 276 (2001) 45580-45587
12. He L., and Hristova K. Pathogenic activation of receptor tyrosine kinases in mammalian membranes. J. Mol. Biol. 384 (2008) 1130-1142
13. Hubbard S.R., and Miller W.T. Receptor tyrosine kinases: mechanisms of activation and signaling. Curr. Opin. Cell Biol. 19 (2007) 117-123
14. Huber O., Kemler R., and Langosch D. Mutations affecting transmembrane segment interactions impair adhesiveness of E-cadherin. J. Cell Sci. 112 (1999) 4415-4423
15. Langosch D., Brosig B., Kolmar H., and Fritz H.J. Dimerisation of the glycophorin a transmembrane segment in membranes probed with the ToxR transcription activator. J. Mol. Biol. 263 (1996) 525-530
16. Lemmon M.A., and Engelman D.M. Specificity and promiscuity in membrane helix interactions. Q. Rev. Biophys. 27 (1994) 157-218
17. Li E., and Hristova K. Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies. Biochemistry 45 (2006) 6241-6251
18. Li E., You M., and Hristova K. SDS-PAGE and FRET suggest weak interactions between FGFR3 TM domains in the absence of extracellular domains and ligands. Biochemistry 44 (2005) 352-360
19. Li E., You M., and Hristova K. FGFR3 dimer stabilization due to a single amino acid pathogenic mutation. J. Mol. Biol. 356 (2006) 600-612
20. Lin J., Merzlyakov M., Hristova K., and Searson P.C. Impedance spectroscopy of bilayer membranes on single crystal silicon. Biointerphases 3 (2008) 33-40
21. Liu J.F., and Rost B. Comparing function and structure between entire proteomes. Protein Sci. 10 (2001) 1970-1979
22. Lofts F.J., Hurst H.C., Sternberg M.J.E., and Gullick W.J. Specific short transmembrane sequences can inhibit transformation by the mutant neu growth-factor receptor in-vitro and in-vivo. Oncogene 8 (1993) 2813-2820
23. Longo N., Shuster R.C., Griffin L.D., Langley S.D., and Elsas L.J. Activation of insulin-receptor signaling by a single amino-acid substitution in the transmembrane domain. J. Biol. Chem. 267 (1992) 12416-12419
24. MacKenzie K.R. Folding and stability of alpha-helical integral membrane proteins. Chem. Rev. 106 (2006) 1931-1977
25. Merzlyakov M., Chen L., and Hristova K. Studies of receptor tyrosine kinase transmembrane domain interactions: The EmEx-FRET method. J. Membr. Biol. 215 (2007) 93-103
26. Merzlyakov M., Li E., Casas R., and Hristova K. Spectral Forster resonance energy transfer detection of protein interactions in surface-supported bilayers. Langmuir 22 (2006) 6986-6992
27. Merzlyakov M., Li E., Gitsov I., and Hristova K. Surface-supported bilayers with transmembrane proteins: role of the polymer cushion revisited. Langmuir 22 (2006) 10145-10151
28. Merzlyakov M., Li E., and Hristova K. Directed assembly of surface-supported bilayers with transmembrane helices. Langmuir 22 (2006) 1247-1253
29. Merzlyakov M., Li E., and Hristova K. Surface supported bilayer platform for studies of lateral association of proteins in membranes. Biointerphases 3 (2008) 80-84
30. Merzlyakov M., You M., Li E., and Hristova K. Transmembrane helix heterodimerization in lipids bilayers: probing the energetics behind autosomal dominant growth disorders. J. Mol. Biol. 358 (2006) 1-7
31. Meyers G.A., Orlow S.J., Munro I.R., Przylepa K.A., and Jabs E.W. Fibroblast-growth-factor-receptor-3 (Fgfr3) transmembrane mutation in Crouzon-syndrome with Acanthosis nigricans. Nat. Genet. 11 (1995) 462-464
32. Nagy J.K., Lonzer W.L., and Sanders C.R. Kinetic study of folding and misfolding of diacylglycerol kinase in model membranes. Biochemistry 40 (2001) 8971-8980
33. Nikolov V., Lin J., Merzlyakov M., Hristova K., and Searson P.C. Electrical measurements of bilayer membranes formed by Langmuir-Blodgett deposition on single-crystal silicon. Langmuir 23 (2007) 13040-13045
34. Oxenoid K., Sönnichsen F.D., and Sanders C.R. Conformationally specific misfolding of an integral membrane protein. Biochemistry 40 (2001) 5111-5118
35. Popot J.-L., and Engelman D.M. Helical membrane protein folding, stability, and evolution. Annu. Rev. Biochem. 69 (2000) 881-922
36. Posokhov Y.O., Merzlyakov M., Hristova K., and Ladokhin A.S. A simple "proximity" correction for Forster resonance energy transfer efficiency determination in membranes using lifetime measurements. Anal. Biochem. 380 (2008) 134-136
37. Ridder A., Skupjen P., Unterreitmeier S., and Langosch D. Tryptophan supports interaction of transmembrane helices. J. Mol. Biol. 354 (2005) 894-902
38. Ruan W.M., Becker V., Klingmuller U., and Langosch D. The interface between self-assembling erythropoietin receptor transmembrane segments corresponds to a membrane-spanning leucine zipper. J. Biol. Chem. 279 (2004) 3273-3279
39. Russ W.P., and Engelman D.M. TOXCAT: a measure of transmembrane helix association in a biological membrane. Proc. Natl. Acad. Sci. USA 96 (1999) 863-868
40. Sackmann E. Supported membranes: scientific and practical applications. Science 271 (1996) 43-48
41. Sackmann E., and Tanaka M. Supported membranes on soft polymer cushions: fabrication, characterization and applications. Trends Biotechnol. 18 (2000) 58-64
42. Sanders C.R., Ismail-Beigi F., and McEnery M.W. Mutations of peripheral myelin protein 22 result in defective trafficking through mechanisms which may be common to diseases involving tetraspan membrane proteins. Biochemistry 40 (2001) 9453-9459
43. Schneider D., and Engelman D.M. GALLEX, a measurement of heterologous association of transmembrane helices in a biological membrane. J. Biol. Chem. 278 (2003) 3105-3111
44. Schneider D., and Engelman D.M. Motifs of two small residues can assist but are not sufficient to mediate transmembrane helix interactions. J. Mol. Biol. 343 (2004) 799-804
45. Vajo Z., Francomano C.A., and Wilkin D.J. The molecular and genetic basis of fibroblast growth factor receptor 3 disorders: The achondroplasia family of skeletal dysplasias, Muenke craniosynostosis, and Crouzon syndrome with acanthosis nigricans. Endocr. Rev. 21 (2000) 23-39
46. van Rhijin B., van Tilborg A., Lurkin I., Bonaventure J., de Vries A., Thiery J.P., van der Kwast T.H., Zwarthoff E., and Radvanyi F. Novel fibroblast growth factor receptor 3 (FGFR3) mutations in bladder cancer previously identified in non-lethal skeletal disorders. Eur. J. Human Genet. 10 (2002) 819-824
47. Wagner M.L., and Tamm L.K. Tethered polymer-supported planar lipid bilayers for reconstitution of integral membrane proteins: Silane-polyethyleneglycol-lipid as a cushion and covalent linker. Biophys. J. 79 (2000) 1400-1414
48. Wagner M.L., and Tamm L.K. Reconstituted syntaxin 1A/SNAP25 interacts with negatively charged lipids as measured by lateral diffusion in planar supported bilayers. Biophys. J. 81 (2001) 266-275
49. Wallin E., and von Heijne G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 7 (1998) 1029-1038
50. Webster M.K., and Donoghue D.J. Constitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasia. EMBO J. 15 (1996) 520-527
51. Webster M.K., and Donoghue D.J. FGFR activation in skeletal disorders: Too much of a good thing. Trends Genet. 13 (1997) 178-182
52. White S.H., Ladokhin A.S., Jayasinghe S., and Hristova K. How membranes shape protein structure. J. Biol. Chem. 276 (2001) 32395-32398
53. White S.H., and Wimley W.C. Membrane protein folding and stability: physical principles. Annu. Rev. Biophys. Biomol. Struc. 28 (1999) 319-365
54. White S.H., Wimley W.C., Ladokhin A.S., and Hristova K. Protein folding in membranes: Pondering the nature of the bilayer milieu. Biol. Skr. Dan. Selsk. 49 (1998) 91-98
55. You M., Li E., and Hristova K. The achondroplasia mutation does not alter the dimerization energetics of FGFR3 transmembrane domain. Biochemistry 45 (2006) 5551-5556
56. You M., Li E., Wimley W.C., and Hristova K. FRET in liposomes: measurements of TM helix dimerization in the native bilayer environment. Anal. Biochem. 340 (2005) 154-164
57. You M., Spangler J., Li E., Han X., Ghosh P., and Hristova K. Effect of pathogenic cysteine mutations on FGFR3 transmembrane domain dimerization in detergents and lipid bilayers. Biochemistry 46 (2007) 11039-11046