Adsorption of GST-PI3Kγ at the air-buffer interface and at substrate and nonsubstrate phospholipid monolayers

Biophysical Journal

Volumn 96, Issue 3, 2009, Pages 1016-1025

  Hermelink, Antje ^a   Kirsch, Cornelia ^b   Klinger, Reinhard ^b   Reiter, Gerald ^a   Brezesinski, Gerald ^a  

^a MAX PLANCK INSTITUTE OF COLLOIDS AND INTERFACES   (Germany)

^b FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMPHOLYTE; ANION; BUFFER; GLUTATHIONE TRANSFERASE; INOSITOL; PHOSPHATE; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOLIPID; WATER; ARACHIDONIC ACID; ISOENZYME; PHOSPHATIDYLINOSITOL 3 KINASE GAMMA; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PHOSPHATIDYLINOSITOL 3,4,5-TRIPHOSPHATE; PHOSPHATIDYLINOSITOL 3-KINASE GAMMA; POLYPHOSPHOINOSITIDE;

ABSORPTION SPECTROSCOPY; ADSORPTION; ARTICLE; BINDING AFFINITY; COMPRESSION; DESORPTION; ENZYME SUBSTRATE COMPLEX; INFLAMMATION; INFRARED REFLECTION ABSORPTION SPECTROSCOPY; IONIZATION; PROTEIN LIPID INTERACTION; SECOND MESSENGER; ABSORPTION; AIR; ANIMAL; CELL LINE; CHEMISTRY; HEART CONTRACTION; HYDROPHOBICITY; INFRARED SPECTROPHOTOMETRY; METABOLISM; PROTEIN SECONDARY STRUCTURE; SIGNAL TRANSDUCTION;

1-PHOSPHATIDYLINOSITOL 3-KINASE; ABSORPTION; ADSORPTION; AIR; ANIMALS; ARACHIDONIC ACID; BUFFERS; CELL LINE; GLUTATHIONE TRANSFERASE; HYDROPHOBICITY; ISOENZYMES; MYOCARDIAL CONTRACTION; PHOSPHATIDYLINOSITOL PHOSPHATES; PHOSPHOLIPIDS; PROTEIN STRUCTURE, SECONDARY; SIGNAL TRANSDUCTION; SPECTROPHOTOMETRY, INFRARED;

EID: 61549100917     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2008.10.032     Document Type: Article

References (48)

1. Martin, T. F. J. 1998. Phosphoinositide lipids as signaling molecules: common themes for signal transduction, cytoskeletal regulation, and membrane trafficking. Annu. Rev. Cell Dev. Biol. 14:231-264.
2. Rameh, L. E., and L. C. Cantley. 1999. The role of phosphoinositide 3-kinase lipid products in cell function. J. Biol. Chem. 274:8347-8350.
3. Toker, A. 2002. Phosphoinositides and signal transduction. Cell. Mol. Life Sci. 59:761-779.
4. Vanhaesebroeck, B., K. Higashi, C. Raven, M. Welham, S. Anderson, et al. 1999. Autophosphorylation of p1105δ phosphoinositide 3-kinase: a new paradigm for the regulation of lipid kinases in vitro and in vivo. EMBO J. 18:1292-1302.
5. Vanhaesebroeck, B., G. E. Jones, W. E. Allen, D. Zicha, R. Hoosh- mand-Rad, et al. 1999. Distinct PI(3)Ks mediate mitogenic signalling and cell migration in macrophages. Nat. Cell Biol. 1:69-71.
6. Vanhaesebroeck, B., and M. D. Waterfield. 1999. Signaling by distinct classes of phosphoinositide 3-kinases. Exp. Cell Res. 253:239-254.
7. Wymann, M. P., and L. Pirola. 1998. Structure and function of phos- phoinositide 3-kinases. Biochim. Biophys. Acta. 1436:127-150.
8. Stephens, L., A. Smrcka, F. T. Cooke, T. R. Jackson, P. C. Sternweis, et al. 1994. A novel phosphoinositide 3 kinase activity in myeloid- derived cells is activated by G protein βγ subunits. Cell. 77:83-93.
9. Ma, A. D., A. Metjian, S. Bagrodia, S. Taylor, and C. S. Abrams. 1998. Cytoskeletal reorganization by G protein-coupled receptors is dependent on phosphoinositide 3-kinase γ, a Rac guanosine exchange factor, and Rac. Mol. Cell Biol. 18:4744-1751.
10. Murga, C., L. Laguinge, R. Wetzker, A. Cuadrado, and J. S. Gutkind. 1998. Activation of Akt/protein kinase B by G protein-coupled receptors. A role for α and βγ subunits of heterotrimeric G proteins acting through phosphatidylinositol-3-OH kinase γ. J. Biol. Chem. 273: 19080-19085.
11. Stoyanova, S., G. Bulgarelli-Leva, C. Kirsch, T. Hanck, R. Klinger, et al. 1997. Lipid kinase and protein kinase activities of G-protein-coupled phosphoinositide 3-kinase γ: structure-activity analysis and interactions with wortmannin. Biochem. J. 324:489-495.
12. Perrino, C., S. V. N. Prasad, J. N. Schroder, J. A. Hata, C. Milano, et al. 2005. Restoration of β-adrenergic receptor signaling and contractile function in heart failure by disruption of the βARK1/phosphoinositide 3-kinase complex. Circulation. 111:2579-2587.
13. Patrucco, E., A. Notte, L. Barberis, G. Selvetella, A. Maffei, et al. 2004. PI3Kg modulates the cardiac response to chronic pressure overload by distinct kinase-dependent and -independent effects. Cell. 118: 375-387.
14. Kirsch, C., R. Wetzker, and R. Klinger. 2001. Anionic phospholipids are involved in membrane targeting of PI 3-kinase γ. Biochem. Biophys. Res. Commun. 282:691-696.
15. Hirsch, E., V. L. Katanaev, C. Garlanda, O. Azzolino, L. Pirola, et al. 2000. Central role for G protein-coupled phosphoinositide 3-kinase g in inflammation. Science. 287:1049-1053.
16. Sasaki, T., J. Irie-Sasaki, R. G. Jones, A. J. Oliveira-dos-Santos, W. L. Stanford, et al. 2000. Function of PI3Kγ in thymocyte development, T cell activation, and neutrophil migration. Science. 287:1040-1046.
17. Suire, S., W. J. Coadwell, G. J. Ferguson, K. Davidson, P. T. Hawkins, et al. 2005. P84, a new Gbg-activated regulatory subunit of the type IB phosphoinositide 3-kinase p110g. Curr. Biol. 15:566-570.
18. Brock, C., M. Schaefer, H. P. Reusch, C. Czupalla, M. Michalke, et al. 2003. Roles of Gβγ in membrane recruitment and activation of p110γ/ p101 phosphoinositide 3-kinase γ. J. Cell Biol. 160:89-99.
19. Feng, S. S. 1999. 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. 15:998-1010.
20. Dluhy, R. A. 1986. Quantitative external reflection infrared spectro-scopic analysis of insoluble monolayers spread at the air-water interface. J. Phys. Chem. 90:1373-1379.
21. Dluhy, R. A., and D. G. Cornell. 1985. In situ measurement of the infrared spectra of insoluble monolayers at the air-water interface. J. Phys. Chem. 89:3195-3197.
22. Dluhy, R. A., M. L. Mitchell, T. Pettenski, and J. Beers. 1988. Design and interfacing of an automated Langmuir-type film balance to an FT-IR Spectrometer. Appl. Spectrosc. 42:1289-1293.
23. Mendelsohn, R., J. W. Brauner, and A. Gericke. 1995. External infrared reflection absorption spectrometry of monolayer films at the air-water interface. Annu. Rev. Phys. Chem. 46:305-334.
24. Cabiaux, V., B. Agerberth, J. Johansson, F. Homble, E. Goormaghtigh, et al. 1994. Secondary structure and membrane interaction of PR-39, a Pro+Arg-rich antibacterial peptide. Eur. J. Biochem. 224:1019-1027.
25. 4K, a therapeutic agent for respiratory distress syndrome, in aqueous mono-layers with phospholipids. Biochemistry. 42:9446-9452.
26. Zhou, Y., L. Fang, D. Du, W. Zhou, X. Feng, et al. 2008. Proteome identification of binding-partners interacting with cell polarity protein Par3 in Jurkat cells. Acta Biochim. Biophys. Sin. (Shanghai). 40:729-739.
27. Phi, Q. T., Y. M. Park, C. M. Ryu, S. H. Park, and S. Y. Ghim. 2008. Functional identification and expression of indole-3-pyruvate decarbox-ylase from Paenibacillus polymyxa E681. J. Microbiol. Biotechnol. 18:1235-1244.
28. Tan, F., L. Lu, Y. Cai, J. Wang, Y. Xie, et al. 2008. Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells. Proteomics. 8:2885-2896.
29. Trudel, E., S. Beaufils, A. Renault, R. Breton, and C. Salesse. 2006. Binding of RPE65 fragments to lipid monolayers and identification of its partners by glutathione STransferase pull-down assays. Biochemistry. 45:3337-3347.
30. Walker, E. H., O. Perisic, C. Ried, L. Stephens, and R. L. Williams. 1999. Structural insights into phosphoinositide 3-kinase catalysis and signalling. Nature. 402:313-320.
31. Maltseva, E., A. Kerth, A. Blume, H. Mohwald, and G. Brezesinski. 2005. Adsorption of amyloid b (1-40) peptide at phospholipid mono- layers. Chem. Bio. Chem. 6:1817-1824.
32. Chirgadze, Y. N., and N. A. Nevskaya. 1976. Infrared spectra and resonance interaction of amide-I vibration of the antiparallel-chain pleated sheet. Biopolymers. 15:607-625.
33. Macphail, R. A., H. L. Strauss, R. G. Snyder, and C. A. Elliger. 1984. C-H stretching modes and the structure of n-alkyl chains. 2. Long, all-trans chains. J. Phys. Chem. 88:334-341.
34. Snyder, R. G., H. L. Strauss, and C. A. Elliger. 1982. C-H stretching modes and the structure of n-alkyl chains. 1. Long, disordered chains. J. Phys. Chem. 86:5145-5150.
35. Galla, H. J., and E. Sackmann. 1975. Chemically induced lipid phase separation in model membranes containing charged lipids: a spin label study. Biochim. Biophys. Acta. 401:509-529.
36. Galla, H. J., and E. Sackmann. 1975. Chemically induced phase separation in mixed vesicles containing phosphatidic acid. An Optical Study. J. Am. Chem. Soc. 97:4114-4120.
37. Träuble, H., and H. Eibl. 1974. Electrostatic effects on lipid phase transitions: membrane structure and ionic environment. Proc. Natl. Acad. Sci. USA. 71:214-219.
38. Tamm, L. K., and S. A. Tatulian. 1997. Infrared spectroscopy of proteins and peptides in lipid bilayers. Q. Rev. Biophys. 30:365-429.
39. Thomas, L. C., and R. A. Chittenden. 1970. Characteristic infrared absorption frequencies of organophosphorus compounds-VII. Phosphorus ions. Spectrochim. Acta. [A]. 26:781-800.
40. Casal, H. L., U. Kohler, H. H. Mantsch, F. M. Goni, and J. L. R. Arrondo. 1987. Conformational changes in proteins induced by low- temperatures: an infrared study. Z. Naturforsch. [C]. 42:1339-1342.
41. 2+ on phosphatidylser- ines. Biochim. Biophys. Acta. 919:275-286.
42. 2+. Biochemistry. 26:7395-7401.
43. Klähn, M., G. Mathias, C. Kötting, M. Nonella, J. Schlitter, et al. 2004. IR Spectra of phosphate ions in aqueous solution: predictions of a DFT/MM approach compared with observations. J. Phys. Chem. A. 108:6186-6194.
44. Laroche, G., E. J. Dufourc, J. Dufourcq, and M. Pezolet. 1991. Structure and dynamics of dimyristoylphosphatidic acid/calcium complexes by 2H NMR, infrared, and Raman spectroscopies and small-angle X-ray diffraction. Biochemistry. 30:3105-3114.
45. Antipina, M. N., B. Dobner, O. V. Konovalov, V. L. Shapovalov, and G. Brezesinski. 2007. Investigation of the protonation state of novel cationic lipids designed for gene transfection. J. Phys. Chem. B. 111:13845-13850.
46. a in phosphorylated compounds. J. Phys. Chem. A. 111:3602-3612.
47. Buffeteau, T., E. Le Calvez, S. Castano, B. Desbat, D. Blaudez, et al. 2000. Anisotropic optical constants of α-helix and β-sheet secondary structures in the infrared. J. Phys. Chem. B. 104:4537-4544.
48. Goormaghtigh, E., V. Cabiaux, and J.-M. Ruysschaert. 1994. Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary Structures. In Physicochemical Methods in the Study of Biomembranes. H.J. Hilderson and G.B. Ralston, editors. In Subcellular Biochemistry, Vol. 23. Plenum Press, New York. 405-450.