메뉴 건너뛰기




Volumn 2, Issue 99, 2009, Pages

Quantitative analysis of protein-lipid interactions using tryptophan fluorescence

Author keywords

[No Author keywords available]

Indexed keywords

KINASE SUPPRESSOR OF RAS 1; PHOSPHATIDIC ACID; PROTEIN; RAF PROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG; KSR 1 PROTEIN KINASE; KSR-1 PROTEIN KINASE; LIPID; PHOTOPROTEIN; PROTEIN KINASE;

EID: 77950351987     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.299pl4     Document Type: Review
Times cited : (34)

References (28)
  • 1
    • 0000944228 scopus 로고
    • Fluorescence-polarization spectrum and electronic-energy transfer in tyrosine, tryptophan and related compounds
    • G.Weber, Fluorescence-polarization spectrum and electronic-energy transfer in tyrosine, tryptophan and related compounds. Biochem. J. 75, 335-345 (1960).
    • (1960) Biochem. J. , vol.75 , pp. 335-345
    • Weber, G.1
  • 2
    • 0002564671 scopus 로고
    • Fluorescence of some proteins, nucleic acids and related compounds
    • V. G. Shore, A. B. Pardee, Fluorescence of some proteins, nucleic acids and related compounds. Arch. Biochem. Biophys. 60, 100-107 (1956).
    • (1956) Arch. Biochem. Biophys. , vol.60 , pp. 100-107
    • Shore, V.G.1    Pardee, A.B.2
  • 3
    • 70449159833 scopus 로고
    • Ultraviolet fluorescence of the aromatic amino acids
    • F.W. Teale, G.Weber, Ultraviolet fluorescence of the aromatic amino acids. Biochem. J. 65, 476-482 (1957).
    • (1957) Biochem. J. , vol.65 , pp. 476-482
    • Teale, F.W.1    Weber, G.2
  • 4
    • 0001516275 scopus 로고
    • The ultraviolet fluorescence of proteins in neutral solution
    • F.W. Teale, The ultraviolet fluorescence of proteins in neutral solution. Biochem. J. 76, 381-388 (1960).
    • (1960) Biochem. J. , vol.76 , pp. 381-388
    • Teale, F.W.1
  • 5
    • 0001630008 scopus 로고
    • Fluorescence and the structure of proteins. II. Fluorescence of peptides containing tryptophan or tyrosine
    • R.W. Cowgill, Fluorescence and the structure of proteins. II. Fluorescence of peptides containing tryptophan or tyrosine. Biochim. Biophys. Acta 75, 272-273 (1963).
    • (1963) Biochim. Biophys. Acta , vol.75 , pp. 272-273
    • Cowgill, R.W.1
  • 6
    • 0024121613 scopus 로고
    • Principles of frequency-domain fluorescence spectroscopy and applications to cell membranes
    • J. R. Lakowicz, Principles of frequency-domain fluorescence spectroscopy and applications to cell membranes. Subcell. Biochem. 13, 89-126 (1988).
    • (1988) Subcell. Biochem. , vol.13 , pp. 89-126
    • Lakowicz, J.R.1
  • 7
    • 0037279631 scopus 로고    scopus 로고
    • Fluorescence: Basic concepts, practical aspects, and some anecdotes.
    • D. M. Jameson, J. C. Croney, P. D. Moens, Fluorescence: Basic concepts, practical aspects, and some anecdotes. Methods Enzymol. 360, 1-43 (2003).
    • (2003) Methods Enzymol. , vol.360 , pp. 1-43
    • Jameson, D.M.1    Croney, J.C.2    Moens, P.D.3
  • 8
    • 7744240086 scopus 로고    scopus 로고
    • Influence of the lipid composition on the kinetics of concerted insertion and folding of melittin in bilayers
    • I. Constantinescu, M. Lafleur, Influence of the lipid composition on the kinetics of concerted insertion and folding of melittin in bilayers. Biochim. Biophys. Acta 1667, 26-37 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1667 , pp. 26-37
    • Constantinescu, I.1    Lafleur, M.2
  • 9
    • 0036519842 scopus 로고    scopus 로고
    • Site-specific tryptophan fluorescence spectroscopy as a probe of membrane peptide structure and dynamics
    • A. H. A. Clayton, W. H. Sawyer, Site-specific tryptophan fluorescence spectroscopy as a probe of membrane peptide structure and dynamics. Eur. Biophys. J. 31, 9-13 (2002).
    • (2002) Eur. Biophys. J. , vol.31 , pp. 9-13
    • Clayton, A.H.A.1    Sawyer, W.H.2
  • 10
    • 0030738720 scopus 로고    scopus 로고
    • Transmembrane orientation of hydrophobic alpha-helices is regulated both by the relationship of helix length to bilayer thickness and by the cholesterol concentration
    • J. Ren, S. Lew, Z.Wang, E. London, Transmembrane orientation of hydrophobic alpha-helices is regulated both by the relationship of helix length to bilayer thickness and by the cholesterol concentration. Biochemistry 36, 10213-10220 (1997).
    • (1997) Biochemistry , vol.36 , pp. 10213-10220
    • Ren, J.1    Lew, S.2    Wang Z3    London, E.4
  • 11
    • 0037137178 scopus 로고    scopus 로고
    • Determining the membrane topology of proteins: Insertion pathway of a transmembrane helix of annexin 12.
    • A. S. Ladokhin, J. M. Isas, H. T. Haigler, S. H. White, Determining the membrane topology of proteins: Insertion pathway of a transmembrane helix of annexin 12. Biochemistry 41, 13617-13626 (2002).
    • (2002) Biochemistry , vol.41 , pp. 13617-13626
    • Ladokhin, A.S.1    Isas, J.M.2    Haigler, H.T.3    White, S.H.4
  • 12
    • 2442442435 scopus 로고    scopus 로고
    • Interfacial folding and membrane insertion of a designed helical peptide
    • A. S. Ladokhin, S. H. White, Interfacial folding and membrane insertion of a designed helical peptide. Biochemistry 43, 5782-5791 (2004).
    • (2004) Biochemistry , vol.43 , pp. 5782-5791
    • Ladokhin, A.S.1    White, S.H.2
  • 13
    • 0034635171 scopus 로고    scopus 로고
    • Determining the membrane topology of peptides by fluorescence quenching
    • W. C. Wimley, S. H. White, Determining the membrane topology of peptides by fluorescence quenching. Biochemistry 39, 161-170 (2000).
    • (2000) Biochemistry , vol.39 , pp. 161-170
    • Wimley, S.H.1    White, S.H.2
  • 14
    • 0031001049 scopus 로고    scopus 로고
    • Regulation of Raf-1 kinase by interaction with the lipid second messenger, phosphatidic acid
    • S. Ghosh, R. M. Bell, Regulation of Raf-1 kinase by interaction with the lipid second messenger, phosphatidic acid. Biochem. Soc. Trans. 25, 561-565 (1997).
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 561-565
    • Ghosh, S.1    Bell, R.M.2
  • 15
    • 0034604717 scopus 로고    scopus 로고
    • The recruitment of Raf-1 to membranes is mediated by direct interaction with phosphatidic acid and is independent of association with Ras
    • M. A. Rizzo, K. Shome, S. C.Watkins, G. Romero, The recruitment of Raf-1 to membranes is mediated by direct interaction with phosphatidic acid and is independent of association with Ras. J. Biol. Chem. 275, 23911-23918 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 23911-23918
    • Rizzo, M.A.1    Shome, K.2    Watkins, S.C.3    Romero, G.4
  • 17
    • 0037025377 scopus 로고    scopus 로고
    • Associations of B- and C-Raf with cholesterol, phosphatidylserine, and lipid second messengers: Preferential binding of Raf to artificial lipid rafts
    • M. Hekman, H. Hamm, A. V. Villar, B. Bader, J. Kuhlmann, J. Nickel, U. R. Rapp, Associations of B- and C-Raf with cholesterol, phosphatidylserine, and lipid second messengers: Preferential binding of Raf to artificial lipid rafts. J. Biol. Chem. 277, 24090-24102 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 24090-24102
    • Hekman, M.1    Hamm, H.2    Villar, A.V.3    Bader, B.4    Kuhlmann, J.5    Nickel, J.6    Rapp, U.R.7
  • 18
    • 34447568476 scopus 로고    scopus 로고
    • Phospholipase D2-generated phosphatidic acid couples EGFR stimulation to Ras activation by Sos
    • C. Zhao, G. Du, K. Skowronek, M. A. Frohman, D. Bar-Sagi, Phospholipase D2-generated phosphatidic acid couples EGFR stimulation to Ras activation by Sos. Nat. Cell Biol. 9, 707-712 (2007).
    • (2007) Nat. Cell Biol. , vol.9 , pp. 707-712
    • Zhao, C.1    Du, G.2    Skowronek, K.3    Frohman, M.A.4    Bar-Sagi, D.5
  • 20
    • 0033534687 scopus 로고    scopus 로고
    • Phospholipase D and its product, phosphatidic acid, mediate agonist-dependent Raf-1 translocation to the plasma membrane and the activation of the mitogen-activated protein kinase pathway
    • M. A. Rizzo, K. Shome, C. Vasudevan, D. B. Stolz, T. C. Sung, M. A. Frohman, S. C.Watkins, G. Romero, Phospholipase D and its product, phosphatidic acid, mediate agonist-dependent Raf-1 translocation to the plasma membrane and the activation of the mitogen-activated protein kinase pathway. J. Biol. Chem. 274, 1131-1139 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 1131-1139
    • Rizzo, M.A.1    Shome, K.2    Vasudevan, C.3    Stolz, D.B.4    Sung, T.C.5    Frohman, M.A.6    Watkins, S.C.7    Romero, G.8
  • 21
    • 0029935339 scopus 로고    scopus 로고
    • Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid: Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells
    • S. Ghosh, J. C. Strum, V. A. Sciorra, L. Daniel, R. M. Bell, Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid: Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells. J. Biol. Chem. 271, 8472-8480 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 8472-8480
    • Ghosh, S.1    Strum, J.C.2    Sciorra, V.A.3    Daniel, L.4    Bell, R.M.5
  • 22
    • 0242664746 scopus 로고    scopus 로고
    • Functional analysis of a phosphatidic acid binding domain in human Raf-1 kinase: Mutations in the phosphatidate binding domain lead to tail and trunk abnormalities in developing zebrafish embryos
    • S. Ghosh, S. Moore, R. M. Bell, M. Dush, Functional analysis of a phosphatidic acid binding domain in human Raf-1 kinase: Mutations in the phosphatidate binding domain lead to tail and trunk abnormalities in developing zebrafish embryos. J. Biol. Chem. 278, 45690-45696 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 45690-45696
    • Ghosh, S.1    Moore, S.2    Bell, R.M.3    Dush, M.4
  • 23
    • 0030570797 scopus 로고    scopus 로고
    • Dependence of critical micelle concentration of a zwitterionic detergent on ionic strength: Implications in receptor solubilization.
    • A. Chattopadhyay, K. G. Harikumar, Dependence of critical micelle concentration of a zwitterionic detergent on ionic strength: Implications in receptor solubilization. FEBS Lett. 391, 199-202 (1996).
    • (1996) FEBS Lett. , vol.391 , pp. 199-202
    • Chattopadhyay, A.1    Harikumar, K.G.2
  • 24
    • 0023043195 scopus 로고
    • Kinetic and structural aspects of reconstitution of phosphatidylcholine vesicles by dilution of phosphatidylcholine-sodium cholate mixed micelles
    • S. Almog, T. Kushnir, S. Nir, D. Lichtenberg, Kinetic and structural aspects of reconstitution of phosphatidylcholine vesicles by dilution of phosphatidylcholine-sodium cholate mixed micelles. Biochemistry 25, 2597-2605 (1986).
    • (1986) Biochemistry , vol.25 , pp. 2597-2605
    • Almog, S.1    Kushnir, T.2    Nir, S.3    Lichtenberg, D.4
  • 25
    • 34447291808 scopus 로고    scopus 로고
    • Binding of lysozyme to phospholipid bilayers: Evidence for protein aggregation upon membrane association.
    • G. P. Gorbenko, V. M. Ioffe, P. K. Kinnunen, Binding of lysozyme to phospholipid bilayers: Evidence for protein aggregation upon membrane association. Biophys. J. 93, 140-153 (2007).
    • (2007) Biophys. J. , vol.93 , pp. 140-153
    • Gorbenko, G.P.1    Ioffe, V.M.2    Kinnunen, P.K.3
  • 26
    • 0035960561 scopus 로고    scopus 로고
    • Mechanism of the interaction of β2-glycoprotein I with negatively charged phospholipid membranes.
    • M. Hammel, R. Schwarzenbacher, A. Gries, G. M. Kostner, P. Laggner, R. Prassl, Mechanism of the interaction of β2-glycoprotein I with negatively charged phospholipid membranes. Biochemistry 40, 14173-14181 (2001).
    • (2001) Biochemistry , vol.40 , pp. 14173-14181
    • Hammel, M.1    Schwarzenbacher, R.2    Gries, R.3    Kostner, G.M.4    Laggner, P.5    Prassl, R.6
  • 27
    • 77953659587 scopus 로고    scopus 로고
    • Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val;W, Trp; and Y, Tyr.
    • Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val;W, Trp; and Y, Tyr.
  • 28
    • 77953674469 scopus 로고    scopus 로고
    • Funding was from NIH R01 DK54782 (to G.R.) and T32-GM-54812.
    • Funding was from NIH R01 DK54782 (to G.R.) and T32-GM-54812.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.