메뉴 건너뛰기




Volumn 585, Issue 8, 2011, Pages 1163-1168

The binding of 14-3-3γ to membranes studied by intrinsic fluorescence spectroscopy

Author keywords

Acidic liposomes; Cell signalling; Membrane binding; Pi stacking; Quenching; Tryptophan fluorescence

Indexed keywords

LIPOSOME; PROTEIN 14 3 3; PROTEIN 14 3 3 GAMMA; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 79954448500     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.03.027     Document Type: Article
Times cited : (8)

References (26)
  • 1
    • 79953139417 scopus 로고    scopus 로고
    • Quantitative assessment of peptide-lipid interactions. Ubiquitous fluorescence methodologies
    • P.M. Matos, H.G. Franquelim, M.A. Castanho, and N.C. Santos Quantitative assessment of peptide-lipid interactions. Ubiquitous fluorescence methodologies Biochim. Biophys. Acta 1798 2010 1999 2012
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1999-2012
    • Matos, P.M.1    Franquelim, H.G.2    Castanho, M.A.3    Santos, N.C.4
  • 2
    • 34547174917 scopus 로고    scopus 로고
    • Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins
    • DOI 10.1016/j.bbamem.2007.03.015, PII S0005273607000806
    • L.A. Munishkina, and A.L. Fink Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins Biochim. Biophys. Acta 1768 2007 1862 1885 (Pubitemid 47125851)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.8 , pp. 1862-1885
    • Munishkina, L.A.1    Fink, A.L.2
  • 3
    • 0037821763 scopus 로고    scopus 로고
    • The interaction of peripheral proteins and membranes studied with α-lactalbumin and phospholipid bilayers of various compositions
    • DOI 10.1074/jbc.M211466200
    • A.V. Agasøster, Ø. Halskau, E. Fuglebakk, N.A. Frøystein, A. Muga, H. Holmsen, and A. Martínez The interaction of peripheral proteins and membranes studied with a-lactalbumin and phospholipid bilayers of various compositions J. Biol. Chem. 278 2003 21790 21797 (Pubitemid 36792583)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.24 , pp. 21790-21797
    • Varnier Agasoster, A.1    Halskau, O.2    Fuglebakk, E.3    Froystein, N.A.4    Muga, A.5    Holmsen, H.6    Martinez, A.7
  • 4
    • 0029591840 scopus 로고
    • Binding of molten globule-like conformations to lipid bilayers. Structure of native and partially folded a-lactalbumin bound to model membranes
    • S. Banuelos, and A. Muga Binding of molten globule-like conformations to lipid bilayers. Structure of native and partially folded a-lactalbumin bound to model membranes J. Biol. Chem. 270 1995 29910 29915
    • (1995) J. Biol. Chem. , vol.270 , pp. 29910-29915
    • Banuelos, S.1    Muga, A.2
  • 5
    • 17044441821 scopus 로고    scopus 로고
    • Structural and kinetic description of cytochrome c unfolding induced by the interaction with lipid vesicles
    • DOI 10.1021/bi971235z
    • T.J. Pinheiro, G.A. Elove, A. Watts, and H. Roder Structural and kinetic description of cytochrome c unfolding induced by the interaction with lipid vesicles Biochemistry 36 1997 13122 13132 (Pubitemid 27465428)
    • (1997) Biochemistry , vol.36 , Issue.42 , pp. 13122-13132
    • Pinheiro, T.J.T.1    Elove, G.A.2    Watts, A.3    Roder, H.4
  • 8
    • 33646926129 scopus 로고    scopus 로고
    • 14-3-3 proteins: A historic overview
    • DOI 10.1016/j.semcancer.2006.03.005, PII S1044579X06000253
    • A. Aitken 14-3-3 proteins: a historic overview Semin. Cancer Biol. 16 2006 162 172 (Pubitemid 43796128)
    • (2006) Seminars in Cancer Biology , vol.16 , Issue.3 , pp. 162-172
    • Aitken, A.1
  • 10
    • 33745196467 scopus 로고    scopus 로고
    • Reversible membrane interaction of BAD requires two C-terminal lipid binding domains in conjunction with 14-3-3 protein binding
    • M. Hekman Reversible membrane interaction of BAD requires two C-terminal lipid binding domains in conjunction with 14-3-3 protein binding J. Biol. Chem. 281 2006 17321 17336
    • (2006) J. Biol. Chem. , vol.281 , pp. 17321-17336
    • Hekman, M.1
  • 11
    • 64049087382 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of cytosolic localization and oncogenic function of Skp2 by Akt/PKB
    • H.K. Lin Phosphorylation-dependent regulation of cytosolic localization and oncogenic function of Skp2 by Akt/PKB Nat. Cell. Biol. 11 2009 420 432
    • (2009) Nat. Cell. Biol. , vol.11 , pp. 420-432
    • Lin, H.K.1
  • 12
    • 0034528346 scopus 로고    scopus 로고
    • 14-3-3 Proteins: Regulation of subcellular localization by molecular interference
    • DOI 10.1016/S0898-6568(00)00131-5, PII S0898656800001315
    • A.J. Muslin, and H. Xing 14-3-3 proteins: regulation of subcellular localization by molecular interference Cell. Signal. 12 2000 703 709 (Pubitemid 32056337)
    • (2000) Cellular Signalling , vol.12 , Issue.11-12 , pp. 703-709
    • Muslin, A.J.1    Xing, H.2
  • 13
    • 77950467109 scopus 로고    scopus 로고
    • Insulin-stimulated interaction with 14-3-3 promotes cytoplasmic localization of lipin-1 in adipocytes
    • M. Peterfy, T.E. Harris, N. Fujita, and K. Reue Insulin-stimulated interaction with 14-3-3 promotes cytoplasmic localization of lipin-1 in adipocytes J. Biol. Chem. 285 2010 3857 3864
    • (2010) J. Biol. Chem. , vol.285 , pp. 3857-3864
    • Peterfy, M.1    Harris, T.E.2    Fujita, N.3    Reue, K.4
  • 14
    • 0028063607 scopus 로고
    • Subcellular localisation of 14-3-3 isoforms in rat brain using specific antibodies
    • H. Martin, J. Rostas, Y. Patel, and A. Aitken Subcellular localisation of 14-3-3 isoforms in rat brain using specific antibodies J. Neurochem. 63 1994 2259 2265 (Pubitemid 24370003)
    • (1994) Journal of Neurochemistry , vol.63 , Issue.6 , pp. 2259-2265
    • Martin, H.1    Rostas, J.2    Patel, Y.3    Aitken, A.4
  • 15
    • 0028235265 scopus 로고
    • Characterization of 14-3-3 proteins in adrenal chromaffin cells and demonstration of isoform-specific phospholipid binding
    • D. Roth, A. Morgan, H. Martin, D. Jones, G.J. Martens, A. Aitken, and R.D. Burgoyne Characterization of 14-3-3 proteins in adrenal chromaffin cells and demonstration of isoform-specific phospholipid binding Biochem. J. 301 Pt 1 1994 305 310 (Pubitemid 24214715)
    • (1994) Biochemical Journal , vol.301 , Issue.1 , pp. 305-310
    • Roth, D.1    Morgan, A.2    Martin, H.3    Jones, D.4    Martens, G.J.M.5    Aitken, A.6    Burgoyne, R.D.7
  • 16
    • 0028962533 scopus 로고
    • Expression and structural analysis of 14-3-3 proteins
    • D.H. Jones Expression and structural analysis of 14-3-3 proteins J. Mol. Biol. 245 1995 375 384
    • (1995) J. Mol. Biol. , vol.245 , pp. 375-384
    • Jones, D.H.1
  • 18
    • 70450245195 scopus 로고    scopus 로고
    • Three-way interaction between 14-3-3 proteins, the N-terminal region of tyrosine hydroxylase, and negatively charged membranes
    • Ø. Halskau Jr., M. Ying, A. Baumann, R. Kleppe, D. Rodriguez-Larrea, B. Almas, J. Haavik, and A. Martinez Three-way interaction between 14-3-3 proteins, the N-terminal region of tyrosine hydroxylase, and negatively charged membranes J. Biol. Chem. 284 2009 32758 32769
    • (2009) J. Biol. Chem. , vol.284 , pp. 32758-32769
    • Halskau Jr., Ø.1    Ying, M.2    Baumann, A.3    Kleppe, R.4    Rodriguez-Larrea, D.5    Almas, B.6    Haavik, J.7    Martinez, A.8
  • 19
    • 0029850169 scopus 로고    scopus 로고
    • Log-normal description of fluorescence spectra of organic fluorophores
    • E.A. Burstein, and V.I. Emelyanenko Log-normal description of fluorescence spectra of organic fluorophores Photochem. Photobiol. 64 1996 316 320 (Pubitemid 26351257)
    • (1996) Photochemistry and Photobiology , vol.64 , Issue.2 , pp. 316-320
    • Burstein, E.A.1    Emelyanenko, V.I.2
  • 21
    • 0025741701 scopus 로고
    • Fluorescence spectrum of barnase: Contributions of three tryptophan residues and a histidine-related pH dependence
    • R. Loewenthal, J. Sancho, and A.R. Fersht Fluorescence spectrum of barnase: contributions of three tryptophan residues and a histidine-related pH dependence Biochemistry 30 1991 6775 6779
    • (1991) Biochemistry , vol.30 , pp. 6775-6779
    • Loewenthal, R.1    Sancho, J.2    Fersht, A.R.3
  • 22
    • 34548846644 scopus 로고    scopus 로고
    • Ab initio prediction of tryptophan fluorescence quenching by protein electric field enabled electron transfer
    • DOI 10.1021/jp0744883
    • P.R. Callis, A. Petrenko, P.L. Muino, and J.R. Tusell Ab initio prediction of tryptophan fluorescence quenching by protein electric field enabled electron transfer J. Phys. Chem. B 111 2007 10335 10339 (Pubitemid 47447594)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.35 , pp. 10335-10339
    • Callis, P.R.1    Petrenko, A.2    Muino, P.L.3    Tusell, J.R.4
  • 23
  • 25
    • 0037067706 scopus 로고    scopus 로고
    • Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence
    • DOI 10.1074/jbc.M203186200
    • H. Zhao, and P.K. Kinnunen Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence J. Biol. Chem. 277 2002 25170 25177 (Pubitemid 34951823)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25170-25177
    • Zhao, H.1    Kinnunen, P.K.J.2
  • 26
    • 79954432010 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System
    • Schrodinger, L.L.C. (2010) The PyMOL Molecular Graphics System, Version 1.3r1.
    • (2010) Version 1.3r1
    • Schrodinger, L.L.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.