메뉴 건너뛰기




Volumn 290, Issue 2, 2015, Pages 744-754

Structural features of membrane-bound glucocerebrosidase and α-synuclein probed by neutron reflectometry and fluorescence spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; DISEASES; ENZYMES; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; LIPID BILAYERS; MEMBRANES; NEUTRON REFLECTION; NEUTRON SCATTERING; PROTEINS; REFLECTION; REFLECTOMETERS; SURFACE PLASMON RESONANCE;

EID: 84920913800     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.610584     Document Type: Article
Times cited : (41)

References (59)
  • 4
    • 84855444970 scopus 로고    scopus 로고
    • Biophysics of α-synuclein membrane interactions
    • Pfefferkorn, C. M., Jiang, Z., and Lee, J. C. (2012) Biophysics of α-synuclein membrane interactions. Biochim. Biophys. Acta 1818, 162-171
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 162-171
    • Pfefferkorn, C.M.1    Jiang, Z.2    Lee, J.C.3
  • 5
    • 84871414210 scopus 로고    scopus 로고
    • The many faces of α-synuclein: From structure and toxicity to therapeutic target
    • Lashuel, H. A., Overk, C. R., Oueslati, A., and Masliah, E. (2013) The many faces of α-synuclein: from structure and toxicity to therapeutic target. Nat. Rev. Neurosci. 14, 38-48
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 38-48
    • Lashuel, H.A.1    Overk, C.R.2    Oueslati, A.3    Masliah, E.4
  • 6
    • 78149410222 scopus 로고    scopus 로고
    • Glucocerebrosidase is present in α-synuclein inclusions in Lewy body disorders
    • Goker-Alpan, O., Stubblefield, B. K., Giasson, B. I., and Sidransky, E. (2010) Glucocerebrosidase is present in α-synuclein inclusions in Lewy body disorders. Acta Neuropathol. 120, 641-649
    • (2010) Acta Neuropathol. , vol.120 , pp. 641-649
    • Goker-Alpan, O.1    Stubblefield, B.K.2    Giasson, B.I.3    Sidransky, E.4
  • 9
    • 84867616698 scopus 로고    scopus 로고
    • The link between the GBA gene and parkinsonism
    • Sidransky, E., and Lopez, G. (2012) The link between the GBA gene and parkinsonism. Lancet Neurol. 11, 986-998
    • (2012) Lancet Neurol. , vol.11 , pp. 986-998
    • Sidransky, E.1    Lopez, G.2
  • 12
    • 84887948427 scopus 로고    scopus 로고
    • Emerging insights into the mechanistic link between α-synuclein and glucocerebrosidase in Parkinson's disease
    • McGlinchey, R. P., and Lee, J. C. (2013) Emerging insights into the mechanistic link between α-synuclein and glucocerebrosidase in Parkinson's disease. Biochem. Soc. Trans. 41, 1509-1512
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 1509-1512
    • McGlinchey, R.P.1    Lee, J.C.2
  • 13
    • 0015154711 scopus 로고
    • Gaucher's disease: Deficiency of "acid" β-glucosidase and reconstitution of enzyme activity in vitro
    • Ho, M. W., and O'Brien, J. S. (1971) Gaucher's disease: deficiency of "acid" β-glucosidase and reconstitution of enzyme activity in vitro. Proc. Natl. Acad. Sci. U.S.A. 68, 2810-2813
    • (1971) Proc. Natl. Acad. Sci. U.S.A. , vol.68 , pp. 2810-2813
    • Ho, M.W.1    O'Brien, J.S.2
  • 14
    • 25444443570 scopus 로고    scopus 로고
    • Principles of lysosomal membrane digestion: Stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids
    • Kolter, T., and Sandhoff, K. (2005) Principles of lysosomal membrane digestion: stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids. Annu. Rev. Cell Dev. Biol. 21, 81-103
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 81-103
    • Kolter, T.1    Sandhoff, K.2
  • 16
    • 0027494660 scopus 로고
    • Function of saposin C in the reconstitution of glucosylceramidase by phosphatidylserine liposomes
    • Vaccaro, A. M., Tatti, M., Ciaffoni, F., Salvioli, R., Maras, B., and Barca, A. (1993) Function of saposin C in the reconstitution of glucosylceramidase by phosphatidylserine liposomes. FEBS Lett. 336, 159-162
    • (1993) FEBS Lett. , vol.336 , pp. 159-162
    • Vaccaro, A.M.1    Tatti, M.2    Ciaffoni, F.3    Salvioli, R.4    Maras, B.5    Barca, A.6
  • 17
    • 0032514902 scopus 로고    scopus 로고
    • Lysosomal degradation on vesicular membrane surfaces: Enhanced glucosylceramide degradation by lysosomal anionic lipids and activators
    • Wilkening, G., Linke, T., and Sandhoff, K. (1998) Lysosomal degradation on vesicular membrane surfaces: enhanced glucosylceramide degradation by lysosomal anionic lipids and activators. J. Biol. Chem. 273, 30271-30278
    • (1998) J. Biol. Chem. , vol.273 , pp. 30271-30278
    • Wilkening, G.1    Linke, T.2    Sandhoff, K.3
  • 18
    • 79959925894 scopus 로고    scopus 로고
    • α-Synuclein interacts with glucocerebrosidase providing a molecular link between Parkinson and Gaucher diseases
    • Yap, T. L., Gruschus, J. M., Velayati, A., Westbroek, W., Goldin, E., Moaven, N., Sidransky, E., and Lee, J. C. (2011) α-Synuclein interacts with glucocerebrosidase providing a molecular link between Parkinson and Gaucher diseases. J. Biol. Chem. 286, 28080-28088
    • (2011) J. Biol. Chem. , vol.286 , pp. 28080-28088
    • Yap, T.L.1    Gruschus, J.M.2    Velayati, A.3    Westbroek, W.4    Goldin, E.5    Moaven, N.6    Sidransky, E.7    Lee, J.C.8
  • 19
    • 84871720426 scopus 로고    scopus 로고
    • Membranebound α-synuclein interacts with glucocerebrosidase and inhibits enzyme activity
    • Yap, T. L., Velayati, A., Sidransky, E., and Lee, J. C. (2013) Membranebound α-synuclein interacts with glucocerebrosidase and inhibits enzyme activity. Mol. Genet. Metab. 108, 56-64
    • (2013) Mol. Genet. Metab. , vol.108 , pp. 56-64
    • Yap, T.L.1    Velayati, A.2    Sidransky, E.3    Lee, J.C.4
  • 21
    • 84879606955 scopus 로고    scopus 로고
    • α-Synuclein and protein degradation systems: A reciprocal relationship
    • Xilouri, M., Brekk, O. R., and Stefanis, L. (2013) α-Synuclein and protein degradation systems: a reciprocal relationship. Mol. Neurobiol. 47, 537-551
    • (2013) Mol. Neurobiol. , vol.47 , pp. 537-551
    • Xilouri, M.1    Brekk, O.R.2    Stefanis, L.3
  • 22
    • 84886020944 scopus 로고    scopus 로고
    • Saposin C protects glucocerebrosidase against α-synuclein inhibition
    • Yap, T. L., Gruschus, J. M., Velayati, A., Sidransky, E., and Lee, J. C. (2013) Saposin C protects glucocerebrosidase against α-synuclein inhibition. Biochemistry 52, 7161-7163
    • (2013) Biochemistry , vol.52 , pp. 7161-7163
    • Yap, T.L.1    Gruschus, J.M.2    Velayati, A.3    Sidransky, E.4    Lee, J.C.5
  • 25
    • 84856599940 scopus 로고    scopus 로고
    • Guided tour of the structural biology of Gaucher disease: Acid-β-glucosidase and saposin c
    • Lieberman, R. L. A. (2011) Guided tour of the structural biology of Gaucher disease: acid-β-glucosidase and saposin c. Enzyme Res. 2011, 973231
    • (2011) Enzyme Res. , vol.2011 , pp. 973231
    • Lieberman, R.L.A.1
  • 28
    • 84903789702 scopus 로고    scopus 로고
    • Zooming in on disordered systems: Neutron reflection studies of proteins associated with fluid membranes
    • Heinrich, F., and Lösche, M. (2014) Zooming in on disordered systems: neutron reflection studies of proteins associated with fluid membranes. Biochim. Biophys. Acta 1838, 2341-2349
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 2341-2349
    • Heinrich, F.1    Lösche, M.2
  • 29
    • 84881046157 scopus 로고    scopus 로고
    • Examining protein-lipid complexes using neutron scattering
    • Clifton, L. A., Neylon, C., and Lakey, J. H. (2013) Examining protein-lipid complexes using neutron scattering. Methods Mol. Biol. 974, 119-150
    • (2013) Methods Mol. Biol. , vol.974 , pp. 119-150
    • Clifton, L.A.1    Neylon, C.2    Lakey, J.H.3
  • 30
    • 84859593968 scopus 로고    scopus 로고
    • Membrane association of the PTEN tumor suppressor: Molecular details of the protein-membrane complex from SPR binding studies and neutron reflection
    • Shenoy, S., Shekhar, P., Heinrich, F., Daou, M. C., Gericke, A., Ross, A. H., and Lösche, M. (2012) Membrane association of the PTEN tumor suppressor: molecular details of the protein-membrane complex from SPR binding studies and neutron reflection. PLoS One 7, e32591
    • (2012) PLoS One , vol.7 , pp. e32591
    • Shenoy, S.1    Shekhar, P.2    Heinrich, F.3    Daou, M.C.4    Gericke, A.5    Ross, A.H.6    Lösche, M.7
  • 31
    • 84898070947 scopus 로고    scopus 로고
    • Myristoylation restricts orientation of the GRASP domain on membranes and promotes membrane tethering
    • Heinrich, F., Nanda, H., Goh, H. Z., Bachert, C., Lösche, M., and Linstedt, A. D. (2014) Myristoylation restricts orientation of the GRASP domain on membranes and promotes membrane tethering. J. Biol. Chem. 289, 9683-9691
    • (2014) J. Biol. Chem. , vol.289 , pp. 9683-9691
    • Heinrich, F.1    Nanda, H.2    Goh, H.Z.3    Bachert, C.4    Lösche, M.5    Linstedt, A.D.6
  • 33
    • 78049231897 scopus 로고    scopus 로고
    • Electrostatic interactions and binding orientation of HIV-1 matrix studied by neutron reflectivity
    • Nanda, H., Datta, S. A. K., Heinrich, F., Lösche, M., Rein, A., Krueger, S., and Curtis, J. E. (2010) Electrostatic interactions and binding orientation of HIV-1 matrix studied by neutron reflectivity. Biophys. J. 99, 2516-2524
    • (2010) Biophys. J. , vol.99 , pp. 2516-2524
    • Nanda, H.1    Datta, S.A.K.2    Heinrich, F.3    Lösche, M.4    Rein, A.5    Krueger, S.6    Curtis, J.E.7
  • 34
    • 84863012541 scopus 로고    scopus 로고
    • Depth of α-synuclein in a bilayer determined by fluorescence, neutron reflectometry, and computation
    • Pfefferkorn, C. M., Heinrich, F., Sodt, A. J., Maltsev, A. S., Pastor, R. W., and Lee, J. C. (2012) Depth of α-synuclein in a bilayer determined by fluorescence, neutron reflectometry, and computation. Biophys. J. 102, 613-621
    • (2012) Biophys. J. , vol.102 , pp. 613-621
    • Pfefferkorn, C.M.1    Heinrich, F.2    Sodt, A.J.3    Maltsev, A.S.4    Pastor, R.W.5    Lee, J.C.6
  • 36
    • 84892410771 scopus 로고    scopus 로고
    • Investigating the interactions of the 18 kDa translocator protein and its ligand PK11195 in planar lipid bilayers
    • Hatty, C. R., Le Brun, A. P., Lake, V., Clifton, L. A., Liu, G. J., James, M., and Banati, R. B. (2014) Investigating the interactions of the 18 kDa translocator protein and its ligand PK11195 in planar lipid bilayers. Biochim. Biophys. Acta 1838, 1019-1030
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 1019-1030
    • Hatty, C.R.1    Le Brun, A.P.2    Lake, V.3    Clifton, L.A.4    Liu, G.J.5    James, M.6    Banati, R.B.7
  • 38
    • 84887035378 scopus 로고    scopus 로고
    • Membrane remodeling by α-synuclein and effects on amyloid formation
    • Jiang, Z., de Messieres, M., and Lee, J. C. (2013) Membrane remodeling by α-synuclein and effects on amyloid formation. J. Am. Chem. Soc. 135, 15970-15973
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 15970-15973
    • Jiang, Z.1    De Messieres, M.2    Lee, J.C.3
  • 39
    • 3042841923 scopus 로고    scopus 로고
    • Uniform and residue-specific N-15-labeling of proteins on a highly deuterated background
    • Fiaux, J., Bertelsen, E. B., Horwich, A. L., and Wüthrich, K. (2004) Uniform and residue-specific N-15-labeling of proteins on a highly deuterated background. J. Biomol. NMR 29, 289-297
    • (2004) J. Biomol. NMR , vol.29 , pp. 289-297
    • Fiaux, J.1    Bertelsen, E.B.2    Horwich, A.L.3    Wüthrich, K.4
  • 40
    • 77950559887 scopus 로고    scopus 로고
    • Tryptophan probes at the α-synuclein and membrane interface
    • Pfefferkorn, C. M., and Lee, J. C. (2010) Tryptophan probes at the α-synuclein and membrane interface. J. Phys. Chem. B 114, 4615-4622
    • (2010) J. Phys. Chem. B , vol.114 , pp. 4615-4622
    • Pfefferkorn, C.M.1    Lee, J.C.2
  • 43
    • 0033032331 scopus 로고    scopus 로고
    • Analysis of protein and peptide penetration into membranes by depth-dependent fluorescence quenching: Theoretical considerations
    • Ladokhin, A. S. (1999) Analysis of protein and peptide penetration into membranes by depth-dependent fluorescence quenching: theoretical considerations. Biophys. J. 76, 946-955
    • (1999) Biophys. J. , vol.76 , pp. 946-955
    • Ladokhin, A.S.1
  • 44
    • 0027001134 scopus 로고
    • Subsurface profile refinement for neutron specular reflectivity
    • Ankner, J. F., and Majkrzak, C. F. (1992) Subsurface profile refinement for neutron specular reflectivity. Proc. SPIE 10.1117/12.130637
    • (1992) Proc. SPIE
    • Ankner, J.F.1    Majkrzak, C.F.2
  • 45
    • 83055162367 scopus 로고    scopus 로고
    • Continuous distribution model for the investigation of complex molecular architectures near interfaces with scattering techniques
    • 12
    • Shekhar, P., Nanda, H., Lösche, M., and Heinrich, F. (2011) Continuous distribution model for the investigation of complex molecular architectures near interfaces with scattering techniques. J. Appl. Phys. 110, 102216-102216-12
    • (2011) J. Appl. Phys. , vol.110 , pp. 102216-102216
    • Shekhar, P.1    Nanda, H.2    Lösche, M.3    Heinrich, F.4
  • 46
    • 0042354624 scopus 로고    scopus 로고
    • X-ray structure of human acid-β-glucosidase, the defective enzyme in Gaucher disease
    • Dvir, H., Harel, M., McCarthy, A. A., Toker, L., Silman, I., Futerman, A. H., and Sussman, J. L. (2003) X-ray structure of human acid-β-glucosidase, the defective enzyme in Gaucher disease. EMBO Rep. 4, 704-709
    • (2003) EMBO Rep. , vol.4 , pp. 704-709
    • Dvir, H.1    Harel, M.2    McCarthy, A.A.3    Toker, L.4    Silman, I.5    Futerman, A.H.6    Sussman, J.L.7
  • 50
  • 51
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human α-synuclein
    • Ulmer, T. S., Bax, A., Cole, N. B., and Nussbaum, R. L. (2005) Structure and dynamics of micelle-bound human α-synuclein. J. Biol. Chem. 280, 9595-9603
    • (2005) J. Biol. Chem. , vol.280 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 52
    • 0023111150 scopus 로고
    • Determination of the depth of bromine atoms in bilayers formed from bromolipid probes
    • McIntosh, T. J., and Holloway, P. W. (1987) Determination of the depth of bromine atoms in bilayers formed from bromolipid probes. Biochemistry 26, 1783-1788
    • (1987) Biochemistry , vol.26 , pp. 1783-1788
    • McIntosh, T.J.1    Holloway, P.W.2
  • 53
    • 0032544195 scopus 로고    scopus 로고
    • Acid β-glucosidase: Intrinsic fluorescence and conformational changes induced by phospholipids and saposin c
    • Qi, X., and Grabowski, G. A. (1998) Acid β-glucosidase: intrinsic fluorescence and conformational changes induced by phospholipids and saposin c. Biochemistry 37, 11544-11554
    • (1998) Biochemistry , vol.37 , pp. 11544-11554
    • Qi, X.1    Grabowski, G.A.2
  • 54
    • 33845490892 scopus 로고    scopus 로고
    • Structural comparison of differently glycosylated forms of acid-β-glucosidase, the defective enzyme in Gaucher disease
    • Brumshtein, B., Wormald, M. R., Silman, I., Futerman, A. H., and Sussman, J. L. (2006) Structural comparison of differently glycosylated forms of acid-β-glucosidase, the defective enzyme in Gaucher disease. Acta Crystallogr. D Biol. Crystallogr. 62, 1458-1465
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 1458-1465
    • Brumshtein, B.1    Wormald, M.R.2    Silman, I.3    Futerman, A.H.4    Sussman, J.L.5
  • 55
    • 38549097709 scopus 로고    scopus 로고
    • An evolutionary and structure-based docking model for glucocerebrosidase-saposin C and glucocerebrosidasesubstrate interactions: Relevance for Gaucher disease
    • Atrian, S., López-Viñas, E., Gómez-Puertas, P., Chabás, A., Vilageliu, L., and Grinberg, D. (2008) An evolutionary and structure-based docking model for glucocerebrosidase-saposin C and glucocerebrosidasesubstrate interactions: relevance for Gaucher disease. Proteins 70, 882-891
    • (2008) Proteins , vol.70 , pp. 882-891
    • Atrian, S.1    López-Viñas, E.2    Gómez-Puertas, P.3    Chabás, A.4    Vilageliu, L.5    Grinberg, D.6
  • 56
    • 36849049619 scopus 로고    scopus 로고
    • Molecular imaging of membrane interfaces reveals mode of β-glucosidase activation by saposin C
    • Alattia, J. R., Shaw, J. E., Yip, C. M., and Privé, G. G. (2007) Molecular imaging of membrane interfaces reveals mode of β-glucosidase activation by saposin C. Proc. Natl. Acad. Sci. U.S.A. 104, 17394-17399
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 17394-17399
    • Alattia, J.R.1    Shaw, J.E.2    Yip, C.M.3    Privé, G.G.4
  • 57
    • 67649380327 scopus 로고    scopus 로고
    • Multiple tight phospho-lipid-binding modes of α-synuclein revealed by solution NMR spectroscopy
    • Bodner, C. R., Dobson, C. M., and Bax, A. (2009) Multiple tight phospho-lipid-binding modes of α-synuclein revealed by solution NMR spectroscopy. J. Mol. Biol. 390, 775-790
    • (2009) J. Mol. Biol. , vol.390 , pp. 775-790
    • Bodner, C.R.1    Dobson, C.M.2    Bax, A.3
  • 59
    • 77958482255 scopus 로고    scopus 로고
    • The N-terminus of the intrinsically disordered protein α-synuclein triggers membrane binding and helix folding
    • Bartels, T., Ahlstrom, L. S., Leftin, A., Kamp, F., Haass, C., Brown, M. F., and Beyer, K. (2010) The N-terminus of the intrinsically disordered protein α-synuclein triggers membrane binding and helix folding. Biophys. J. 99, 2116-2124
    • (2010) Biophys. J. , vol.99 , pp. 2116-2124
    • Bartels, T.1    Ahlstrom, L.S.2    Leftin, A.3    Kamp, F.4    Haass, C.5    Brown, M.F.6    Beyer, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.