메뉴 건너뛰기




Volumn 7, Issue 18, 2016, Pages 3535-3541

Specific Binding of Cholesterol to C99 Domain of Amyloid Precursor Protein Depends Critically on Charge State of Protein

Author keywords

[No Author keywords available]

Indexed keywords

BINS; BIOLOGICAL MEMBRANES; CHEMICAL SHIFT; CYTOLOGY; GLYCOPROTEINS; PROTEINS;

EID: 84987924576     PISSN: None     EISSN: 19487185     Source Type: Journal    
DOI: 10.1021/acs.jpclett.6b01624     Document Type: Article
Times cited : (32)

References (50)
  • 1
    • 79959886270 scopus 로고    scopus 로고
    • Amyloid Precursor Protein Processing and Alzheimer's Disease
    • O'Brien, R. J.; Wong, P. C. Amyloid Precursor Protein Processing and Alzheimer's Disease Annu. Rev. Neurosci. 2011, 34, 185-204 10.1146/annurev-neuro-061010-113613
    • (2011) Annu. Rev. Neurosci. , vol.34 , pp. 185-204
    • O'Brien, R.J.1    Wong, P.C.2
  • 2
    • 70350451482 scopus 로고    scopus 로고
    • γ-Secretase: Successive Tripeptide and Tetrapeptide Release from the Transmembrane Domain of β-Carboxyl Terminal Fragment
    • Takami, M.; Nagashima, Y.; Sano, Y.; Ishihara, S.; Morishima-Kawashima, M.; Funamoto, S.; Ihara γ-Secretase: Successive Tripeptide and Tetrapeptide Release from the Transmembrane Domain of β-Carboxyl Terminal Fragment J. Neurosci. 2009, 29, 13042-13052 10.1523/JNEUROSCI.2362-09.2009
    • (2009) J. Neurosci. , vol.29 , pp. 13042-13052
    • Takami, M.1    Nagashima, Y.2    Sano, Y.3    Ishihara, S.4    Morishima-Kawashima, M.5    Funamoto, S.6    Ihara7
  • 3
    • 81155154306 scopus 로고    scopus 로고
    • Lysine 624 of the Amyloid Precursor Protein (APP) Is a Critical Determinant of Amyloid Peptide Length: Support for a Sequential Model of γ-Secretase Intramembrane Proteolysis and Regulation by the Amyloid Precursor Protein (APP) Juxtamembrane Region
    • Kukar, T. L.; Ladd, T. B.; Robertson, P.; Pintchovski, S. A.; Moore, B.; Bann, M. A.; Ren, Z.; Jansen-West, K.; Malphrus, K.; Eggert, S. et al. Lysine 624 of the Amyloid Precursor Protein (APP) Is a Critical Determinant of Amyloid Peptide Length: Support for a Sequential Model of γ-Secretase Intramembrane Proteolysis and Regulation by the Amyloid Precursor Protein (APP) Juxtamembrane Region J. Biol. Chem. 2011, 286, 39804-39812 10.1074/jbc.M111.274696
    • (2011) J. Biol. Chem. , vol.286 , pp. 39804-39812
    • Kukar, T.L.1    Ladd, T.B.2    Robertson, P.3    Pintchovski, S.A.4    Moore, B.5    Bann, M.A.6    Ren, Z.7    Jansen-West, K.8    Malphrus, K.9    Eggert, S.10
  • 4
    • 79953118623 scopus 로고    scopus 로고
    • Toward a Molecular Theory of Early and Late Events in Monomer to Amyloid Fibril Formation
    • Straub, J. E.; Thirumalai, D. Toward a Molecular Theory of Early and Late Events in Monomer to Amyloid Fibril Formation Annu. Rev. Phys. Chem. 2011, 62, 437-463 10.1146/annurev-physchem-032210-103526
    • (2011) Annu. Rev. Phys. Chem. , vol.62 , pp. 437-463
    • Straub, J.E.1    Thirumalai, D.2
  • 5
    • 77649240855 scopus 로고    scopus 로고
    • Identifying the Amylome, Proteins Capable of Forming Amyloid-like Fibrils
    • Goldschmidt, L.; Teng, P. K.; Riek, R.; Eisenberg, D. Identifying the Amylome, Proteins Capable of Forming Amyloid-like Fibrils Proc. Natl. Acad. Sci. U. S. A. 2010, 107, 3487-3492 10.1073/pnas.0915166107
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 3487-3492
    • Goldschmidt, L.1    Teng, P.K.2    Riek, R.3    Eisenberg, D.4
  • 8
    • 84892958093 scopus 로고    scopus 로고
    • Transmembrane Fragment Structures of Amyloid Precursor Protein Depend on Membrane Surface Curvature
    • Dominguez, L.; Meredith, S. C.; Straub, J. E.; Thirumalai, D. Transmembrane Fragment Structures of Amyloid Precursor Protein Depend on Membrane Surface Curvature J. Am. Chem. Soc. 2014, 136, 854-857 10.1021/ja410958j
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 854-857
    • Dominguez, L.1    Meredith, S.C.2    Straub, J.E.3    Thirumalai, D.4
  • 9
    • 84903973868 scopus 로고    scopus 로고
    • Structural Heterogeneity in Transmembrane Amyloid Precursor Protein Homodimer Is a Consequence of Environmental Selection
    • Dominguez, L.; Foster, L.; Meredith, S. C.; Straub, J. E.; Thirumalai, D. Structural Heterogeneity in Transmembrane Amyloid Precursor Protein Homodimer Is a Consequence of Environmental Selection J. Am. Chem. Soc. 2014, 136, 9619-9626 10.1021/ja503150x
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 9619-9626
    • Dominguez, L.1    Foster, L.2    Meredith, S.C.3    Straub, J.E.4    Thirumalai, D.5
  • 10
    • 84889045199 scopus 로고    scopus 로고
    • Structural and Dynamic Study of the Transmembrane Domain of the Amyloid Precursor Protein
    • Nadezhdin, K. D.; Bocharova, O. V.; Bocharov, E. V.; Arseniev, A. S. Structural and Dynamic Study of the Transmembrane Domain of the Amyloid Precursor Protein Acta Naturae 2011, 3, 69-76
    • (2011) Acta Naturae , vol.3 , pp. 69-76
    • Nadezhdin, K.D.1    Bocharova, O.V.2    Bocharov, E.V.3    Arseniev, A.S.4
  • 11
    • 51549106517 scopus 로고    scopus 로고
    • Structural Studies of the Transmembrane C-Terminal Domain of the Amyloid Precursor Protein (APP): Does APP Function as a Cholesterol Sensor?
    • Beel, A. J.; Mobley, C. K.; Kim, H. J.; Tian, F.; Hadziselimovic, A.; Jap, B.; Prestegard, J. H.; Sanders, C. R. Structural Studies of the Transmembrane C-Terminal Domain of the Amyloid Precursor Protein (APP): Does APP Function as a Cholesterol Sensor? Biochemistry 2008, 47, 9428-9446 10.1021/bi800993c
    • (2008) Biochemistry , vol.47 , pp. 9428-9446
    • Beel, A.J.1    Mobley, C.K.2    Kim, H.J.3    Tian, F.4    Hadziselimovic, A.5    Jap, B.6    Prestegard, J.H.7    Sanders, C.R.8
  • 13
    • 84896692890 scopus 로고    scopus 로고
    • Perturbations of the Straight Transmembrane α-Helical Structure of the Amyloid Precursor Protein Affect Its Processing by γ-Secretase
    • Lemmin, T.; Dimitrov, M.; Fraering, P., C.; Dal Peraro, M. Perturbations of the Straight Transmembrane α-Helical Structure of the Amyloid Precursor Protein Affect Its Processing by γ-Secretase J. Biol. Chem. 2014, 289, 6763-6774 10.1074/jbc.M113.470781
    • (2014) J. Biol. Chem. , vol.289 , pp. 6763-6774
    • Lemmin, T.1    Dimitrov, M.2    Fraering, P.C.3    Dal Peraro, M.4
  • 14
    • 84883556425 scopus 로고    scopus 로고
    • How Cholesterol Interacts with Membrane Proteins: An Exploration of Cholesterol-Binding Sites Including CRAC, CARC, and Tilted Domains
    • Fantini, J.; Barrantes, F. J. How Cholesterol Interacts with Membrane Proteins: An Exploration of Cholesterol-Binding Sites Including CRAC, CARC, and Tilted Domains Front. Physiol. 2013, 4, 00031 10.3389/fphys.2013.00031
    • (2013) Front. Physiol. , vol.4 , pp. 00031
    • Fantini, J.1    Barrantes, F.J.2
  • 15
    • 84895768344 scopus 로고    scopus 로고
    • Cholesterol as a Co-Solvent and a Ligand for Membrane Proteins
    • Song, Y.; Kenworthy, A. K.; Sanders, C. R. Cholesterol as a Co-Solvent and a Ligand for Membrane Proteins Protein Sci. 2014, 23, 1-22 10.1002/pro.2385
    • (2014) Protein Sci. , vol.23 , pp. 1-22
    • Song, Y.1    Kenworthy, A.K.2    Sanders, C.R.3
  • 16
    • 84987781493 scopus 로고    scopus 로고
    • Effect of the Synaptic Plasma Membrane on the Stability of the Amyloid Precursor Protein Homodimer
    • Audagnotto, M.; Lemmin, T.; Barducci, A.; Dal Peraro, M. Effect of the Synaptic Plasma Membrane on the Stability of the Amyloid Precursor Protein Homodimer J. Phys. Chem. Lett. 2016, 10.1021/acs.jpclett.6b01721
    • (2016) J. Phys. Chem. Lett.
    • Audagnotto, M.1    Lemmin, T.2    Barducci, A.3    Dal Peraro, M.4
  • 18
    • 84881040452 scopus 로고    scopus 로고
    • Competition between Homodimerization and Cholesterol Binding to the C99 Domain of the Amyloid Precursor Protein
    • Song, Y.; Hustedt, E. J.; Brandon, S.; Sanders, C. R. Competition Between Homodimerization and Cholesterol Binding to the C99 Domain of the Amyloid Precursor Protein Biochemistry 2013, 52, 5051-5064 10.1021/bi400735x
    • (2013) Biochemistry , vol.52 , pp. 5051-5064
    • Song, Y.1    Hustedt, E.J.2    Brandon, S.3    Sanders, C.R.4
  • 21
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic Processing of the Alzheimer β-Amyloid Precursor Protein Depends on Lipid Rafts
    • Ehehalt, R.; Keller, P.; Haass, C.; Thiele, C.; Simons, K. Amyloidogenic Processing of the Alzheimer β-Amyloid Precursor Protein Depends on Lipid Rafts J. Cell Biol. 2003, 160, 113-123 10.1083/jcb.200207113
    • (2003) J. Cell Biol. , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 22
    • 0031746979 scopus 로고    scopus 로고
    • A Detergent-Insoluble Membrance Compartment Contains Aβ in Vivo
    • Lee, S. J.; Liyanage, U.; Bickel, P. E.; Xia, W.; Lansbury, P. T.; Kosik, K. S. A Detergent-Insoluble Membrance Compartment Contains Aβ in Vivo Nat. Med. 1998, 4, 730-734 10.1038/nm0698-730
    • (1998) Nat. Med. , vol.4 , pp. 730-734
    • Lee, S.J.1    Liyanage, U.2    Bickel, P.E.3    Xia, W.4    Lansbury, P.T.5    Kosik, K.S.6
  • 23
    • 84929166414 scopus 로고    scopus 로고
    • Specific Binding of Cholesterol to the Amyloid Precursor Protein: Structure of the Complex and Driving Forces Characterized in Molecular Detail
    • Nierzwicki, A.; Czub, J. Specific Binding of Cholesterol to the Amyloid Precursor Protein: Structure of the Complex and Driving Forces Characterized in Molecular Detail J. Phys. Chem. Lett. 2015, 6, 784-790 10.1021/acs.jpclett.5b00197
    • (2015) J. Phys. Chem. Lett. , vol.6 , pp. 784-790
    • Nierzwicki, A.1    Czub, J.2
  • 24
    • 84896507992 scopus 로고    scopus 로고
    • Impact of Bilayer Lipid Composition on the Structure and Topology of the Transmembrane Amyloid Precursor C99 Protein
    • Song, Y.; Mittendorf, K. F.; Lu, Z.; Sanders, C. R. Impact of Bilayer Lipid Composition on the Structure and Topology of the Transmembrane Amyloid Precursor C99 Protein J. Am. Chem. Soc. 2014, 136, 4093-4096 10.1021/ja4114374
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 4093-4096
    • Song, Y.1    Mittendorf, K.F.2    Lu, Z.3    Sanders, C.R.4
  • 25
    • 84884538771 scopus 로고    scopus 로고
    • Cholesterol Accelerates the Binding of Alzheimer's β-Amyloid Peptide to Ganglioside GM1 through a Universal Hydrogen-Bond-Dependent Sterol Tuning of Glycolipid Conformation
    • Fantini, J.; Yahi, N.; Garmy, N. Cholesterol Accelerates the Binding of Alzheimer's β-Amyloid Peptide to Ganglioside GM1 through a Universal Hydrogen-Bond-Dependent Sterol Tuning of Glycolipid Conformation Front. Physiol. 2013, 4, 1-10 10.3389/fphys.2013.00120
    • (2013) Front. Physiol. , vol.4 , pp. 1-10
    • Fantini, J.1    Yahi, N.2    Garmy, N.3
  • 26
    • 79958185452 scopus 로고    scopus 로고
    • MDAnalysis: A Toolkit for the Analysis of Molecular Dynamics Simulations
    • Michaud-Agrawal, N.; Denning, E. J.; Woolf, T. B.; Beckstein, O. MDAnalysis: A Toolkit for the Analysis of Molecular Dynamics Simulations J. Comput. Chem. 2011, 32, 2319-2327 10.1002/jcc.21787
    • (2011) J. Comput. Chem. , vol.32 , pp. 2319-2327
    • Michaud-Agrawal, N.1    Denning, E.J.2    Woolf, T.B.3    Beckstein, O.4
  • 27
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual Molecular Dynamics
    • Humphrey, W.; Dalke, A.; Schulten, K. VMD: Visual Molecular Dynamics J. Mol. Graphics 1996, 14, 33-38 10.1016/0263-7855(96)00018-5
    • (1996) J. Mol. Graphics , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 29
    • 0028276801 scopus 로고
    • Evidence That Production and Release of Amyloid β-Protein Involves the Endocytic Pathway
    • Koo, E. H.; Squazzo, S. L. Evidence That Production and Release of Amyloid β-Protein Involves the Endocytic Pathway J. Biol. Chem. 1994, 269, 17386-17389
    • (1994) J. Biol. Chem. , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 30
    • 79954584874 scopus 로고    scopus 로고
    • Local Cholesterol Increase Triggers Amyloid Precursor Protein-Bace1 Clustering in Lipid Rafts and Rapid Endocytosis
    • Marquer, C.; Devauges, V.; Cossec, J.-C.; Liot, G.; Lecart, S.; Saudou, F.; Duyckaerts, C.; Leveque-Fort, S.; Potier, M.-C. Local Cholesterol Increase Triggers Amyloid Precursor Protein-Bace1 Clustering in Lipid Rafts and Rapid Endocytosis FASEB J. 2011, 25, 1295-1305 10.1096/fj.10-168633
    • (2011) FASEB J. , vol.25 , pp. 1295-1305
    • Marquer, C.1    Devauges, V.2    Cossec, J.-C.3    Liot, G.4    Lecart, S.5    Saudou, F.6    Duyckaerts, C.7    Leveque-Fort, S.8    Potier, M.-C.9
  • 31
    • 0033516554 scopus 로고    scopus 로고
    • Mutagenesis Identifies New Signals for β-Amyloid Precursor Protein Endocytosis, Turnover, and the Generation of Secreted Fragments, Including Aβ 42
    • Perez, R. G.; Soriano, S.; Hayes, J. D.; Ostaszewski, B.; Xia, W.; Selkoe, D. J.; Chen, X.; Stokin, G. B.; Koo, E. H. Mutagenesis Identifies New Signals for β-Amyloid Precursor Protein Endocytosis, Turnover, and the Generation of Secreted Fragments, Including Aβ 42 J. Biol. Chem. 1999, 274, 18851-18856 10.1074/jbc.274.27.18851
    • (1999) J. Biol. Chem. , vol.274 , pp. 18851-18856
    • Perez, R.G.1    Soriano, S.2    Hayes, J.D.3    Ostaszewski, B.4    Xia, W.5    Selkoe, D.J.6    Chen, X.7    Stokin, G.B.8    Koo, E.H.9
  • 32
    • 0042733013 scopus 로고    scopus 로고
    • Rab5-Stimulated Up-Regulation of the Endocytic Pathway Increases Intracellular β-Cleaved Amyloid Precursor Protein Carboxyl-Terminal Fragment Levels and Aβ Production
    • Grbovic, O. M.; Mathews, P. M.; Jiang, Y.; Schmidt, S. D.; Dinakar, R.; Summers-Terio, N. B.; Ceresa, B. P.; Nixon, R. A.; Cataldo, A. M. Rab5-Stimulated Up-Regulation of the Endocytic Pathway Increases Intracellular β-Cleaved Amyloid Precursor Protein Carboxyl-Terminal Fragment Levels and Aβ Production J. Biol. Chem. 2003, 278, 31261-31268 10.1074/jbc.M304122200
    • (2003) J. Biol. Chem. , vol.278 , pp. 31261-31268
    • Grbovic, O.M.1    Mathews, P.M.2    Jiang, Y.3    Schmidt, S.D.4    Dinakar, R.5    Summers-Terio, N.B.6    Ceresa, B.P.7    Nixon, R.A.8    Cataldo, A.M.9
  • 34
  • 35
    • 84926443744 scopus 로고    scopus 로고
    • Membrane Environment Modulates the pKa Values of Transmembrane Helices
    • Panahi, A.; Brooks, C. L. Membrane Environment Modulates the pKa Values of Transmembrane Helices J. Phys. Chem. B 2015, 119, 4601-4607 10.1021/acs.jpcb.5b00289
    • (2015) J. Phys. Chem. B , vol.119 , pp. 4601-4607
    • Panahi, A.1    Brooks, C.L.2
  • 36
    • 41149134824 scopus 로고    scopus 로고
    • Automated Builder and Database of Protein/membrane Complexes for Molecular Dynamics Simulations
    • Jo, S.; Kim, T.; Im, W. Automated Builder and Database of Protein/membrane Complexes for Molecular Dynamics Simulations PLoS One 2007, 2, e880 10.1371/journal.pone.0000880
    • (2007) PLoS One , vol.2 , pp. e880
    • Jo, S.1    Kim, T.2    Im, W.3
  • 37
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A Package for Molecular Simulation and Trajectory Analysis
    • Lindahl, E.; Hess, B.; van der Spoel, D. GROMACS 3.0: A Package for Molecular Simulation and Trajectory Analysis Mol. Model. Annu. 2001, 7, 306-317 10.1007/s008940100045
    • (2001) Mol. Model. Annu. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 38
    • 0029633168 scopus 로고
    • ROMACS: A Message-Passing Parallel Molecular Dynamics Implementation
    • Berendsen, H. J. C.; van der Spoel, D.; van Drunen, R. ROMACS: A Message-Passing Parallel Molecular Dynamics Implementation Comput. Phys. Commun. 1995, 91, 43-56 10.1016/0010-4655(95)00042-E
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    Van Der Spoel, D.2    Van Drunen, R.3
  • 40
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • Hess, B.; Kutzner, C.; van der Spoel, D.; Lindahl, E. GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation J. Chem. Theory Comput. 2008, 4, 435-447 10.1021/ct700301q
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 41
    • 84946416234 scopus 로고    scopus 로고
    • GROMACS: High Performance Molecular Simulations through Multi-Level Parallelism from Laptops to Supercomputers
    • Abraham, M. J.; Murtola, T.; Schulz, R.; Páll, S.; Smith, J. C.; Hess, B.; Lindahl, E. GROMACS: High Performance Molecular Simulations through Multi-Level Parallelism from Laptops to Supercomputers SoftwareX 2015, 1-2, 19-25 10.1016/j.softx.2015.06.001
    • (2015) SoftwareX , vol.12 , pp. 19-25
    • Abraham, M.J.1    Murtola, T.2    Schulz, R.3    Páll, S.4    Smith, J.C.5    Hess, B.6    Lindahl, E.7
  • 45
    • 80052811290 scopus 로고    scopus 로고
    • Applying Efficient Implicit Nongeometric Constraints in Alchemical Free Energy Simulations
    • Knight, J. L.; Brooks, C. L. Applying Efficient Implicit Nongeometric Constraints in Alchemical Free Energy Simulations J. Comput. Chem. 2011, 32, 3423-3432 10.1002/jcc.21921
    • (2011) J. Comput. Chem. , vol.32 , pp. 3423-3432
    • Knight, J.L.1    Brooks, C.L.2
  • 46
    • 80052805166 scopus 로고    scopus 로고
    • Multi-Site λ-Dynamics for Simulated Structure-Activity Relationship Studies
    • Knight, J. L.; Brooks, C. L. Multi-Site λ-Dynamics for Simulated Structure-Activity Relationship Studies J. Chem. Theory Comput. 2011, 7, 2728-2739 10.1021/ct200444f
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 2728-2739
    • Knight, J.L.1    Brooks, C.L.2
  • 47
    • 84902127084 scopus 로고    scopus 로고
    • Constant pH Molecular Dynamics of Proteins in Explicit Solvent with Proton Tautomerism
    • Goh, G. B.; Hulbert, B. S.; Zhou, H.; Brooks, C. L. Constant pH Molecular Dynamics of Proteins in Explicit Solvent with Proton Tautomerism Proteins: Struct., Funct., Genet. 2014, 82, 1319-1331 10.1002/prot.24499
    • (2014) Proteins: Struct., Funct., Genet. , vol.82 , pp. 1319-1331
    • Goh, G.B.1    Hulbert, B.S.2    Zhou, H.3    Brooks, C.L.4
  • 48
    • 84855710487 scopus 로고    scopus 로고
    • Constant pH Molecular Dynamics Simulations of Nucleic Acids in Explicit Solvent
    • Goh, G. B.; Knight, J. L.; Brooks, C. L. Constant pH Molecular Dynamics Simulations of Nucleic Acids in Explicit Solvent J. Chem. Theory Comput. 2012, 8, 36-46 10.1021/ct2006314
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 36-46
    • Goh, G.B.1    Knight, J.L.2    Brooks, C.L.3
  • 49
    • 84902669883 scopus 로고    scopus 로고
    • Uncovering pH-Dependent Transient States of Proteins with Buried Ionizable Residues
    • Goh, G. B.; Laricheva, E. N.; Brooks, C. L. Uncovering pH-Dependent Transient States of Proteins with Buried Ionizable Residues J. Am. Chem. Soc. 2014, 136, 8496-8499 10.1021/ja5012564
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 8496-8499
    • Goh, G.B.1    Laricheva, E.N.2    Brooks, C.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.