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Volumn 7, Issue 9, 2012, Pages

Homodimerization of Amyloid Precursor Protein at the Plasma Membrane: A homoFRET Study by Time-Resolved Fluorescence Anisotropy Imaging

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; ENHANCED GREEN FLUORESCENT PROTEIN; FLUORESCEIN; MUTANT PROTEIN;

EID: 84866039219     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0044434     Document Type: Article
Times cited : (31)

References (45)
  • 1
    • 34249724978 scopus 로고    scopus 로고
    • Imaging proteins in vivo using fluorescence lifetime microscopy
    • Festy F, Ameer-Beg SM, Ng T, Suhling K, (2007) Imaging proteins in vivo using fluorescence lifetime microscopy. Molecular bioSystems 3: 381-391.
    • (2007) Molecular BioSystems , vol.3 , pp. 381-391
    • Festy, F.1    Ameer-Beg, S.M.2    Ng, T.3    Suhling, K.4
  • 4
    • 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, Lécart S, et al. (2011) Local cholesterol increase triggers amyloid precursor protein-Bace1 clustering in lipid rafts and rapid endocytosis. The FASEB journal: 1-11.
    • (2011) The FASEB journal , pp. 1-11
    • Marquer, C.1    Devauges, V.2    Cossec, J.-C.3    Liot, G.4    Lécart, S.5
  • 5
    • 13844297577 scopus 로고    scopus 로고
    • Imaging protein molecules using FRET and FLIM microscopy
    • Wallrabe H, Periasamy A, (2005) Imaging protein molecules using FRET and FLIM microscopy. Current opinion in biotechnology 16: 19-27.
    • (2005) Current Opinion in Biotechnology , vol.16 , pp. 19-27
    • Wallrabe, H.1    Periasamy, A.2
  • 6
    • 33748453084 scopus 로고    scopus 로고
    • Comparing the quantification of Forster resonance energy transfer measurement accuracies based on intensity, spectral, and lifetime imaging
    • Pelet S, Previte MJR, So PTC, (2006) Comparing the quantification of Forster resonance energy transfer measurement accuracies based on intensity, spectral, and lifetime imaging. Journal of biomedical optics 11: 34017.
    • (2006) Journal of Biomedical Optics , vol.11 , pp. 34017
    • Pelet, S.1    Previte, M.J.R.2    So, P.T.C.3
  • 7
    • 0034964906 scopus 로고    scopus 로고
    • Homo-FRET microscopy in living cells to measure monomer-dimer transition of GFP-tagged proteins
    • Gautier I, Tramier M, Durieux C, Coppey J, Pansu RB, et al. (2001) Homo-FRET microscopy in living cells to measure monomer-dimer transition of GFP-tagged proteins. Biophys J 80: 3000-3008.
    • (2001) Biophys J , vol.80 , pp. 3000-3008
    • Gautier, I.1    Tramier, M.2    Durieux, C.3    Coppey, J.4    Pansu, R.B.5
  • 8
    • 0036932415 scopus 로고    scopus 로고
    • Picosecond-hetero-FRET microscopy to probe protein-protein interactions in live cells
    • Tramier M, Gautier I, Piolot T, Ravalet S, Kemnitz K, et al. (2002) Picosecond-hetero-FRET microscopy to probe protein-protein interactions in live cells. Biophysical journal 83: 3570-3577.
    • (2002) Biophysical Journal , vol.83 , pp. 3570-3577
    • Tramier, M.1    Gautier, I.2    Piolot, T.3    Ravalet, S.4    Kemnitz, K.5
  • 9
    • 34249674419 scopus 로고    scopus 로고
    • Imaging of protein cluster sizes by means of confocal time-gated fluorescence anisotropy microscopy
    • Bader AN, Hofman EG, van Bergen En Henegouwen PM, Gerritsen HC, (2007) Imaging of protein cluster sizes by means of confocal time-gated fluorescence anisotropy microscopy. Opt Express 15: 6934-6945.
    • (2007) Opt Express , vol.15 , pp. 6934-6945
    • Bader, A.N.1    Hofman, E.G.2    van Bergen En Henegouwen, P.M.3    Gerritsen, H.C.4
  • 11
    • 65549154337 scopus 로고    scopus 로고
    • Structural rearrangement of CaMKIIα catalytic domains encodes activation
    • Thaler C, Koushik SV, Puhl HL, Blank PS, Vogel SS, (2009) Structural rearrangement of CaMKIIα catalytic domains encodes activation. PNAS 106: 6369-6374.
    • (2009) PNAS , vol.106 , pp. 6369-6374
    • Thaler, C.1    Koushik, S.V.2    Puhl, H.L.3    Blank, P.S.4    Vogel, S.S.5
  • 12
    • 34247599842 scopus 로고    scopus 로고
    • Enumeration of oligomerization states of membrane proteins in living cells by homo-FRET spectroscopy and microscopy: Theory and application
    • Yeow EKL, Clayton AHA, (2007) Enumeration of oligomerization states of membrane proteins in living cells by homo-FRET spectroscopy and microscopy: Theory and application. Biophys J 92: 3098-3104.
    • (2007) Biophys J , vol.92 , pp. 3098-3104
    • Yeow, E.K.L.1    Clayton, A.H.A.2
  • 14
    • 84859569462 scopus 로고    scopus 로고
    • A multi-functional imaging approach to high-content protein interaction screening
    • Matthews DR, Fruhwirth GO, Weitsman G, Carlin LM, Ofo E, et al. (2012) A multi-functional imaging approach to high-content protein interaction screening. PLoS One 7: e33231.
    • (2012) PLoS One , vol.7
    • Matthews, D.R.1    Fruhwirth, G.O.2    Weitsman, G.3    Carlin, L.M.4    Ofo, E.5
  • 16
    • 67349143998 scopus 로고    scopus 로고
    • Classification and basic pathology of Alzheimer disease
    • Duyckaerts C, Delatour B, Potier MC, (2009) Classification and basic pathology of Alzheimer disease. Acta Neuropathol 118: 5-36.
    • (2009) Acta Neuropathol , vol.118 , pp. 5-36
    • Duyckaerts, C.1    Delatour, B.2    Potier, M.C.3
  • 17
    • 58149497521 scopus 로고    scopus 로고
    • Biochemistry and molecular biology of amyloid beta-protein and the mechanism of Alzheimer's disease
    • Selkoe DJ, (2008) Biochemistry and molecular biology of amyloid beta-protein and the mechanism of Alzheimer's disease. Handb Clin Neurol 89: 245-260.
    • (2008) Handb Clin Neurol , vol.89 , pp. 245-260
    • Selkoe, D.J.1
  • 18
    • 0035823495 scopus 로고    scopus 로고
    • Homodimerization of amyloid precursor protein and its implication in the amyloidogenic pathway of Alzheimer's disease
    • Scheuermann S, Hambsch B, Hesse L, Stumm J, Schmidt C, et al. (2001) Homodimerization of amyloid precursor protein and its implication in the amyloidogenic pathway of Alzheimer's disease. J Biol Chem 276: 33923-33929.
    • (2001) J Biol Chem , vol.276 , pp. 33923-33929
    • Scheuermann, S.1    Hambsch, B.2    Hesse, L.3    Stumm, J.4    Schmidt, C.5
  • 19
    • 33947597857 scopus 로고    scopus 로고
    • GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Abeta42
    • Munter L-M, Voigt P, Harmeier A, Kaden D, Gottschalk KE, et al. (2007) GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Abeta42. The EMBO journal 26: 1702-1712.
    • (2007) The EMBO Journal , vol.26 , pp. 1702-1712
    • Munter, L.-M.1    Voigt, P.2    Harmeier, A.3    Kaden, D.4    Gottschalk, K.E.5
  • 20
    • 77957096840 scopus 로고    scopus 로고
    • Amyloid beta 42 peptide (Abeta42)-lowering compounds directly bind to Abeta and interfere with amyloid precursor protein (APP) transmembrane dimerization
    • Richter L, Munter LM, Ness J, Hildebrand PW, Dasari M, et al. (2010) Amyloid beta 42 peptide (Abeta42)-lowering compounds directly bind to Abeta and interfere with amyloid precursor protein (APP) transmembrane dimerization. Proc Natl Acad Sci USA 107: 14597-14602.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 14597-14602
    • Richter, L.1    Munter, L.M.2    Ness, J.3    Hildebrand, P.W.4    Dasari, M.5
  • 21
    • 70350350069 scopus 로고    scopus 로고
    • Induced dimerization of the amyloid precursor protein leads to decreased amyloid-beta protein production
    • Eggert S, Midthune B, Cottrell B, Koo EH, (2009) Induced dimerization of the amyloid precursor protein leads to decreased amyloid-beta protein production. J Biol Chem 284: 28943-28952.
    • (2009) J Biol Chem , vol.284 , pp. 28943-28952
    • Eggert, S.1    Midthune, B.2    Cottrell, B.3    Koo, E.H.4
  • 22
    • 0018389150 scopus 로고
    • Carbocyanine dye orientation in red cell membrane studied by microscopic fluorescence polarization
    • Axelrod D, (1979) Carbocyanine dye orientation in red cell membrane studied by microscopic fluorescence polarization. Biophysical journal 26: 557-573.
    • (1979) Biophysical Journal , vol.26 , pp. 557-573
    • Axelrod, D.1
  • 23
    • 0042229743 scopus 로고
    • Physical properties of glycerol and its solutions
    • (CS Miner and NN Dalton, Eds.), (Reinhold Publishing, New York.) ISBN 52 14292
    • Godfrey TM, Hanke ME, Kem JC, Segur JB, and Werkman CH (1953). Physical properties of glycerol and its solutions. Glycerol (CS Miner and NN Dalton, Eds.), (Reinhold Publishing, New York.) ISBN 52 14292.
    • (1953) Glycerol
    • Godfrey, T.M.1    Hanke, M.E.2    Kem, J.C.3    Segur, J.B.4    Werkman, C.H.5
  • 24
    • 61349120748 scopus 로고    scopus 로고
    • Time-gated total internal reflection fluorescence microscopy with a supercontinuum excitation source
    • Blandin P, Lévêque-Fort S, Lecart S, Cossec JC, Potier MC, et al. (2009) Time-gated total internal reflection fluorescence microscopy with a supercontinuum excitation source. Applied Optics 48: 553-559.
    • (2009) Applied Optics , vol.48 , pp. 553-559
    • Blandin, P.1    Lévêque-Fort, S.2    Lecart, S.3    Cossec, J.C.4    Potier, M.C.5
  • 25
    • 0001650484 scopus 로고    scopus 로고
    • Comparison Between Fluorescence Correlation Spectroscopy and Time-Resolved Fluorescence Anisotropy as Illustrated with a Fluorescent Dextran Conjugate
    • Visser NV, Hink MA, Hoek AV, Visser AJWG, (1999) Comparison Between Fluorescence Correlation Spectroscopy and Time-Resolved Fluorescence Anisotropy as Illustrated with a Fluorescent Dextran Conjugate. Journal of Fluorescence 9: 251-255.
    • (1999) Journal of Fluorescence , vol.9 , pp. 251-255
    • Visser, N.V.1    Hink, M.A.2    Hoek, A.V.3    Visser, A.J.W.G.4
  • 26
    • 34548828829 scopus 로고    scopus 로고
    • Fluorescence polarization spectroscopy at combined high-aperture excitation and detection: application to one-photon-excitation fluorescence microscopy
    • Fisz JJ, (2007) Fluorescence polarization spectroscopy at combined high-aperture excitation and detection: application to one-photon-excitation fluorescence microscopy. Journal of Physical Chemistry A 111: 8606-8621.
    • (2007) Journal of Physical Chemistry A , vol.111 , pp. 8606-8621
    • Fisz, J.J.1
  • 27
    • 64849097265 scopus 로고    scopus 로고
    • Another Treatment of Fluorescence Polarization Microspectroscopy and Imaging
    • Fisz JJ, (2009) Another Treatment of Fluorescence Polarization Microspectroscopy and Imaging. Journal of Physical Chemistry A 113: 3505-3516.
    • (2009) Journal of Physical Chemistry A , vol.113 , pp. 3505-3516
    • Fisz, J.J.1
  • 28
    • 0001039396 scopus 로고
    • Time-Dependent Fluorescence Depolarization Analysis in 3-Dimensional Microspectroscopy
    • Koshioka M, Sasaki K, Masuhara H, (1995) Time-Dependent Fluorescence Depolarization Analysis in 3-Dimensional Microspectroscopy. Applied Spectroscopy 49: 224-228.
    • (1995) Applied Spectroscopy , vol.49 , pp. 224-228
    • Koshioka, M.1    Sasaki, K.2    Masuhara, H.3
  • 29
    • 12244293373 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer imaging microscopy and fluorescence polarization imaging microscopy
    • Yan Y, Marriott G, (2003) Fluorescence resonance energy transfer imaging microscopy and fluorescence polarization imaging microscopy. Methods Enzymol 360: 561-580.
    • (2003) Methods Enzymol , vol.360 , pp. 561-580
    • Yan, Y.1    Marriott, G.2
  • 33
    • 66449129795 scopus 로고    scopus 로고
    • Mechanochemical delivery and dynamic tracking of fluorescent quantum dots in the cytoplasm and nucleus of living cells
    • Yum K, Na S, Xiang Y, Wang N, Yu M-F, (2009) Mechanochemical delivery and dynamic tracking of fluorescent quantum dots in the cytoplasm and nucleus of living cells. Nano letters 9: 2193-2198.
    • (2009) Nano Letters , vol.9 , pp. 2193-2198
    • Yum, K.1    Na, S.2    Xiang, Y.3    Wang, N.4    Yu, M.-F.5
  • 34
    • 0034022816 scopus 로고    scopus 로고
    • Restrained torsional dynamics of nuclear DNA in living proliferative mammalian cells
    • Tramier M, Kemnitz K, Durieux C, Coppey J, Denjean P, et al. (2000) Restrained torsional dynamics of nuclear DNA in living proliferative mammalian cells. Biophys J 78: 2614-2627.
    • (2000) Biophys J , vol.78 , pp. 2614-2627
    • Tramier, M.1    Kemnitz, K.2    Durieux, C.3    Coppey, J.4    Denjean, P.5
  • 35
    • 0002617657 scopus 로고    scopus 로고
    • The Influence of Solvent Viscosity on the Fluorescence Decay and Time-Resolved Anisotropy of Green Fluorescent Protein
    • Suhling K, Davis DM, Phillips D, (2002) The Influence of Solvent Viscosity on the Fluorescence Decay and Time-Resolved Anisotropy of Green Fluorescent Protein. Journal of Fluorescence 12: 91-95-95.
    • (2002) Journal of Fluorescence , vol.12 , pp. 91-95
    • Suhling, K.1    Davis, D.M.2    Phillips, D.3
  • 36
    • 65449126189 scopus 로고    scopus 로고
    • Time-resolved evanescent wave-induced fluorescence anisotropy measurements
    • In: Geddes CD, Lakowicz JR, editors, Springer
    • Smith TA, Gee ML, Scholes Ca (2005) Time-resolved evanescent wave-induced fluorescence anisotropy measurements. In: Geddes CD, Lakowicz JR, editors. Reviews in Fluorescence 2005: Springer. 245-269.
    • (2005) Reviews in Fluorescence 2005 , pp. 245-269
    • Smith, T.A.1    Gee, M.L.2    Scholes, C.3
  • 37
    • 84856541323 scopus 로고    scopus 로고
    • Structural features of the KPI domain control APP dimerization, trafficking, and processing
    • Ben Khalifa N, Tyteca D, Marinangeli C, Depuydt M, Collet JF, et al. (2011) Structural features of the KPI domain control APP dimerization, trafficking, and processing. FASEB J 26: 855-867.
    • (2011) FASEB J , vol.26 , pp. 855-867
    • Ben Khalifa, N.1    Tyteca, D.2    Marinangeli, C.3    Depuydt, M.4    Collet, J.F.5
  • 38
    • 67649366042 scopus 로고    scopus 로고
    • Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers
    • Gralle M, Botelho MG, Wouters FS, (2009) Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers. J Biol Chem 284: 15016-15025.
    • (2009) J Biol Chem , vol.284 , pp. 15016-15025
    • Gralle, M.1    Botelho, M.G.2    Wouters, F.S.3
  • 39
    • 43149088724 scopus 로고    scopus 로고
    • Amyloidogenic processing but not amyloid precursor protein (APP) intracellular C-terminal domain production requires a precisely oriented APP dimer assembled by transmembrane GXXXG motifs
    • Kienlen-Campard P, Tasiaux B, Van Hees J, Li M, Huysseune S, et al. (2008) Amyloidogenic processing but not amyloid precursor protein (APP) intracellular C-terminal domain production requires a precisely oriented APP dimer assembled by transmembrane GXXXG motifs. J Biol Chem 283: 7733-7744.
    • (2008) J Biol Chem , vol.283 , pp. 7733-7744
    • Kienlen-Campard, P.1    Tasiaux, B.2    van Hees, J.3    Li, M.4    Huysseune, S.5
  • 40
    • 43749112022 scopus 로고    scopus 로고
    • Homophilic interactions of the amyloid precursor protein (APP) ectodomain are regulated by the loop region and affect beta-secretase cleavage of APP
    • Kaden D, Munter LM, Joshi M, Treiber C, Weise C, et al. (2008) Homophilic interactions of the amyloid precursor protein (APP) ectodomain are regulated by the loop region and affect beta-secretase cleavage of APP. J Biol Chem 283: 7271-7279.
    • (2008) J Biol Chem , vol.283 , pp. 7271-7279
    • Kaden, D.1    Munter, L.M.2    Joshi, M.3    Treiber, C.4    Weise, C.5
  • 41
    • 40549088246 scopus 로고    scopus 로고
    • Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants
    • Gorman PM, Kim S, Guo M, Melnyk RA, McLaurin J, et al. (2008) Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants. BMC Neurosci 9: 17.
    • (2008) BMC Neurosci , vol.9 , pp. 17
    • Gorman, P.M.1    Kim, S.2    Guo, M.3    Melnyk, R.A.4    McLaurin, J.5
  • 42
    • 80053571400 scopus 로고    scopus 로고
    • N-cadherin enhances APP dimerization at the extracellular domain and modulates Abeta production
    • Asada-Utsugi M, Uemura K, Noda Y, Kuzuya A, Maesako M, et al. (2011) N-cadherin enhances APP dimerization at the extracellular domain and modulates Abeta production. J Neurochem 119: 354-363.
    • (2011) J Neurochem , vol.119 , pp. 354-363
    • Asada-Utsugi, M.1    Uemura, K.2    Noda, Y.3    Kuzuya, A.4    Maesako, M.5
  • 43
    • 84860869183 scopus 로고    scopus 로고
    • APP dimer formation is initiated in the endoplasmic reticulum and differs between APP isoforms
    • Isbert S, Wagner K, Eggert S, Schweitzer A, Multhaup G, et al. (2012) APP dimer formation is initiated in the endoplasmic reticulum and differs between APP isoforms. Cell Mol Life Sci 69: 1353-1375.
    • (2012) Cell Mol Life Sci , vol.69 , pp. 1353-1375
    • Isbert, S.1    Wagner, K.2    Eggert, S.3    Schweitzer, A.4    Multhaup, G.5
  • 44
    • 27144547977 scopus 로고    scopus 로고
    • Homo- and heterodimerization of APP family members promotes intercellular adhesion
    • Soba P, Eggert S, Wagner K, Zentgraf H, Siehl K, et al. (2005) Homo- and heterodimerization of APP family members promotes intercellular adhesion. EMBO J 24: 3624-3634.
    • (2005) EMBO J , vol.24 , pp. 3624-3634
    • Soba, P.1    Eggert, S.2    Wagner, K.3    Zentgraf, H.4    Siehl, K.5
  • 45
    • 77953260583 scopus 로고    scopus 로고
    • Clathrin-dependent APP endocytosis and Abeta secretion are highly sensitive to the level of plasma membrane cholesterol
    • Cossec JC, Simon A, Marquer C, Moldrich RX, Leterrier C, et al. (2010) Clathrin-dependent APP endocytosis and Abeta secretion are highly sensitive to the level of plasma membrane cholesterol. Biochim Biophys Acta 1801: 846-852.
    • (2010) Biochim Biophys Acta , vol.1801 , pp. 846-852
    • Cossec, J.C.1    Simon, A.2    Marquer, C.3    Moldrich, R.X.4    Leterrier, C.5


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