메뉴 건너뛰기




Volumn 289, Issue 27, 2014, Pages 19019-19030

Novel zinc-binding site in the E2 domain regulates amyloid precursor-like protein 1 (APLP1) oligomerization

Author keywords

[No Author keywords available]

Indexed keywords

OLIGOMERIZATION; ZINC;

EID: 84903842312     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.570382     Document Type: Article
Times cited : (21)

References (68)
  • 1
    • 0033972608 scopus 로고    scopus 로고
    • What the evolution of the amyloid protein precursor supergene family tells us about its function
    • Coulson, E. J., Paliga, K., Beyreuther, K., and Masters, C. L. (2000) What the evolution of the amyloid protein precursor supergene family tells us about its function. Neurochem. Int. 36, 175-184
    • (2000) Neurochem. Int. , vol.36 , pp. 175-184
    • Coulson, E.J.1    Paliga, K.2    Beyreuther, K.3    Masters, C.L.4
  • 2
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J., and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 3
    • 2442592973 scopus 로고    scopus 로고
    • The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves -, -, -, and -like cleavages: Modulation of APLP-1 processing by N -glycosylation
    • Eggert, S., Paliga, K., Soba, P., Evin, G., Masters, C. L., Weidemann, A., and Beyreuther, K. (2004) The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves -, -, -, and -like cleavages: modulation of APLP-1 processing by N -glycosylation. J. Biol. Chem. 279, 18146-18156
    • (2004) J. Biol. Chem. , vol.279 , pp. 18146-18156
    • Eggert, S.1    Paliga, K.2    Soba, P.3    Evin, G.4    Masters, C.L.5    Weidemann, A.6    Beyreuther, K.7
  • 4
    • 1642345964 scopus 로고    scopus 로고
    • Cleavage of amyloid- precursor protein and amyloid- precursor-like protein by BACE 1
    • Li, Q., and Südhof, T. C. (2004) Cleavage of amyloid- precursor protein and amyloid- precursor-like protein by BACE 1. J. Biol. Chem. 279, 10542-10550
    • (2004) J. Biol. Chem. , vol.279 , pp. 10542-10550
    • Li, Q.1    Südhof, T.C.2
  • 7
    • 65249143369 scopus 로고    scopus 로고
    • Subcellular localization and dimerization of APLP1 are strikingly different from APP and APLP2
    • Kaden, D., Voigt, P., Munter, L.-M., Bobowski, K. D., Schaefer, M., and Multhaup, G. (2009) Subcellular localization and dimerization of APLP1 are strikingly different from APP and APLP2. J. Cell Sci. 122, 368-377
    • (2009) J. Cell Sci. , vol.122 , pp. 368-377
    • Kaden, D.1    Voigt, P.2    Munter, L.-M.3    Bobowski, K.D.4    Schaefer, M.5    Multhaup, G.6
  • 10
    • 8144230876 scopus 로고    scopus 로고
    • Cortical dysplasia resembling human type 2 lissencephaly in mice lacking all three APP family members
    • Herms, J., Anliker, B., Heber, S., Ring, S., Fuhrmann, M., Kretzschmar, H., Sisodia, S., and Müller, U. (2004) Cortical dysplasia resembling human type 2 lissencephaly in mice lacking all three APP family members. EMBO J. 23, 4106-4115
    • (2004) EMBO J. , vol.23 , pp. 4106-4115
    • Herms, J.1    Anliker, B.2    Heber, S.3    Ring, S.4    Fuhrmann, M.5    Kretzschmar, H.6    Sisodia, S.7    Müller, U.8
  • 14
    • 69749115919 scopus 로고    scopus 로고
    • Presynaptic and postsynaptic interaction of the amyloid precursor protein promotes peripheral and central synaptogenesis
    • Wang, Z., Wang, B., Yang, L., Guo, Q., Aithmitti, N., Songyang, Z., and Zheng, H. (2009) Presynaptic and postsynaptic interaction of the amyloid precursor protein promotes peripheral and central synaptogenesis. J. Neurosci. 29, 10788-10801
    • (2009) J. Neurosci. , vol.29 , pp. 10788-10801
    • Wang, Z.1    Wang, B.2    Yang, L.3    Guo, Q.4    Aithmitti, N.5    Songyang, Z.6    Zheng, H.7
  • 18
    • 0028914672 scopus 로고
    • Expression in mouse embryos and in adult mouse brain of three members of the amyloid precursor protein family, of the -2-macroglobulin receptor/low density lipoprotein receptor-related protein and of its ligands apolipoprotein E, lipoprotein lipase, -2-macroglobulin and the 40,000 molecular weight receptor-associated protein
    • Lorent, K., Overbergh, L., Moechars, D., De Strooper, B., Van Leuven, F., and Van den Berghe, H. (1995) Expression in mouse embryos and in adult mouse brain of three members of the amyloid precursor protein family, of the -2-macroglobulin receptor/low density lipoprotein receptor-related protein and of its ligands apolipoprotein E, lipoprotein lipase, -2-macroglobulin and the 40,000 molecular weight receptor-associated protein. Neuroscience 65, 1009-1025
    • (1995) Neuroscience , vol.65 , pp. 1009-1025
    • Lorent, K.1    Overbergh, L.2    Moechars, D.3    De Strooper, B.4    Van Leuven, F.5    Van Den Berghe, H.6
  • 21
    • 0028171064 scopus 로고
    • The amyloid -protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily
    • Bush, A. I., Pettingell, W. H., Jr., de Paradis, M., Tanzi, R. E., and Wasco, W. (1994) The amyloid -protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily. J. Biol. Chem. 269, 26618-26621
    • (1994) J. Biol. Chem. , vol.269 , pp. 26618-26621
    • Bush, A.I.1    Pettingell Jr., W.H.2    De Paradis, M.3    Tanzi, R.E.4    Wasco, W.5
  • 22
    • 80053620192 scopus 로고    scopus 로고
    • Crystal structure of amyloid precursorlike protein 1 and heparin complex suggests a dual role of heparin in E2 dimerization
    • Xue, Y., Lee, S., and Ha, Y. (2011) Crystal structure of amyloid precursorlike protein 1 and heparin complex suggests a dual role of heparin in E2 dimerization. Proc. Natl. Acad. Sci. U. S. A. 108, 16229-16234
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 16229-16234
    • Xue, Y.1    Lee, S.2    Ha, Y.3
  • 23
    • 0027981759 scopus 로고
    • Identification and regulation of the high affinity binding site of the Alzheimer's disease amyloid protein precursor (APP) to glycosaminoglycans
    • Multhaup, G. (1994) Identification and regulation of the high affinity binding site of the Alzheimer's disease amyloid protein precursor (APP) to glycosaminoglycans. Biochimie 76, 304-311
    • (1994) Biochimie , vol.76 , pp. 304-311
    • Multhaup, G.1
  • 24
    • 0028213567 scopus 로고
    • A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth
    • Small, D. H., Nurcombe, V., Reed, G., Clarris, H., Moir, R., Beyreuther, K., and Masters, C. L. (1994) A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth. J. Neurosci. 14, 2117-2127
    • (1994) J. Neurosci. , vol.14 , pp. 2117-2127
    • Small, D.H.1    Nurcombe, V.2    Reed, G.3    Clarris, H.4    Moir, R.5    Beyreuther, K.6    Masters, C.L.7
  • 25
    • 0029331504 scopus 로고
    • Characterization of the high affinity heparin binding site of the Alzheimer's disease-amyloid precursor protein (APP) and its enhancement by zinc (II)
    • Multhaup, G., Mechler, H., and Masters, C. L. (1995) Characterization of the high affinity heparin binding site of the Alzheimer's disease-amyloid precursor protein (APP) and its enhancement by zinc (II). J. Mol. Recognit. 8, 247-257
    • (1995) J. Mol. Recognit. , vol.8 , pp. 247-257
    • Multhaup, G.1    Mechler, H.2    Masters, C.L.3
  • 26
    • 84857355873 scopus 로고    scopus 로고
    • The amyloid precursor protein and its homologues: Structural and functional aspects of native and pathogenic oligomerization
    • Kaden, D., Munter, L. M., Reif, B., and Multhaup, G. (2012) The amyloid precursor protein and its homologues: structural and functional aspects of native and pathogenic oligomerization. Eur. J. Cell Biol. 91, 234-239
    • (2012) Eur. J. Cell Biol. , vol.91 , pp. 234-239
    • Kaden, D.1    Munter, L.M.2    Reif, B.3    Multhaup, G.4
  • 28
    • 0028177269 scopus 로고
    • The - A4 amyloid precursor protein binding to copper
    • Hesse, L., Beher, D., Masters, C. L., and Multhaup, G. (1994) The - A4 amyloid precursor protein binding to copper. FEBS Lett. 349, 109-116
    • (1994) FEBS Lett. , vol.349 , pp. 109-116
    • Hesse, L.1    Beher, D.2    Masters, C.L.3    Multhaup, G.4
  • 31
    • 3843146246 scopus 로고    scopus 로고
    • An efficient one-step site-directed and site-saturation mutagenesis protocol
    • Zheng, L., Baumann, U., and Reymond, J.-L. (2004) An efficient one-step site-directed and site-saturation mutagenesis protocol. Nucleic Acids Res. 32, e115
    • (2004) Nucleic Acids Res. , vol.32
    • Zheng, L.1    Baumann, U.2    Reymond, J.-L.3
  • 35
    • 44349093749 scopus 로고    scopus 로고
    • The protein fluorescence and structural toolkit: Database and programs for the analysis of protein fluorescence and structural data
    • Shen, C., Menon, R., Das, D., Bansal, N., Nahar, N., Guduru, N., Jaegle, S., Peckham, J., and Reshetnyak, Y. K. (2008) The protein fluorescence and structural toolkit: Database and programs for the analysis of protein fluorescence and structural data. Proteins 71, 1744-1754
    • (2008) Proteins , vol.71 , pp. 1744-1754
    • Shen, C.1    Menon, R.2    Das, D.3    Bansal, N.4    Nahar, N.5    Guduru, N.6    Jaegle, S.7    Peckham, J.8    Reshetnyak, Y.K.9
  • 36
    • 4143105782 scopus 로고    scopus 로고
    • The x-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain
    • Wang, Y., and Ha, Y. (2004) The x-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain. Mol. Cell 15, 343-353
    • (2004) Mol. Cell , vol.15 , pp. 343-353
    • Wang, Y.1    Ha, Y.2
  • 37
    • 79959284264 scopus 로고    scopus 로고
    • The E2 domains of APP and APLP1 share a conserved mode of dimerization
    • Lee, S., Xue, Y., Hu, J., Wang, Y., Liu, X., Demeler, B., and Ha, Y. (2011) The E2 domains of APP and APLP1 share a conserved mode of dimerization. Biochemistry 50, 5453-5464
    • (2011) Biochemistry , vol.50 , pp. 5453-5464
    • Lee, S.1    Xue, Y.2    Hu, J.3    Wang, Y.4    Liu, X.5    Demeler, B.6    Ha, Y.7
  • 38
    • 0037138362 scopus 로고    scopus 로고
    • EVH1 domains: Structure, function and interactions
    • Ball, L. J., Jarchau, T., Oschkinat, H., and Walter, U. (2002) EVH1 domains: structure, function and interactions. FEBS Lett. 513, 45-52
    • (2002) FEBS Lett. , vol.513 , pp. 45-52
    • Ball, L.J.1    Jarchau, T.2    Oschkinat, H.3    Walter, U.4
  • 39
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee, B. L., and Falchuk, K. H. (1993) The biochemical basis of zinc physiology. Physiol. Rev. 73, 79-118
    • (1993) Physiol. Rev. , vol.73 , pp. 79-118
    • Vallee, B.L.1    Falchuk, K.H.2
  • 41
    • 0013770181 scopus 로고
    • The concentrations of cobalt, copper, iron and zinc in some normal human tissues as determined by neutronactivation analysis
    • Parr, R. M., and Taylor, D. M. (1964) The concentrations of cobalt, copper, iron and zinc in some normal human tissues as determined by neutronactivation analysis. Biochem. J. 91, 424-431
    • (1964) Biochem. J. , vol.91 , pp. 424-431
    • Parr, R.M.1    Taylor, D.M.2
  • 42
    • 44849102395 scopus 로고    scopus 로고
    • Metals in neurobiology: Probing their chemistry and biology with molecular imaging
    • Que, E. L., Domaille, D. W., and Chang, C. J. (2008) Metals in neurobiology: probing their chemistry and biology with molecular imaging. Chem. Rev. 108, 1517-1549
    • (2008) Chem. Rev. , vol.108 , pp. 1517-1549
    • Que, E.L.1    Domaille, D.W.2    Chang, C.J.3
  • 44
    • 0000844197 scopus 로고
    • Surface topography of histidine residues: A facile probe by immobilized metal ion affinity chromatography
    • Hemdan, E. S., Zhao, Y. J., Sulkowski, E., and Porath, J. (1989) Surface topography of histidine residues: a facile probe by immobilized metal ion affinity chromatography. Proc. Natl. Acad. Sci. U. S. A. 86, 1811-1815
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 1811-1815
    • Hemdan, E.S.1    Zhao, Y.J.2    Sulkowski, E.3    Porath, J.4
  • 45
    • 0034682776 scopus 로고    scopus 로고
    • Metallochaperones, an intracellular shuttle service for metal ions
    • O'Halloran, T. V. (2000) Metallochaperones, an intracellular shuttle service for metal ions. J. Biol. Chem. 275, 25057-25060
    • (2000) J. Biol. Chem. , vol.275 , pp. 25057-25060
    • O'Halloran, T.V.1
  • 46
    • 0015596885 scopus 로고
    • Major glycoprotein of the human erythrocyte membrane: Evidence for an amphipathic molecular structure
    • Segrest, J. P., Kahane, I., Jackson, R. L., and Marchesi, V. T. (1973) Major glycoprotein of the human erythrocyte membrane: evidence for an amphipathic molecular structure. Arch. Biochem. Biophys. 155, 167-183
    • (1973) Arch. Biochem. Biophys. , vol.155 , pp. 167-183
    • Segrest, J.P.1    Kahane, I.2    Jackson, R.L.3    Marchesi, V.T.4
  • 49
    • 0035690880 scopus 로고    scopus 로고
    • Zinc coordination sphere in biochemical zinc sites
    • Auld, D. S. (2001) Zinc coordination sphere in biochemical zinc sites. Biometals 14, 271-313
    • (2001) Biometals , vol.14 , pp. 271-313
    • Auld, D.S.1
  • 50
    • 0037853148 scopus 로고    scopus 로고
    • Decorin binds fibrinogen in a Zn2-dependent interaction
    • Dugan, T. A., Yang, V. W., McQuillan, D. J., and Höök, M. (2003) Decorin binds fibrinogen in a Zn2-dependent interaction. J. Biol. Chem. 278, 13655-13662
    • (2003) J. Biol. Chem. , vol.278 , pp. 13655-13662
    • Dugan, T.A.1    Yang, V.W.2    McQuillan, D.J.3    Höök, M.4
  • 51
    • 77953566262 scopus 로고    scopus 로고
    • Zinc induces structural reorganization of gelatin binding domain from human fibronectin and affects collagen binding
    • Graille, M., Pagano, M., Rose, T., Ravaux, M. R., and van Tilbeurgh, H. (2010) Zinc induces structural reorganization of gelatin binding domain from human fibronectin and affects collagen binding. Structure 18, 710-718
    • (2010) Structure , vol.18 , pp. 710-718
    • Graille, M.1    Pagano, M.2    Rose, T.3    Ravaux, M.R.4    Van Tilbeurgh, H.5
  • 53
    • 84869232590 scopus 로고    scopus 로고
    • Copper signaling in the mammalian nervous system: Synaptic effects
    • Gaier, E. D., Eipper, B. A., and Mains, R. E. (2013) Copper signaling in the mammalian nervous system: synaptic effects. J. Neurosci. Res. 91, 2-19
    • (2013) J. Neurosci. Res. , vol.91 , pp. 2-19
    • Gaier, E.D.1    Eipper, B.A.2    Mains, R.E.3
  • 54
    • 79960155322 scopus 로고    scopus 로고
    • Dynamic action of neurometals at the synapse
    • Tamano, H., and Takeda, A. (2011) Dynamic action of neurometals at the synapse. Metallomics 3, 656-661
    • (2011) Metallomics , vol.3 , pp. 656-661
    • Tamano, H.1    Takeda, A.2
  • 55
    • 84855336131 scopus 로고    scopus 로고
    • Modulation of neuronal signal transduction and memory formation by synaptic zinc
    • Sindreu, C., and Storm, D. R. (2011) Modulation of neuronal signal transduction and memory formation by synaptic zinc. Front. Behav. Neurosci. 5, 68
    • (2011) Front. Behav. Neurosci. , vol.5 , pp. 68
    • Sindreu, C.1    Storm, D.R.2
  • 57
    • 0031777548 scopus 로고    scopus 로고
    • Design, total synthesis, and functional overexpression of the Candida rugosa lipl gene coding for a major industrial lipase
    • Brocca, S., Schmidt-Dannert, C., Lotti, M., Alberghina, L., and Schmid, R. D. (1998) Design, total synthesis, and functional overexpression of the Candida rugosa lipl gene coding for a major industrial lipase. Protein Sci. 7, 1415-1422
    • (1998) Protein Sci. , vol.7 , pp. 1415-1422
    • Brocca, S.1    Schmidt-Dannert, C.2    Lotti, M.3    Alberghina, L.4    Schmid, R.D.5
  • 59
    • 84862953172 scopus 로고    scopus 로고
    • Amyloid precursor protein revisited: Neuron-specific expression and highly stable nature of soluble derivatives
    • Guo, Q., Li, H., Gaddam, S. S., Justice, N. J., Robertson, C. S., and Zheng, H. (2012) Amyloid precursor protein revisited: neuron-specific expression and highly stable nature of soluble derivatives. J. Biol. Chem. 287, 2437-2445
    • (2012) J. Biol. Chem. , vol.287 , pp. 2437-2445
    • Guo, Q.1    Li, H.2    Gaddam, S.S.3    Justice, N.J.4    Robertson, C.S.5    Zheng, H.6
  • 62
    • 84862867237 scopus 로고    scopus 로고
    • Structural aspects and physiological consequences of APP/APLP transdimerization
    • Baumkötter, F., Wagner, K., Eggert, S., Wild, K., and Kins, S. (2012) Structural aspects and physiological consequences of APP/APLP transdimerization. Exp. Brain Res. 217, 389-395
    • (2012) Exp. Brain Res. , vol.217 , pp. 389-395
    • Baumkötter, F.1    Wagner, K.2    Eggert, S.3    Wild, K.4    Kins, S.5
  • 63
    • 0029015855 scopus 로고
    • Selective localization of amyloid precursor-like protein 1 in the cerebral cortex postsynaptic density
    • Kim, T. W., Wu, K., Xu, J. L., McAuliffe, G., Tanzi, R. E., Wasco, W., and Black, I. B. (1995) Selective localization of amyloid precursor-like protein 1 in the cerebral cortex postsynaptic density. Mol. Brain Res. 32, 36-44
    • (1995) Mol. Brain Res. , vol.32 , pp. 36-44
    • Kim, T.W.1    Wu, K.2    Xu, J.L.3    McAuliffe, G.4    Tanzi, R.E.5    Wasco, W.6    Black, I.B.7
  • 65
    • 0032079899 scopus 로고    scopus 로고
    • Post-translational processing and turnover kinetics of presynaptically targeted amyloid precursor superfamily proteins in the central nervous system
    • Lyckman, A. W., Confaloni, A. M., Thinakaran, G., Sisodia, S. S., and Moya, K. L. (1998) Post-translational processing and turnover kinetics of presynaptically targeted amyloid precursor superfamily proteins in the central nervous system. J. Biol. Chem. 273, 11100-11106
    • (1998) J. Biol. Chem. , vol.273 , pp. 11100-11106
    • Lyckman, A.W.1    Confaloni, A.M.2    Thinakaran, G.3    Sisodia, S.S.4    Moya, K.L.5
  • 67
    • 0032828711 scopus 로고    scopus 로고
    • Fragmentation of protonated oligopeptides XLDVLQ (X-L, H, K or R) by surface induced dissociation: Additional evidence for the "mobile proton" model
    • Gu, C., Somogyi, Á., Wysocki, V. H., and Medzihradszky, K. F. (1999) Fragmentation of protonated oligopeptides XLDVLQ (X-L, H, K or R) by surface induced dissociation: additional evidence for the "mobile proton" model. Anal. Chim. Acta 397, 247-256
    • (1999) Anal. Chim. Acta , vol.397 , pp. 247-256
    • Gu, C.1    Somogyi, Á.2    Wysocki, V.H.3    Medzihradszky, K.F.4
  • 68
    • 0036636707 scopus 로고    scopus 로고
    • Sequence dependent fragmentation of peptides generated by MALDI quadrupole time-of-flight (MALDI Q-TOF) mass spectrometry and its implications for protein identification
    • Wattenberg, A., Organ, A. J., Schneider, K., Tyldesley, R., Bordoli, R., and Bateman, R. H. (2002) Sequence dependent fragmentation of peptides generated by MALDI quadrupole time-of-flight (MALDI Q-TOF) mass spectrometry and its implications for protein identification. J. Am. Soc. Mass Spectrom. 13, 772-783
    • (2002) J. Am. Soc. Mass Spectrom. , vol.13 , pp. 772-783
    • Wattenberg, A.1    Organ, A.J.2    Schneider, K.3    Tyldesley, R.4    Bordoli, R.5    Bateman, R.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.