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Volumn 21, Issue 9, 2015, Pages 1054-1059

APP intracellular domain-WAVE1 pathway reduces amyloid-β production

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; GAMMA SECRETASE INHIBITOR; MESSENGER RNA; SMALL INTERFERING RNA; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR AICD; UNCLASSIFIED DRUG; WAVE1 PROTEIN; WISKOTT ALDRICH SYNDROME PROTEIN;

EID: 84941022788     PISSN: 10788956     EISSN: 1546170X     Source Type: Journal    
DOI: 10.1038/nm.3924     Document Type: Article
Times cited : (33)

References (41)
  • 1
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypothesis: A genetic perspective
    • Tanzi, R.E. & Bertram, L. Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell 120, 545-555 (2005).
    • (2005) Cell , vol.120 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 2
    • 79952747862 scopus 로고    scopus 로고
    • Alzheimer's disease
    • Ballard, C. et al. Alzheimer's disease. Lancet 377, 1019-1031 (2011).
    • (2011) Lancet , vol.377 , pp. 1019-1031
    • Ballard, C.1
  • 3
    • 33845729059 scopus 로고    scopus 로고
    • The WASP-WAVE protein network: Connecting the membrane to the cytoskeleton
    • Takenawa, T. & Suetsugu, S. The WASP-WAVE protein network: connecting the membrane to the cytoskeleton. Nat. Rev. Mol. Cell Biol. 8, 37-48 (2007).
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 37-48
    • Takenawa, T.1    Suetsugu, S.2
  • 4
    • 0037452615 scopus 로고    scopus 로고
    • Loss of WAVE-1 causes sensorimotor retardation and reduced learning and memory in mice
    • Soderling, S.H. et al. Loss of WAVE-1 causes sensorimotor retardation and reduced learning and memory in mice. Proc. Natl. Acad. Sci. USA 100, 1723-1728 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1723-1728
    • Soderling, S.H.1
  • 5
    • 0037102301 scopus 로고    scopus 로고
    • Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
    • Eden, S., Rohatgi, R., Podtelejnikov, A.V., Mann, M. & Kirschner, M.W. Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature 418, 790-793 (2002).
    • (2002) Nature , vol.418 , pp. 790-793
    • Eden, S.1    Rohatgi, R.2    Podtelejnikov, A.V.3    Mann, M.4    Kirschner, M.W.5
  • 6
    • 33747482904 scopus 로고    scopus 로고
    • Phosphorylation of WAVE1 regulates actin polymerization and dendritic spine morphology
    • Kim, Y. et al. Phosphorylation of WAVE1 regulates actin polymerization and dendritic spine morphology. Nature 442, 814-817 (2006).
    • (2006) Nature , vol.442 , pp. 814-817
    • Kim, Y.1
  • 7
    • 0034048704 scopus 로고    scopus 로고
    • Molecular cloning of a novel apoptosis-related gene, human Nap1 (NCKAP1), and its possible relation to Alzheimer disease
    • Suzuki, T. et al. Molecular cloning of a novel apoptosis-related gene, human Nap1 (NCKAP1), and its possible relation to Alzheimer disease. Genomics 63, 246-254 (2000).
    • (2000) Genomics , vol.63 , pp. 246-254
    • Suzuki, T.1
  • 8
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's disease with plaques and tangles: Intracellular Aβ and synaptic dysfunction
    • Oddo, S. et al. Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Aβ and synaptic dysfunction. Neuron 39, 409-421 (2003).
    • (2003) Neuron , vol.39 , pp. 409-421
    • Oddo, S.1
  • 9
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice
    • Hsiao, K. et al. Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice. Science 274, 99-102 (1996).
    • (1996) Science , vol.274 , pp. 99-102
    • Hsiao, K.1
  • 10
    • 0028172238 scopus 로고
    • Metabolism of the "swedish" amyloid precursor protein variant in Madin-Darby canine kidney cells
    • Lo, A.C., Haass, C., Wagner, S.L., Teplow, D.B. & Sisodia, S.S. Metabolism of the "Swedish" amyloid precursor protein variant in Madin-Darby canine kidney cells. J. Biol. Chem. 269, 30966-30973 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 30966-30973
    • Lo, A.C.1    Haass, C.2    Wagner, S.L.3    Teplow, D.B.4    Sisodia, S.S.5
  • 11
    • 48349085043 scopus 로고    scopus 로고
    • The amyloid precursor protein intracellular domain (AICD) as modulator of gene expression, apoptosis, and cytoskeletal dynamics-relevance for Alzheimer's disease
    • Müller, T., Meyer, H.E., Egensperger, R. & Marcus, K. The amyloid precursor protein intracellular domain (AICD) as modulator of gene expression, apoptosis, and cytoskeletal dynamics-relevance for Alzheimer's disease. Prog. Neurobiol. 85, 393-406 (2008).
    • (2008) Prog. Neurobiol. , vol.85 , pp. 393-406
    • Müller, T.1    Meyer, H.E.2    Egensperger, R.3    Marcus, K.4
  • 13
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao, X. & Sudhof, T.C. A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293, 115-120 (2001).
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 14
    • 70350370474 scopus 로고    scopus 로고
    • Nuclear signaling by the APP intracellular domain occurs predominantly through the amyloidogenic processing pathway
    • Goodger, Z.V. et al. Nuclear signaling by the APP intracellular domain occurs predominantly through the amyloidogenic processing pathway. J. Cell Sci. 122, 3703-3714 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 3703-3714
    • Goodger, Z.V.1
  • 15
    • 78650669822 scopus 로고    scopus 로고
    • The transcriptionally active amyloid precursor protein (APP) intracellular domain is preferentially produced from the 695 isoform of APP in a β-secretase-dependent pathway
    • Belyaev, N.D. et al. The transcriptionally active amyloid precursor protein (APP) intracellular domain is preferentially produced from the 695 isoform of APP in a β-secretase-dependent pathway. J. Biol. Chem. 285, 41443-41454 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 41443-41454
    • Belyaev, N.D.1
  • 16
    • 84861497482 scopus 로고    scopus 로고
    • Evidence that the amyloid-β protein precursor intracellular domain, AICD, derives from β-secretase-generated C-terminal fragment
    • Flammang, B. et al. Evidence that the amyloid-β protein precursor intracellular domain, AICD, derives from β-secretase-generated C-terminal fragment. J. Alzheimers Dis. 30, 145-153 (2012).
    • (2012) J. Alzheimers Dis. , vol.30 , pp. 145-153
    • Flammang, B.1
  • 17
    • 84655166492 scopus 로고    scopus 로고
    • The physiology of the β-amyloid precursor protein intracellular domain AICD
    • Pardossi-Piquard, R. & Checler, F. The physiology of the β-amyloid precursor protein intracellular domain AICD. J. Neurochem. 120 (suppl. 1), 109-124 (2012).
    • (2012) J. Neurochem. , vol.120 , pp. 109-124
    • Pardossi-Piquard, R.1    Checler, F.2
  • 18
    • 58049089518 scopus 로고    scopus 로고
    • Neprilysin gene expression requires binding of the amyloid precursor protein intracellular domain to its promoter: Implications for Alzheimer disease
    • Belyaev, N.D., Nalivaeva, N.N., Makova, N.Z. & Turner, A.J. Neprilysin gene expression requires binding of the amyloid precursor protein intracellular domain to its promoter: implications for Alzheimer disease. EMBO Rep. 10, 94-100 (2009).
    • (2009) EMBO Rep. , vol.10 , pp. 94-100
    • Belyaev, N.D.1    Nalivaeva, N.N.2    Makova, N.Z.3    Turner, A.J.4
  • 19
    • 1642555780 scopus 로고    scopus 로고
    • Mutant presenilins specifically elevate the levels of the 42 residue β-amyloid peptide in vivo: Evidence for augmentation of a 42-specific? Secretase
    • Jankowsky, J.L. et al. Mutant presenilins specifically elevate the levels of the 42 residue β-amyloid peptide in vivo: evidence for augmentation of a 42-specific ? secretase. Hum. Mol. Genet. 13, 159-170 (2004).
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 159-170
    • Jankowsky, J.L.1
  • 20
    • 84860919373 scopus 로고    scopus 로고
    • Membrane trafficking pathways in Alzheimer's disease
    • Rajendran, L. & Annaert, W. Membrane trafficking pathways in Alzheimer's disease. Traffic 13, 759-770 (2012).
    • (2012) Traffic , vol.13 , pp. 759-770
    • Rajendran, L.1    Annaert, W.2
  • 21
    • 84857794759 scopus 로고    scopus 로고
    • Synergistic BAR-NPF interactions in actin-driven membrane remodeling
    • Suetsugu, S. & Gautreau, A. Synergistic BAR-NPF interactions in actin-driven membrane remodeling. Trends Cell Biol. 22, 141-150 (2012).
    • (2012) Trends Cell Biol. , vol.22 , pp. 141-150
    • Suetsugu, S.1    Gautreau, A.2
  • 22
    • 84255195050 scopus 로고    scopus 로고
    • Bridging membrane and cytoskeleton dynamics in the secretory and endocytic pathways
    • Anitei, M. & Hoflack, B. Bridging membrane and cytoskeleton dynamics in the secretory and endocytic pathways. Nat. Cell Biol. 14, 11-19 (2012).
    • (2012) Nat. Cell Biol. , vol.14 , pp. 11-19
    • Anitei, M.1    Hoflack, B.2
  • 23
    • 64149105182 scopus 로고    scopus 로고
    • Genetic control of human brain transcript expression in Alzheimer disease
    • Webster, J.A. et al. Genetic control of human brain transcript expression in Alzheimer disease. Am. J. Hum. Genet. 84, 445-458 (2009).
    • (2009) Am. J. Hum. Genet. , vol.84 , pp. 445-458
    • Webster, J.A.1
  • 24
    • 77953305556 scopus 로고    scopus 로고
    • Signaling pathways controlling the phosphorylation state of WAVE1, a regulator of actin polymerization
    • Ceglia, I., Kim, Y., Nairn, A.C. & Greengard, P. Signaling pathways controlling the phosphorylation state of WAVE1, a regulator of actin polymerization. J. Neurochem. 114, 182-190 (2010).
    • (2010) J. Neurochem. , vol.114 , pp. 182-190
    • Ceglia, I.1    Kim, Y.2    Nairn, A.C.3    Greengard, P.4
  • 25
    • 0344672942 scopus 로고    scopus 로고
    • APP processing and synaptic function
    • Kamenetz, F. et al. APP processing and synaptic function. Neuron 37, 925-937 (2003).
    • (2003) Neuron , vol.37 , pp. 925-937
    • Kamenetz, F.1
  • 26
    • 26844574739 scopus 로고    scopus 로고
    • NMDA receptor activation inhibits a-secretase and promotes neuronal amyloid-β production
    • Lesné, S. et al. NMDA receptor activation inhibits a-secretase and promotes neuronal amyloid-β production. J. Neurosci. 25, 9367-9377 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 9367-9377
    • Lesné, S.1
  • 27
    • 29144487182 scopus 로고    scopus 로고
    • Synaptic activity regulates interstitial fluid amyloid-β levels in vivo
    • Cirrito, J.R. et al. Synaptic activity regulates interstitial fluid amyloid-β levels in vivo. Neuron 48, 913-922 (2005).
    • (2005) Neuron , vol.48 , pp. 913-922
    • Cirrito, J.R.1
  • 28
    • 84857720147 scopus 로고    scopus 로고
    • AICD nuclear signaling and its possible contribution to Alzheimer's disease
    • Konietzko, U. AICD nuclear signaling and its possible contribution to Alzheimer's disease. Curr. Alzheimer Res. 9, 200-216 (2012).
    • (2012) Curr. Alzheimer Res. , vol.9 , pp. 200-216
    • Konietzko, U.1
  • 29
    • 84878946078 scopus 로고    scopus 로고
    • The amyloid precursor protein: A biochemical enigma in brain development, function and disease
    • Nalivaeva, N.N. & Turner, A.J. The amyloid precursor protein: a biochemical enigma in brain development, function and disease. FEBS Lett. 587, 2046-2054 (2013).
    • (2013) FEBS Lett. , vol.587 , pp. 2046-2054
    • Nalivaeva, N.N.1    Turner, A.J.2
  • 30
    • 0035871641 scopus 로고    scopus 로고
    • Stimulation of β-amyloid precursor protein trafficking by insulin reduces intraneuronal β-amyloid and requires mitogen-activated protein kinase signaling
    • Gasparini, L. et al. Stimulation of β-amyloid precursor protein trafficking by insulin reduces intraneuronal β-amyloid and requires mitogen-activated protein kinase signaling. J. Neurosci. 21, 2561-2570 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 2561-2570
    • Gasparini, L.1
  • 31
    • 77956303159 scopus 로고    scopus 로고
    • Gamma-secretase activating protein is a therapeutic target for Alzheimer's disease
    • He, G. et al. Gamma-secretase activating protein is a therapeutic target for Alzheimer's disease. Nature 467, 95-98 (2010).
    • (2010) Nature , vol.467 , pp. 95-98
    • He, G.1
  • 32
    • 32444434357 scopus 로고    scopus 로고
    • Presenilin-1 uses phospholipase D1 as a negative regulator of β-amyloid formation
    • Cai, D. et al. Presenilin-1 uses phospholipase D1 as a negative regulator of β-amyloid formation. Proc. Natl. Acad. Sci. USA 103, 1941-1946 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 1941-1946
    • Cai, D.1
  • 33
    • 0037474287 scopus 로고    scopus 로고
    • Presenilin-1 regulates intracellular trafficking and cell surface delivery of β-amyloid precursor protein
    • Cai, D. et al. Presenilin-1 regulates intracellular trafficking and cell surface delivery of β-amyloid precursor protein. J. Biol. Chem. 278, 3446-3454 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 3446-3454
    • Cai, D.1
  • 34
    • 0141886295 scopus 로고    scopus 로고
    • Differential roles of WAVE1 and WAVE2 in dorsal and peripheral ruffle formation for fibroblast cell migration
    • Suetsugu, S., Yamazaki, D., Kurisu, S. & Takenawa, T. Differential roles of WAVE1 and WAVE2 in dorsal and peripheral ruffle formation for fibroblast cell migration. Dev. Cell 5, 595-609 (2003).
    • (2003) Dev. Cell , vol.5 , pp. 595-609
    • Suetsugu, S.1    Yamazaki, D.2    Kurisu, S.3    Takenawa, T.4
  • 35
    • 15844425969 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo
    • Thinakaran, G. et al. Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron 17, 181-190 (1996).
    • (1996) Neuron , vol.17 , pp. 181-190
    • Thinakaran, G.1
  • 36
    • 0025296205 scopus 로고
    • Processing of Alzheimer β/A4 amyloid precursor protein: Modulation by agents that regulate protein phosphorylation
    • Buxbaum, J.D. et al. Processing of Alzheimer β/A4 amyloid precursor protein: modulation by agents that regulate protein phosphorylation. Proc. Natl. Acad. Sci. USA 87, 6003-6006 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6003-6006
    • Buxbaum, J.D.1
  • 37
    • 0036903024 scopus 로고    scopus 로고
    • The WRP component of the WAVE-1 complex attenuates Rac-mediated signalling
    • Soderling, S.H. et al. The WRP component of the WAVE-1 complex attenuates Rac-mediated signalling. Nat. Cell Biol. 4, 970-975 (2002).
    • (2002) Nat. Cell Biol. , vol.4 , pp. 970-975
    • Soderling, S.H.1
  • 38
    • 0029942495 scopus 로고    scopus 로고
    • Metabolism of the "swedish" amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the "beta-secretase" site occurs in the Golgi apparatus
    • Thinakaran, G., Teplow, D.B., Siman, R., Greenberg, B. & Sisodia, S.S. Metabolism of the "Swedish" amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the "beta-secretase" site occurs in the Golgi apparatus. J. Biol. Chem. 271, 9390-9397 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 9390-9397
    • Thinakaran, G.1    Teplow, D.B.2    Siman, R.3    Greenberg, B.4    Sisodia, S.S.5
  • 39
    • 0032463037 scopus 로고    scopus 로고
    • Pulse-chase experiments revealed β-secretase cleavage from immature full-length amyloid precursor protein harboring the Swedish mutation. Implications for distinct pathways
    • Urmoneit, B., Turner, J. & Dyrks, T. Pulse-chase experiments revealed β-secretase cleavage from immature full-length amyloid precursor protein harboring the Swedish mutation. Implications for distinct pathways. J. Mol. Neurosci. 11, 141-150 (1998).
    • (1998) J. Mol. Neurosci. , vol.11 , pp. 141-150
    • Urmoneit, B.1    Turner, J.2    Dyrks, T.3
  • 40
    • 34848883642 scopus 로고    scopus 로고
    • Life-long environmental enrichment differentially affects the mnemonic response to estrogen in young, middle-aged, and aged female mice
    • Gresack, J.E., Kerr, K.M. & Frick, K.M. Life-long environmental enrichment differentially affects the mnemonic response to estrogen in young, middle-aged, and aged female mice. Neurobiol. Learn. Mem. 88, 393-408 (2007).
    • (2007) Neurobiol. Learn. Mem. , vol.88 , pp. 393-408
    • Gresack, J.E.1    Kerr, K.M.2    Frick, K.M.3
  • 41
    • 35148819275 scopus 로고    scopus 로고
    • Age-dependent effects of environmental enrichment on spatial reference memory in male mice
    • Harburger, L.L., Lambert, T.J. & Frick, K.M. Age-dependent effects of environmental enrichment on spatial reference memory in male mice. Behav. Brain Res. 185, 43-48 (2007).
    • (2007) Behav. Brain Res. , vol.185 , pp. 43-48
    • Harburger, L.L.1    Lambert, T.J.2    Frick, K.M.3


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