메뉴 건너뛰기




Volumn 584, Issue 18, 2010, Pages 3936-3942

MEGF10 functions as a receptor for the uptake of amyloid-β

Author keywords

Alzheimer's disease; Amyloid ; Endocytosis; Lipid raft pathway; MEGF10

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; MEMBRANE PROTEIN; MULTIPLE EPIDERMAL GROWTH FACTOR LIKE DOMAIN 10 PROTEIN; PROTEIN ANTIBODY; PROTEIN MEGF10; UNCLASSIFIED DRUG; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); CHOLESTEROL; MEGF10, HUMAN; PEPTIDE FRAGMENT;

EID: 77956898818     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.08.050     Document Type: Article
Times cited : (36)

References (33)
  • 1
    • 0036441486 scopus 로고    scopus 로고
    • A cell biological perspective on Alzheimer's disease
    • Annaert W., De Strooper B. A cell biological perspective on Alzheimer's disease. Annu. Rev. Cell Dev. Biol. 2002, 18:25-51.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 25-51
    • Annaert, W.1    De Strooper, B.2
  • 2
    • 0035943345 scopus 로고    scopus 로고
    • A portrait of Alzheimer secretases - new features and familiar faces
    • Esler W.P., Wolfe M.S. A portrait of Alzheimer secretases - new features and familiar faces. Science 2001, 293:1449-1454.
    • (2001) Science , vol.293 , pp. 1449-1454
    • Esler, W.P.1    Wolfe, M.S.2
  • 3
    • 0034568802 scopus 로고    scopus 로고
    • Intramembrane proteolysis by presenilins
    • Steiner H., Haass C. Intramembrane proteolysis by presenilins. Nat. Rev. Mol. Cell Biol. 2000, 1:217-224.
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 217-224
    • Steiner, H.1    Haass, C.2
  • 4
    • 5344240284 scopus 로고    scopus 로고
    • Amyloid-beta precursor protein processing in neurodegeneration
    • Wilquet V., De Strooper B. Amyloid-beta precursor protein processing in neurodegeneration. Curr. Opin. Neurobiol. 2004, 14:582-588.
    • (2004) Curr. Opin. Neurobiol. , vol.14 , pp. 582-588
    • Wilquet, V.1    De Strooper, B.2
  • 5
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett J.T., Lansbury P.T. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?. Cell 1993, 73:1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 6
    • 4444276735 scopus 로고    scopus 로고
    • Clearance of Alzheimer's Abeta peptide: the many roads to perdition
    • Tanzi R.E., Moir R.D., Wagner S.L. Clearance of Alzheimer's Abeta peptide: the many roads to perdition. Neuron 2004, 43:605-608.
    • (2004) Neuron , vol.43 , pp. 605-608
    • Tanzi, R.E.1    Moir, R.D.2    Wagner, S.L.3
  • 7
    • 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 2005, 120:545-555.
    • (2005) Cell , vol.120 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 8
    • 0035958015 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro
    • Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O. Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2001, 8:85-95.
    • (2001) DNA Res. , vol.8 , pp. 85-95
    • Nagase, T.1    Nakayama, M.2    Nakajima, D.3    Kikuno, R.4    Ohara, O.5
  • 10
    • 34249987983 scopus 로고    scopus 로고
    • The mammalian Ced-1 ortholog MEGF10/KIAA1780 displays a novel adhesion pattern
    • Suzuki E., Nakayama M. The mammalian Ced-1 ortholog MEGF10/KIAA1780 displays a novel adhesion pattern. Exp. Cell Res. 2007, 313:2451-2464.
    • (2007) Exp. Cell Res. , vol.313 , pp. 2451-2464
    • Suzuki, E.1    Nakayama, M.2
  • 11
    • 34648837917 scopus 로고    scopus 로고
    • MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin assembly protein complex 2 medium chain and induces large vacuole formation
    • Suzuki E., Nakayama M. MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin assembly protein complex 2 medium chain and induces large vacuole formation. Exp. Cell Res. 2007, 313:3729-3742.
    • (2007) Exp. Cell Res. , vol.313 , pp. 3729-3742
    • Suzuki, E.1    Nakayama, M.2
  • 12
    • 38149129457 scopus 로고    scopus 로고
    • A transcriptome database for astrocytes, neurons, and oligodendrocytes: a new resource for understanding brain development and function
    • Cahoy J.D., et al. A transcriptome database for astrocytes, neurons, and oligodendrocytes: a new resource for understanding brain development and function. J. Neurosci. 2008, 28:264-278.
    • (2008) J. Neurosci. , vol.28 , pp. 264-278
    • Cahoy, J.D.1
  • 14
    • 16044366039 scopus 로고    scopus 로고
    • Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1
    • Duff K., et al. Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1. Nature 1996, 383:710-713.
    • (1996) Nature , vol.383 , pp. 710-713
    • Duff, K.1
  • 15
    • 70350463858 scopus 로고    scopus 로고
    • C1q tumor necrosis factor alpha-related protein isoform 5 is increased in mitochondrial DNA-depleted myocytes and activates AMP-activated protein kinase
    • Park S.Y., Choi J.H., Ryu H.S., Pak Y.K., Park K.S., Lee H.K., Lee W. C1q tumor necrosis factor alpha-related protein isoform 5 is increased in mitochondrial DNA-depleted myocytes and activates AMP-activated protein kinase. J. Biol. Chem. 2009, 284:27780-27789.
    • (2009) J. Biol. Chem. , vol.284 , pp. 27780-27789
    • Park, S.Y.1    Choi, J.H.2    Ryu, H.S.3    Pak, Y.K.4    Park, K.S.5    Lee, H.K.6    Lee, W.7
  • 16
    • 34247894107 scopus 로고    scopus 로고
    • Evidence of a role for lactadherin in Alzheimer's disease
    • Boddaert J., et al. Evidence of a role for lactadherin in Alzheimer's disease. Am. J. Pathol. 2007, 170:921-929.
    • (2007) Am. J. Pathol. , vol.170 , pp. 921-929
    • Boddaert, J.1
  • 17
    • 0030607177 scopus 로고    scopus 로고
    • Rapid cellular uptake of Alzheimer amyloid betaA4 peptide by cultured human neuroblastoma cells
    • Ida N., Masters C.L., Beyreuther K. Rapid cellular uptake of Alzheimer amyloid betaA4 peptide by cultured human neuroblastoma cells. FEBS Lett. 1996, 394:174-178.
    • (1996) FEBS Lett. , vol.394 , pp. 174-178
    • Ida, N.1    Masters, C.L.2    Beyreuther, K.3
  • 18
    • 29144514689 scopus 로고    scopus 로고
    • Clathrin-independent endocytosis: new insights into caveolae and non-caveolar lipid raft carriers
    • Kirkham M., Parton R.G. Clathrin-independent endocytosis: new insights into caveolae and non-caveolar lipid raft carriers. Biochim. Biophys. Acta 2005, 1746:349-363.
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 349-363
    • Kirkham, M.1    Parton, R.G.2
  • 19
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • Pelkmans L., Kartenbeck J., Helenius A. Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat. Cell Biol. 2001, 3:473-483.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 20
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • Ehehalt R., Keller P., Haass C., Thiele C., Simons K. Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J. Cell Biol. 2003, 160:113-123.
    • (2003) J. Cell Biol. , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 21
    • 0036479204 scopus 로고    scopus 로고
    • Caveolin-1 is a negative regulator of caveolae-mediated endocytosis to the endoplasmic reticulum
    • Le P.U., Guay G., Altschuler Y., Nabi I.R. Caveolin-1 is a negative regulator of caveolae-mediated endocytosis to the endoplasmic reticulum. J. Biol. Chem. 2002, 277:3371-3379.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3371-3379
    • Le, P.U.1    Guay, G.2    Altschuler, Y.3    Nabi, I.R.4
  • 23
    • 70450273117 scopus 로고    scopus 로고
    • Receptor-associated protein interacts with amyloid-beta peptide and promotes its cellular uptake
    • Kanekiyo T., Bu G. Receptor-associated protein interacts with amyloid-beta peptide and promotes its cellular uptake. J. Biol. Chem. 2009, 284:33352-33359.
    • (2009) J. Biol. Chem. , vol.284 , pp. 33352-33359
    • Kanekiyo, T.1    Bu, G.2
  • 24
    • 70549113177 scopus 로고    scopus 로고
    • Glial precursors clear sensory neuron corpses during development via Jedi-1, an engulfment receptor
    • Wu H.H., et al. Glial precursors clear sensory neuron corpses during development via Jedi-1, an engulfment receptor. Nat. Neurosci. 2009, 12:1534-1541.
    • (2009) Nat. Neurosci. , vol.12 , pp. 1534-1541
    • Wu, H.H.1
  • 25
    • 26844466658 scopus 로고    scopus 로고
    • Eater, a transmembrane protein mediating phagocytosis of bacterial pathogens in Drosophila
    • Kocks C., et al. Eater, a transmembrane protein mediating phagocytosis of bacterial pathogens in Drosophila. Cell 2005, 123:335-346.
    • (2005) Cell , vol.123 , pp. 335-346
    • Kocks, C.1
  • 26
    • 34250811784 scopus 로고    scopus 로고
    • LRP in amyloid-beta production and metabolism
    • Bu G., Cam J., Zerbinatti C. LRP in amyloid-beta production and metabolism. Ann. N. Y. Acad. Sci. 2006, 1086:35-53.
    • (2006) Ann. N. Y. Acad. Sci. , vol.1086 , pp. 35-53
    • Bu, G.1    Cam, J.2    Zerbinatti, C.3
  • 27
    • 84935851672 scopus 로고    scopus 로고
    • Mechanism of neuronal versus endothelial cell uptake of Alzheimer's disease amyloid beta protein
    • Kandimalla K.K., Scott O.G., Fulzele S., Davidson M.W., Poduslo J.F. Mechanism of neuronal versus endothelial cell uptake of Alzheimer's disease amyloid beta protein. PLoS ONE 2009, 4:e4627.
    • (2009) PLoS ONE , vol.4
    • Kandimalla, K.K.1    Scott, O.G.2    Fulzele, S.3    Davidson, M.W.4    Poduslo, J.F.5
  • 28
    • 37249062072 scopus 로고    scopus 로고
    • Internalization of beta-amyloid peptide by primary neurons in the absence of apolipoprotein E
    • Saavedra L., Mohamed A., Ma V., Kar S., de Chaves E.P. Internalization of beta-amyloid peptide by primary neurons in the absence of apolipoprotein E. J. Biol. Chem. 2007, 282:35722-35732.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35722-35732
    • Saavedra, L.1    Mohamed, A.2    Ma, V.3    Kar, S.4    de Chaves, E.P.5
  • 29
    • 30544439495 scopus 로고    scopus 로고
    • Sorting nexin 17 facilitates LRP recycling in the early endosome
    • van Kerkhof P., et al. Sorting nexin 17 facilitates LRP recycling in the early endosome. EMBO J. 2005, 24:2851-2861.
    • (2005) EMBO J. , vol.24 , pp. 2851-2861
    • van Kerkhof, P.1
  • 30
    • 45549102847 scopus 로고    scopus 로고
    • Adaptor protein sorting nexin 17 regulates amyloid precursor protein trafficking and processing in the early endosomes
    • Lee J., Retamal C., Cuitino L., Caruano-Yzermans A., Shin J.E., van Kerkhof P., Marzolo M.P., Bu G. Adaptor protein sorting nexin 17 regulates amyloid precursor protein trafficking and processing in the early endosomes. J. Biol. Chem. 2008, 283:11501-11508.
    • (2008) J. Biol. Chem. , vol.283 , pp. 11501-11508
    • Lee, J.1    Retamal, C.2    Cuitino, L.3    Caruano-Yzermans, A.4    Shin, J.E.5    van Kerkhof, P.6    Marzolo, M.P.7    Bu, G.8
  • 31
    • 0042357124 scopus 로고    scopus 로고
    • Autosomal recessive hypercholesterolemia protein interacts with and regulates the cell surface level of Alzheimer's amyloid beta precursor protein
    • Noviello C., Vito P., Lopez P., Abdallah M., D'Adamio L. Autosomal recessive hypercholesterolemia protein interacts with and regulates the cell surface level of Alzheimer's amyloid beta precursor protein. J. Biol. Chem. 2003, 278:31843-31847.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31843-31847
    • Noviello, C.1    Vito, P.2    Lopez, P.3    Abdallah, M.4    D'Adamio, L.5
  • 32
    • 40549088942 scopus 로고    scopus 로고
    • The FE65 proteins and Alzheimer's disease
    • McLoughlin D.M., Miller C.C. The FE65 proteins and Alzheimer's disease. J. Neurosci. Res. 2008, 86:744-754.
    • (2008) J. Neurosci. Res. , vol.86 , pp. 744-754
    • McLoughlin, D.M.1    Miller, C.C.2
  • 33
    • 0037023693 scopus 로고    scopus 로고
    • Interaction of CED-6/GULP, an adapter protein involved in engulfment of apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-related protein (LRP)
    • Su H.P., Nakada-Tsukui K., Tosello-Trampont A.C., Li Y., Bu G., Henson P.M., Ravichandran K.S. Interaction of CED-6/GULP, an adapter protein involved in engulfment of apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-related protein (LRP). J. Biol. Chem. 2002, 277:11772-11779.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11772-11779
    • Su, H.P.1    Nakada-Tsukui, K.2    Tosello-Trampont, A.C.3    Li, Y.4    Bu, G.5    Henson, P.M.6    Ravichandran, K.S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.