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Volumn 361, Issue 2, 2007, Pages 317-322

Fe65 does not stabilize AICD during activation of transcription in a luciferase assay

Author keywords

AICD; Amyloid precursor protein; Fe65; Luciferase; Transcription

Indexed keywords

2 PHENANTHROLINE; AMYLOID PRECURSOR PROTEIN; CYSTINE; LACTACYSTINE; LUCIFERASE; PHENANTHROLINE DERIVATIVE; PROTEASOME; PROTEIN FE65; UNCLASSIFIED DRUG;

EID: 34547540165     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.06.186     Document Type: Article
Times cited : (15)

References (33)
  • 1
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor
    • Buxbaum J.D., Liu K.N., Luo Y., Slack J.L., Stocking K.L., Peschon J.J., Johnson R.S., Castner B.J., Cerretti D.P., and Black R.A. Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor. J. Biol. Chem. 273 (1998) 27765-27767
    • (1998) J. Biol. Chem. , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1    Liu, K.N.2    Luo, Y.3    Slack, J.L.4    Stocking, K.L.5    Peschon, J.J.6    Johnson, R.S.7    Castner, B.J.8    Cerretti, D.P.9    Black, R.A.10
  • 2
    • 0242330374 scopus 로고    scopus 로고
    • ADAMs family members as amyloid precursor protein alpha-secretases
    • Allinson T.M., Parkin E.T., Turner A.J., and Hooper N.M. ADAMs family members as amyloid precursor protein alpha-secretases. J. Neurosci. Res. 74 (2003) 342-352
    • (2003) J. Neurosci. Res. , vol.74 , pp. 342-352
    • Allinson, T.M.1    Parkin, E.T.2    Turner, A.J.3    Hooper, N.M.4
  • 3
    • 0036736218 scopus 로고    scopus 로고
    • Amyloid precursor protein, presenilins, and alpha-synuclein: molecular pathogenesis and pharmacological applications in Alzheimer's disease
    • Suh Y.H., and Checler F. Amyloid precursor protein, presenilins, and alpha-synuclein: molecular pathogenesis and pharmacological applications in Alzheimer's disease. Pharmacol. Rev. 54 (2002) 469-525
    • (2002) Pharmacol. Rev. , vol.54 , pp. 469-525
    • Suh, Y.H.1    Checler, F.2
  • 4
    • 1442264828 scopus 로고    scopus 로고
    • Take five-BACE and the gamma-secretase quartet conduct Alzheimer's amyloid beta-peptide generation
    • Haass C. Take five-BACE and the gamma-secretase quartet conduct Alzheimer's amyloid beta-peptide generation. EMBO J. 23 (2004) 483-488
    • (2004) EMBO J. , vol.23 , pp. 483-488
    • Haass, C.1
  • 5
    • 0035929554 scopus 로고    scopus 로고
    • Distinct intramembrane cleavage of the beta-amyloid precursor protein family resembling gamma-secretase-like cleavage of Notch
    • Gu Y., Misonou H., Sato T., Dohmae N., Takio K., and Ihara Y. Distinct intramembrane cleavage of the beta-amyloid precursor protein family resembling gamma-secretase-like cleavage of Notch. J. Biol. Chem. 276 (2001) 35235-35238
    • (2001) J. Biol. Chem. , vol.276 , pp. 35235-35238
    • Gu, Y.1    Misonou, H.2    Sato, T.3    Dohmae, N.4    Takio, K.5    Ihara, Y.6
  • 6
    • 0142250857 scopus 로고    scopus 로고
    • Functional gamma-secretase complex assembly in Golgi/trans-Golgi network: interactions among presenilin, nicastrin, Aph1, Pen-2, and gamma-secretase substrates
    • Baulac S., LaVoie M.J., Kimberly W.T., Strahle J., Wolfe M.S., Selkoe D.J., and Xia W. Functional gamma-secretase complex assembly in Golgi/trans-Golgi network: interactions among presenilin, nicastrin, Aph1, Pen-2, and gamma-secretase substrates. Neurobiol. Dis. 14 (2003) 194-204
    • (2003) Neurobiol. Dis. , vol.14 , pp. 194-204
    • Baulac, S.1    LaVoie, M.J.2    Kimberly, W.T.3    Strahle, J.4    Wolfe, M.S.5    Selkoe, D.J.6    Xia, W.7
  • 8
    • 0033214675 scopus 로고    scopus 로고
    • Presenilins: molecular switches between proteolysis and signal transduction
    • Annaert W., and De Strooper B. Presenilins: molecular switches between proteolysis and signal transduction. Trends Neurosci. 22 (1999) 439-443
    • (1999) Trends Neurosci. , vol.22 , pp. 439-443
    • Annaert, W.1    De Strooper, B.2
  • 9
    • 0037118248 scopus 로고    scopus 로고
    • A RIP tide in neuronal signal transduction
    • Ebinu J.O., and Yankner B.A. A RIP tide in neuronal signal transduction. Neuron 34 (2002) 499-502
    • (2002) Neuron , vol.34 , pp. 499-502
    • Ebinu, J.O.1    Yankner, B.A.2
  • 11
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X., and Sudhof T.C. A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293 (2001) 115-120
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 12
    • 0029805132 scopus 로고    scopus 로고
    • The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein
    • Borg J.P., Ooi J., Levy E., and Margolis B. The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol. Cell. Biol. 16 (1996) 6229-6241
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6229-6241
    • Borg, J.P.1    Ooi, J.2    Levy, E.3    Margolis, B.4
  • 13
    • 0029598484 scopus 로고
    • The regions of the Fe65 protein homologous to the phosphotyrosine interaction/phosphotyrosine binding domain of Shc bind the intracellular domain of the Alzheimer's amyloid precursor protein
    • Fiore F., Zambrano N., Minopoli G., Donini V., Duilio A., and Russo T. The regions of the Fe65 protein homologous to the phosphotyrosine interaction/phosphotyrosine binding domain of Shc bind the intracellular domain of the Alzheimer's amyloid precursor protein. J. Biol. Chem. 270 (1995) 30853-30856
    • (1995) J. Biol. Chem. , vol.270 , pp. 30853-30856
    • Fiore, F.1    Zambrano, N.2    Minopoli, G.3    Donini, V.4    Duilio, A.5    Russo, T.6
  • 14
    • 2642582435 scopus 로고    scopus 로고
    • Dissection of amyloid-beta precursor protein-dependent transcriptional transactivation
    • Cao X., and Sudhof T.C. Dissection of amyloid-beta precursor protein-dependent transcriptional transactivation. J. Biol. Chem. 279 (2004) 24601-24611
    • (2004) J. Biol. Chem. , vol.279 , pp. 24601-24611
    • Cao, X.1    Sudhof, T.C.2
  • 15
    • 0034839287 scopus 로고    scopus 로고
    • The amyloid precursor protein (APP)-cytoplasmic fragment generated by gamma-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurones in culture
    • Cupers P., Orlans I., Craessaerts K., Annaert W., and De Strooper B. The amyloid precursor protein (APP)-cytoplasmic fragment generated by gamma-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurones in culture. J. Neurochem. 78 (2001) 1168-1178
    • (2001) J. Neurochem. , vol.78 , pp. 1168-1178
    • Cupers, P.1    Orlans, I.2    Craessaerts, K.3    Annaert, W.4    De Strooper, B.5
  • 17
    • 0035955693 scopus 로고    scopus 로고
    • The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner
    • Kimberly W.T., Zheng J.B., Guenette S.Y., and Selkoe D.J. The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner. J. Biol. Chem. 276 (2001) 40288-40292
    • (2001) J. Biol. Chem. , vol.276 , pp. 40288-40292
    • Kimberly, W.T.1    Zheng, J.B.2    Guenette, S.Y.3    Selkoe, D.J.4
  • 18
    • 5444275067 scopus 로고    scopus 로고
    • The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor
    • von Rotz R.C., Kohli B.M., Bosset J., Meier M., Suzuki T., Nitsch R.M., and Konietzko U. The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor. J. Cell Sci. 117 (2004) 4435-4448
    • (2004) J. Cell Sci. , vol.117 , pp. 4435-4448
    • von Rotz, R.C.1    Kohli, B.M.2    Bosset, J.3    Meier, M.4    Suzuki, T.5    Nitsch, R.M.6    Konietzko, U.7
  • 19
    • 33845324145 scopus 로고    scopus 로고
    • C-terminal fragments of amyloid precursor protein exert neurotoxicity by inducing glycogen synthase kinase-3beta expression
    • Kim H.S., Kim E.M., Lee J.P., Park C.H., Kim S., Seo J.H., Chang K.A., Yu E., Jeong S.J., Chong Y.H., and Suh Y.H. C-terminal fragments of amyloid precursor protein exert neurotoxicity by inducing glycogen synthase kinase-3beta expression. FASEB J. 17 (2003) 1951-1953
    • (2003) FASEB J. , vol.17 , pp. 1951-1953
    • Kim, H.S.1    Kim, E.M.2    Lee, J.P.3    Park, C.H.4    Kim, S.5    Seo, J.H.6    Chang, K.A.7    Yu, E.8    Jeong, S.J.9    Chong, Y.H.10    Suh, Y.H.11
  • 20
    • 0037067655 scopus 로고    scopus 로고
    • Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein
    • Baek S.H., Ohgi K.A., Rose D.W., Koo E.H., Glass C.K., and Rosenfeld M.G. Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein. Cell 110 (2002) 55-67
    • (2002) Cell , vol.110 , pp. 55-67
    • Baek, S.H.1    Ohgi, K.A.2    Rose, D.W.3    Koo, E.H.4    Glass, C.K.5    Rosenfeld, M.G.6
  • 21
    • 33645218231 scopus 로고    scopus 로고
    • A dominant role for FE65 (APBB1) in nuclear signaling
    • Yang Z., Cool B.H., Martin G.M., and Hu Q. A dominant role for FE65 (APBB1) in nuclear signaling. J. Biol. Chem. 281 (2006) 4207-4214
    • (2006) J. Biol. Chem. , vol.281 , pp. 4207-4214
    • Yang, Z.1    Cool, B.H.2    Martin, G.M.3    Hu, Q.4
  • 22
    • 33745584643 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of amyloid precursor protein and regulation of expression of putative target genes
    • Hebert S.S., Serneels L., Tolia A., Craessaerts K., Derks C., Filippov M.A., Muller U., and De Strooper B. Regulated intramembrane proteolysis of amyloid precursor protein and regulation of expression of putative target genes. EMBO Rep. 7 (2006) 739-745
    • (2006) EMBO Rep. , vol.7 , pp. 739-745
    • Hebert, S.S.1    Serneels, L.2    Tolia, A.3    Craessaerts, K.4    Derks, C.5    Filippov, M.A.6    Muller, U.7    De Strooper, B.8
  • 23
    • 0034695572 scopus 로고    scopus 로고
    • The role of presenilin-1 in the gamma-secretase cleavage of the amyloid precursor protein of Alzheimer's disease
    • Octave J.N., Essalmani R., Tasiaux B., Menager J., Czech C., and Mercken L. The role of presenilin-1 in the gamma-secretase cleavage of the amyloid precursor protein of Alzheimer's disease. J. Biol. Chem. 275 (2000) 1525-1528
    • (2000) J. Biol. Chem. , vol.275 , pp. 1525-1528
    • Octave, J.N.1    Essalmani, R.2    Tasiaux, B.3    Menager, J.4    Czech, C.5    Mercken, L.6
  • 25
    • 16844374267 scopus 로고    scopus 로고
    • Endoproteolytic cleavage of FE65 converts the adaptor protein to a potent suppressor of the sAPPalpha pathway in primates
    • Hu Q., Wang L., Yang Z., Cool B.H., Zitnik G., and Martin G.M. Endoproteolytic cleavage of FE65 converts the adaptor protein to a potent suppressor of the sAPPalpha pathway in primates. J. Biol. Chem. 280 (2005) 12548-12558
    • (2005) J. Biol. Chem. , vol.280 , pp. 12548-12558
    • Hu, Q.1    Wang, L.2    Yang, Z.3    Cool, B.H.4    Zitnik, G.5    Martin, G.M.6
  • 26
    • 0034797234 scopus 로고    scopus 로고
    • The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from gamma-secretase
    • Nunan J., Shearman M.S., Checler F., Cappai R., Evin G., Beyreuther K., Masters C.L., and Small D.H. The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from gamma-secretase. Eur. J. Biochem. 268 (2001) 5329-5336
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5329-5336
    • Nunan, J.1    Shearman, M.S.2    Checler, F.3    Cappai, R.4    Evin, G.5    Beyreuther, K.6    Masters, C.L.7    Small, D.H.8
  • 28
    • 0037134505 scopus 로고    scopus 로고
    • Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD)
    • Edbauer D., Willem M., Lammich S., Steiner H., and Haass C. Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD). J. Biol. Chem. 277 (2002) 13389-13393
    • (2002) J. Biol. Chem. , vol.277 , pp. 13389-13393
    • Edbauer, D.1    Willem, M.2    Lammich, S.3    Steiner, H.4    Haass, C.5
  • 30
    • 20444403334 scopus 로고    scopus 로고
    • Physiological regulation of the beta-amyloid precursor protein signaling domain by c-Jun N-terminal kinase JNK3 during neuronal differentiation
    • Kimberly W.T., Zheng J.B., Town T., Flavell R.A., and Selkoe D.J. Physiological regulation of the beta-amyloid precursor protein signaling domain by c-Jun N-terminal kinase JNK3 during neuronal differentiation. J. Neurosci. 25 (2005) 5533-5543
    • (2005) J. Neurosci. , vol.25 , pp. 5533-5543
    • Kimberly, W.T.1    Zheng, J.B.2    Town, T.3    Flavell, R.A.4    Selkoe, D.J.5
  • 31
    • 0036677928 scopus 로고    scopus 로고
    • Direct visualization of the gamma secretase-generated carboxyl-terminal domain of the amyloid precursor protein: association with Fe65 and translocation to the nucleus
    • Kinoshita A., Whelan C.M., Smith C.J., Berezovska O., and Hyman B.T. Direct visualization of the gamma secretase-generated carboxyl-terminal domain of the amyloid precursor protein: association with Fe65 and translocation to the nucleus. J. Neurochem. 82 (2002) 839-847
    • (2002) J. Neurochem. , vol.82 , pp. 839-847
    • Kinoshita, A.1    Whelan, C.M.2    Smith, C.J.3    Berezovska, O.4    Hyman, B.T.5
  • 32
    • 33646732989 scopus 로고    scopus 로고
    • Role of APP phosphorylation in FE65-dependent gene transactivation mediated by AICD
    • Nakaya T., and Suzuki T. Role of APP phosphorylation in FE65-dependent gene transactivation mediated by AICD. Genes Cells 11 (2006) 633-645
    • (2006) Genes Cells , vol.11 , pp. 633-645
    • Nakaya, T.1    Suzuki, T.2
  • 33
    • 33846807664 scopus 로고    scopus 로고
    • Response to: Pardossi-Piquard et al., Presenilin-dependent transcriptional control of the abeta-degrading enzyme neprilysin by intracellular domains of betaAPP and APLP, Neuron 46, 541-554
    • Chen A.C., and Selkoe D.J. Response to: Pardossi-Piquard et al., Presenilin-dependent transcriptional control of the abeta-degrading enzyme neprilysin by intracellular domains of betaAPP and APLP, Neuron 46, 541-554. Neuron 53 (2007) 479-483
    • (2007) Neuron , vol.53 , pp. 479-483
    • Chen, A.C.1    Selkoe, D.J.2


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