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Volumn 372, Issue 4, 2008, Pages 913-917

Rac1 changes the substrate specificity of γ-secretase between amyloid precursor protein and Notch1

Author keywords

secretase; Alzheimer's disease; Amyloid precursor protein; Intermembranous cleavage; Notch1; Presenilin 1; Rac1; Small G protein

Indexed keywords

AMYLOID PRECURSOR PROTEIN; GAMMA SECRETASE; NOTCH1 RECEPTOR; NSC 23766; PRESENILIN 1; PROTEIN INHIBITOR; RAC1 PROTEIN;

EID: 45449087037     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.05.153     Document Type: Article
Times cited : (23)

References (32)
  • 1
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, Pen-2, and Nicastrin with Presenilin generate an active γ-secretase complex
    • De Strooper B. Aph-1, Pen-2, and Nicastrin with Presenilin generate an active γ-secretase complex. Neuron 38 (2003) 9-12
    • (2003) Neuron , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 3
    • 0033535555 scopus 로고    scopus 로고
    • Neurogenic phenotypes and altered Notch processing in Drosophila Presenilin mutants
    • Ye Y., Lukinova N., and Fortini M.E. Neurogenic phenotypes and altered Notch processing in Drosophila Presenilin mutants. Nature 398 (1999) 525-529
    • (1999) Nature , vol.398 , pp. 525-529
    • Ye, Y.1    Lukinova, N.2    Fortini, M.E.3
  • 4
    • 0037424348 scopus 로고    scopus 로고
    • The Notch ligands, Delta1 and Jagged2, are substrates for presenilin-dependent "γ-secretase" cleavage
    • Ikeuchi T., and Sisodia S.S. The Notch ligands, Delta1 and Jagged2, are substrates for presenilin-dependent "γ-secretase" cleavage. J. Biol. Chem. 278 (2003) 7751-7754
    • (2003) J. Biol. Chem. , vol.278 , pp. 7751-7754
    • Ikeuchi, T.1    Sisodia, S.S.2
  • 5
    • 0035824391 scopus 로고    scopus 로고
    • γ-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase
    • Ni C.Y., Murphy M.P., Golde T.E., and Carpenter G. γ-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase. Science 294 (2001) 2179-2181
    • (2001) Science , vol.294 , pp. 2179-2181
    • Ni, C.Y.1    Murphy, M.P.2    Golde, T.E.3    Carpenter, G.4
  • 6
    • 0347785491 scopus 로고    scopus 로고
    • Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Abeta-like peptide
    • Lammich S., Okochi M., Takeda M., Kaether C., Capell A., Zimmer A.K., Edbauer D., Walter J., Steiner H., and Haass C. Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Abeta-like peptide. J. Biol. Chem. 277 (2002) 44754-44759
    • (2002) J. Biol. Chem. , vol.277 , pp. 44754-44759
    • Lammich, S.1    Okochi, M.2    Takeda, M.3    Kaether, C.4    Capell, A.5    Zimmer, A.K.6    Edbauer, D.7    Walter, J.8    Steiner, H.9    Haass, C.10
  • 9
    • 0033779635 scopus 로고    scopus 로고
    • Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1
    • Zhang Z., Nadeau P., Song W., Donovie D., Yuan M., Bernstein A., and Yankner B.A. Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1. Nat. Cell Biol. 2 (2000) 463-465
    • (2000) Nat. Cell Biol. , vol.2 , pp. 463-465
    • Zhang, Z.1    Nadeau, P.2    Song, W.3    Donovie, D.4    Yuan, M.5    Bernstein, A.6    Yankner, B.A.7
  • 14
    • 0031721511 scopus 로고    scopus 로고
    • Calsenilin: a calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment
    • Buxbaum J.D., Choi E., Luo Y., Lilliehook C., Crowley A.C., Merriam D.E., and Wasco W. Calsenilin: a calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment. Nat. Med. 4 (1998) 1177-1181
    • (1998) Nat. Med. , vol.4 , pp. 1177-1181
    • Buxbaum, J.D.1    Choi, E.2    Luo, Y.3    Lilliehook, C.4    Crowley, A.C.5    Merriam, D.E.6    Wasco, W.7
  • 16
    • 1642382833 scopus 로고    scopus 로고
    • Notch signaling: control of cell communication and cell fate
    • Lai E.C. Notch signaling: control of cell communication and cell fate. Development 131 (2004) 965-973
    • (2004) Development , vol.131 , pp. 965-973
    • Lai, E.C.1
  • 22
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: biochemistry and biology
    • Jaffe A.B., and Hall A. Rho GTPases: biochemistry and biology. Annu. Rev. Cell Dev. Biol. 21 (2005) 247-269
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 23
    • 0038660598 scopus 로고    scopus 로고
    • Platelet-derived growth factor induces the β-γ-secretase-mediated cleavage of Alzheimer's amyloid precursor protein through a Src-Rac-dependent pathway
    • Gianni D., Zambrano N., Bimonte M., Minopoli G., Mercken L., Talamo F., Scaloni A., and Russo T. Platelet-derived growth factor induces the β-γ-secretase-mediated cleavage of Alzheimer's amyloid precursor protein through a Src-Rac-dependent pathway. J. Biol. Chem. 278 (2003) 9290-9297
    • (2003) J. Biol. Chem. , vol.278 , pp. 9290-9297
    • Gianni, D.1    Zambrano, N.2    Bimonte, M.3    Minopoli, G.4    Mercken, L.5    Talamo, F.6    Scaloni, A.7    Russo, T.8
  • 24
    • 0034602967 scopus 로고    scopus 로고
    • Rac1 regulates interleukin 1-induced nuclear factor κB activation in an inhibitory protein κBα-independent manner by enhancing the ability of the p65 subunit to transactivate gene expression
    • Jefferies C.A., and O'Neill L.A. Rac1 regulates interleukin 1-induced nuclear factor κB activation in an inhibitory protein κBα-independent manner by enhancing the ability of the p65 subunit to transactivate gene expression. J. Biol. Chem. 275 (2000) 3114-3120
    • (2000) J. Biol. Chem. , vol.275 , pp. 3114-3120
    • Jefferies, C.A.1    O'Neill, L.A.2
  • 25
    • 0033813282 scopus 로고    scopus 로고
    • Rac1 inhibits TNF-alpha-induced endothelial cell apoptosis: dual regulation by reactive oxygen species
    • Deshpande S.S., Angkeow P., Huang J., Ozaki M., and Irani K. Rac1 inhibits TNF-alpha-induced endothelial cell apoptosis: dual regulation by reactive oxygen species. FASEB J. 14 (2000) 1705-1714
    • (2000) FASEB J. , vol.14 , pp. 1705-1714
    • Deshpande, S.S.1    Angkeow, P.2    Huang, J.3    Ozaki, M.4    Irani, K.5
  • 26
    • 0034774969 scopus 로고    scopus 로고
    • Presenilin-dependent gamma-secretase processing of beta-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch
    • Sastre M., Steiner H., Fuchs K., Capell A., Multhaup G., Condron M.M., Teplow D.B., and Haass C. Presenilin-dependent gamma-secretase processing of beta-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch. EMBO Rep. 2 (2001) 835-841
    • (2001) EMBO Rep. , vol.2 , pp. 835-841
    • Sastre, M.1    Steiner, H.2    Fuchs, K.3    Capell, A.4    Multhaup, G.5    Condron, M.M.6    Teplow, D.B.7    Haass, C.8
  • 27
    • 30744453036 scopus 로고    scopus 로고
    • ERK1/2 is an endogenous negative regulator of the γ-secretase activity
    • Kim S., Park H., Hong H.S., Baik E.J., Jung M.W., and Mook-Jung I. ERK1/2 is an endogenous negative regulator of the γ-secretase activity. FASEB J. 20 (2006) 157-159
    • (2006) FASEB J. , vol.20 , pp. 157-159
    • Kim, S.1    Park, H.2    Hong, H.S.3    Baik, E.J.4    Jung, M.W.5    Mook-Jung, I.6
  • 28
    • 0141483380 scopus 로고    scopus 로고
    • Regulated hyperaccumulation of presenilin-1 and the "γ-secretase" complex
    • Kim S., Ikeuchi T., Yu C., and Sisodia S.S. Regulated hyperaccumulation of presenilin-1 and the "γ-secretase" complex. J. Biol. Chem. 278 (2003) 33992-34002
    • (2003) J. Biol. Chem. , vol.278 , pp. 33992-34002
    • Kim, S.1    Ikeuchi, T.2    Yu, C.3    Sisodia, S.S.4
  • 30
    • 29644431788 scopus 로고    scopus 로고
    • γ-Secretase substrate selectivity can be modulated directly via interaction with a nucleotide-binding site
    • Fraering P.C., Ye W., LaVoie M.J., Ostaszewski B.L., Selkoe D.J., and Wolfe M.S. γ-Secretase substrate selectivity can be modulated directly via interaction with a nucleotide-binding site. J. Biol. Chem. 280 (2005) 41987-41996
    • (2005) J. Biol. Chem. , vol.280 , pp. 41987-41996
    • Fraering, P.C.1    Ye, W.2    LaVoie, M.J.3    Ostaszewski, B.L.4    Selkoe, D.J.5    Wolfe, M.S.6
  • 32
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley A.J., Paterson H.F., Johnston C.L., Diekmann D., and Hall A. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70 (1992) 401-410
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.