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Volumn 10, Issue 8, 2015, Pages 1925-1931

γ-Secretase Inhibitors and Modulators Induce Distinct Conformational Changes in the Active Sites of γ-Secretase and Signal Peptide Peptidase

Author keywords

[No Author keywords available]

Indexed keywords

CENTRAL NERVOUS SYSTEM AGENTS; GAMMA SECRETASE; GAMMA SECRETASE INHIBITOR; GAMMA SECRETASE MODULATOR; PEPTIDASE; SIGNAL PEPTIDE; UNCLASSIFIED DRUG; ASPARTIC PROTEINASE; BENZOPHENONE DERIVATIVE; MOLECULAR LIBRARY; SECRETASE; SIGNAL PEPTIDE PEPTIDASE;

EID: 84939804034     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.5b00321     Document Type: Article
Times cited : (14)

References (48)
  • 1
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • Brown, M. S., Ye, J., Rawson, R. B., and Goldstein, J. L. (2000) Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans Cell 100, 391-398
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 2
    • 0035576260 scopus 로고    scopus 로고
    • Intramembrane proteolysis of signal peptides: An essential step in the generation of HLA-E epitopes
    • Lemberg, M. K., Bland, F. A., Weihofen, A., Braud, V. M., and Martoglio, B. (2001) Intramembrane proteolysis of signal peptides: an essential step in the generation of HLA-E epitopes J. Immunol. 167, 6441-6446
    • (2001) J. Immunol. , vol.167 , pp. 6441-6446
    • Lemberg, M.K.1    Bland, F.A.2    Weihofen, A.3    Braud, V.M.4    Martoglio, B.5
  • 3
    • 0036683052 scopus 로고    scopus 로고
    • Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets
    • McLauchlan, J., Lemberg, M. K., Hope, G., and Martoglio, B. (2002) Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets EMBO J. 21, 3980-3988
    • (2002) EMBO J. , vol.21 , pp. 3980-3988
    • McLauchlan, J.1    Lemberg, M.K.2    Hope, G.3    Martoglio, B.4
  • 4
    • 79959636033 scopus 로고    scopus 로고
    • The many substrates of presenilin/gamma-secretase
    • Haapasalo, A. and Kovacs, D. M. (2011) The many substrates of presenilin/gamma-secretase J. Alzheimers Dis. 25, 3-28
    • (2011) J. Alzheimers Dis. , vol.25 , pp. 3-28
    • Haapasalo, A.1    Kovacs, D.M.2
  • 5
    • 84877762179 scopus 로고    scopus 로고
    • Development and mechanism of gamma-secretase modulators for Alzheimers disease
    • Crump, C. J., Johnson, D. S., and Li, Y. M. (2013) Development and mechanism of gamma-secretase modulators for Alzheimers disease Biochemistry 52, 3197-3216
    • (2013) Biochemistry , vol.52 , pp. 3197-3216
    • Crump, C.J.1    Johnson, D.S.2    Li, Y.M.3
  • 6
    • 67649794833 scopus 로고    scopus 로고
    • Intramembrane proteolysis by signal peptide peptidases: A comparative discussion of GXGD-type aspartyl proteases
    • Fluhrer, R., Steiner, H., and Haass, C. (2009) Intramembrane proteolysis by signal peptide peptidases: a comparative discussion of GXGD-type aspartyl proteases J. Biol. Chem. 284, 13975-13979
    • (2009) J. Biol. Chem. , vol.284 , pp. 13975-13979
    • Fluhrer, R.1    Steiner, H.2    Haass, C.3
  • 7
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, Pen-2, and Nicastrin with Presenilin generate an active gamma-Secretase complex
    • De Strooper, B. (2003) Aph-1, Pen-2, and Nicastrin with Presenilin generate an active gamma-Secretase complex Neuron 38, 9-12
    • (2003) Neuron , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 10
    • 84922420350 scopus 로고    scopus 로고
    • Complex regulation of gamma-secretase: From obligatory to modulatory subunits
    • Gertsik, N., Chiu, D., and Li, Y. M. (2014) Complex regulation of gamma-secretase: from obligatory to modulatory subunits Front. Aging Neurosci. 6, 342
    • (2014) Front. Aging Neurosci. , vol.6 , pp. 342
    • Gertsik, N.1    Chiu, D.2    Li, Y.M.3
  • 11
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity
    • Wolfe, M. S., Xia, W., Ostaszewski, B. L., Diehl, T. S., Kimberly, W. T., and Selkoe, D. J. (1999) Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity Nature 398, 513-517
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 15
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • Weihofen, A., Binns, K., Lemberg, M. K., Ashman, K., and Martoglio, B. (2002) Identification of signal peptide peptidase, a presenilin-type aspartic protease Science 296, 2215-2218
    • (2002) Science , vol.296 , pp. 2215-2218
    • Weihofen, A.1    Binns, K.2    Lemberg, M.K.3    Ashman, K.4    Martoglio, B.5
  • 16
    • 5644240819 scopus 로고    scopus 로고
    • A signal peptide peptidase (SPP) reporter activity assay based on the cleavage of type II membrane protein substrates provides further evidence for an inverted orientation of the SPP active site relative to presenilin
    • Nyborg, A. C., Jansen, K., Ladd, T. B., Fauq, A., and Golde, T. E. (2004) A signal peptide peptidase (SPP) reporter activity assay based on the cleavage of type II membrane protein substrates provides further evidence for an inverted orientation of the SPP active site relative to presenilin J. Biol. Chem. 279, 43148-43156
    • (2004) J. Biol. Chem. , vol.279 , pp. 43148-43156
    • Nyborg, A.C.1    Jansen, K.2    Ladd, T.B.3    Fauq, A.4    Golde, T.E.5
  • 17
    • 10944270703 scopus 로고    scopus 로고
    • Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins
    • Friedmann, E., Lemberg, M. K., Weihofen, A., Dev, K. K., Dengler, U., Rovelli, G., and Martoglio, B. (2004) Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins J. Biol. Chem. 279, 50790-50798
    • (2004) J. Biol. Chem. , vol.279 , pp. 50790-50798
    • Friedmann, E.1    Lemberg, M.K.2    Weihofen, A.3    Dev, K.K.4    Dengler, U.5    Rovelli, G.6    Martoglio, B.7
  • 19
    • 2442446430 scopus 로고    scopus 로고
    • Signal peptide peptidase forms a homodimer that is labeled by an active site-directed gamma-secretase inhibitor
    • Nyborg, A. C., Kornilova, A. Y., Jansen, K., Ladd, T. B., Wolfe, M. S., and Golde, T. E. (2004) Signal peptide peptidase forms a homodimer that is labeled by an active site-directed gamma-secretase inhibitor J. Biol. Chem. 279, 15153-15160
    • (2004) J. Biol. Chem. , vol.279 , pp. 15153-15160
    • Nyborg, A.C.1    Kornilova, A.Y.2    Jansen, K.3    Ladd, T.B.4    Wolfe, M.S.5    Golde, T.E.6
  • 20
    • 34248162844 scopus 로고    scopus 로고
    • Signal peptide peptidase (SPP) dimer formation as assessed by fluorescence lifetime imaging microscopy (FLIM) in intact cells
    • Nyborg, A. C., Herl, L., Berezovska, O., Thomas, A. V., Ladd, T. B., Jansen, K., Hyman, B. T., and Golde, T. E. (2006) Signal peptide peptidase (SPP) dimer formation as assessed by fluorescence lifetime imaging microscopy (FLIM) in intact cells Mol. Neurodegener 1, 16
    • (2006) Mol. Neurodegener , vol.1 , pp. 16
    • Nyborg, A.C.1    Herl, L.2    Berezovska, O.3    Thomas, A.V.4    Ladd, T.B.5    Jansen, K.6    Hyman, B.T.7    Golde, T.E.8
  • 24
    • 84895079393 scopus 로고    scopus 로고
    • Development of CBAP-BPyne, a probe for gamma-secretase and presenilinase
    • Gertsik, N., Ballard, T. E., Am Ende, C. W., Johnson, D. S., and Li, Y. M. (2014) Development of CBAP-BPyne, a probe for gamma-secretase and presenilinase MedChemComm 5, 338-341
    • (2014) MedChemComm , vol.5 , pp. 338-341
    • Gertsik, N.1    Ballard, T.E.2    Am Ende, C.W.3    Johnson, D.S.4    Li, Y.M.5
  • 27
    • 76249118271 scopus 로고    scopus 로고
    • An APP inhibitory domain containing the Flemish mutation residue modulates gamma-secretase activity for Abeta production
    • Tian, Y., Bassit, B., Chau, D., and Li, Y. M. (2010) An APP inhibitory domain containing the Flemish mutation residue modulates gamma-secretase activity for Abeta production Nat. Struct. Mol. Biol. 17, 151-158
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 151-158
    • Tian, Y.1    Bassit, B.2    Chau, D.3    Li, Y.M.4
  • 28
    • 84861203709 scopus 로고    scopus 로고
    • Familial Alzheimer Disease Presenilin-1 Mutations Alter the Active Site Conformation of gamma-secretase
    • Chau, D. M., Crump, C. J., Villa, J. C., Scheinberg, D. A., and Li, Y. M. (2012) Familial Alzheimer Disease Presenilin-1 Mutations Alter the Active Site Conformation of gamma-secretase J. Biol. Chem. 287, 17288-17296
    • (2012) J. Biol. Chem. , vol.287 , pp. 17288-17296
    • Chau, D.M.1    Crump, C.J.2    Villa, J.C.3    Scheinberg, D.A.4    Li, Y.M.5
  • 30
    • 0034254585 scopus 로고    scopus 로고
    • L-685,458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid beta-protein precursor gamma-secretase activity
    • Shearman, M. S., Beher, D., Clarke, E. E., Lewis, H. D., Harrison, T., Hunt, P., Nadin, A., Smith, A. L., Stevenson, G., and Castro, J. L. (2000) L-685,458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid beta-protein precursor gamma-secretase activity Biochemistry 39, 8698-8704
    • (2000) Biochemistry , vol.39 , pp. 8698-8704
    • Shearman, M.S.1    Beher, D.2    Clarke, E.E.3    Lewis, H.D.4    Harrison, T.5    Hunt, P.6    Nadin, A.7    Smith, A.L.8    Stevenson, G.9    Castro, J.L.10
  • 32
    • 0034613193 scopus 로고    scopus 로고
    • Release of signal peptide fragments into the cytosol requires cleavage in the transmembrane region by a protease activity that is specifically blocked by a novel cysteine protease inhibitor
    • Weihofen, A., Lemberg, M. K., Ploegh, H. L., Bogyo, M., and Martoglio, B. (2000) Release of signal peptide fragments into the cytosol requires cleavage in the transmembrane region by a protease activity that is specifically blocked by a novel cysteine protease inhibitor J. Biol. Chem. 275, 30951-30956
    • (2000) J. Biol. Chem. , vol.275 , pp. 30951-30956
    • Weihofen, A.1    Lemberg, M.K.2    Ploegh, H.L.3    Bogyo, M.4    Martoglio, B.5
  • 33
    • 33745586176 scopus 로고    scopus 로고
    • Signal peptide peptidase: Biochemical properties and modulation by nonsteroidal antiinflammatory drugs
    • Sato, T., Nyborg, A. C., Iwata, N., Diehl, T. S., Saido, T. C., Golde, T. E., and Wolfe, M. S. (2006) Signal peptide peptidase: biochemical properties and modulation by nonsteroidal antiinflammatory drugs Biochemistry 45, 8649-8656
    • (2006) Biochemistry , vol.45 , pp. 8649-8656
    • Sato, T.1    Nyborg, A.C.2    Iwata, N.3    Diehl, T.S.4    Saido, T.C.5    Golde, T.E.6    Wolfe, M.S.7
  • 34
    • 57749120456 scopus 로고    scopus 로고
    • Distinct pharmacological effects of inhibitors of signal peptide peptidase and gamma-secretase
    • Sato, T., Ananda, K., Cheng, C. I., Suh, E. J., Narayanan, S., and Wolfe, M. S. (2008) Distinct pharmacological effects of inhibitors of signal peptide peptidase and gamma-secretase J. Biol. Chem. 283, 33287-33295
    • (2008) J. Biol. Chem. , vol.283 , pp. 33287-33295
    • Sato, T.1    Ananda, K.2    Cheng, C.I.3    Suh, E.J.4    Narayanan, S.5    Wolfe, M.S.6
  • 35
    • 5444256890 scopus 로고    scopus 로고
    • Stereoselective Synthesis of Photoreactive Peptidomimetic gamma-Secretase Inhibitors
    • Chun, J., Yin, Y. I., Yang, G., Tarassishin, L., and Li, Y. M. (2004) Stereoselective Synthesis of Photoreactive Peptidomimetic gamma-Secretase Inhibitors J. Org. Chem. 69, 7344-7347
    • (2004) J. Org. Chem. , vol.69 , pp. 7344-7347
    • Chun, J.1    Yin, Y.I.2    Yang, G.3    Tarassishin, L.4    Li, Y.M.5
  • 40
    • 77950420393 scopus 로고    scopus 로고
    • Characterization of an atypical gamma-secretase complex from hematopoietic origin
    • Placanica, L., Chien, J. W., and Li, Y. M. (2010) Characterization of an atypical gamma-secretase complex from hematopoietic origin Biochemistry 49, 2796-2804
    • (2010) Biochemistry , vol.49 , pp. 2796-2804
    • Placanica, L.1    Chien, J.W.2    Li, Y.M.3
  • 41
    • 77951905218 scopus 로고    scopus 로고
    • In vivo manifestation of Notch related phenotypes in zebrafish treated with Alzheimers amyloid reducing gamma-secretase inhibitors
    • Yang, T., Arslanova, D., Xu, X., Li, Y. M., and Xia, W. (2010) In vivo manifestation of Notch related phenotypes in zebrafish treated with Alzheimers amyloid reducing gamma-secretase inhibitors J. Neurochem. 113, 1200-1209
    • (2010) J. Neurochem. , vol.113 , pp. 1200-1209
    • Yang, T.1    Arslanova, D.2    Xu, X.3    Li, Y.M.4    Xia, W.5
  • 43
    • 84877762179 scopus 로고    scopus 로고
    • Development and Mechanism of γ-Secretase Modulators for Alzheimers Disease
    • Crump, C. J., Johnson, D. S., and Li, Y.-M. (2013) Development and Mechanism of γ-Secretase Modulators for Alzheimers Disease Biochemistry 52, 3197-3216
    • (2013) Biochemistry , vol.52 , pp. 3197-3216
    • Crump, C.J.1    Johnson, D.S.2    Li, Y.-M.3
  • 45
    • 6944250394 scopus 로고    scopus 로고
    • The Caenorhabditis elegans IMPAS gene, imp-2, is essential for development and is functionally distinct from related presenilins
    • Grigorenko, A. P., Moliaka, Y. K., Soto, M. C., Mello, C. C., and Rogaev, E. I. (2004) The Caenorhabditis elegans IMPAS gene, imp-2, is essential for development and is functionally distinct from related presenilins Proc. Natl. Acad. Sci. U. S. A. 101, 14955-14960
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 14955-14960
    • Grigorenko, A.P.1    Moliaka, Y.K.2    Soto, M.C.3    Mello, C.C.4    Rogaev, E.I.5
  • 46
    • 28244456207 scopus 로고    scopus 로고
    • Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3
    • Krawitz, P., Haffner, C., Fluhrer, R., Steiner, H., Schmid, B., and Haass, C. (2005) Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3 J. Biol. Chem. 280, 39515-39523
    • (2005) J. Biol. Chem. , vol.280 , pp. 39515-39523
    • Krawitz, P.1    Haffner, C.2    Fluhrer, R.3    Steiner, H.4    Schmid, B.5    Haass, C.6
  • 47
    • 20444429794 scopus 로고    scopus 로고
    • Drosophila signal peptide peptidase is an essential protease for larval development
    • Casso, D. J., Tanda, S., Biehs, B., Martoglio, B., and Kornberg, T. B. (2005) Drosophila signal peptide peptidase is an essential protease for larval development Genetics 170, 139-148
    • (2005) Genetics , vol.170 , pp. 139-148
    • Casso, D.J.1    Tanda, S.2    Biehs, B.3    Martoglio, B.4    Kornberg, T.B.5


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