메뉴 건너뛰기




Volumn 1, Issue 1, 2006, Pages

Signal peptide peptidase (SPP) dimer formation as assessed by fluorescence lifetime imaging microscopy (FLIM) in intact cells

Author keywords

[No Author keywords available]

Indexed keywords

ALEXA;

EID: 34248162844     PISSN: None     EISSN: 17501326     Source Type: Journal    
DOI: 10.1186/1750-1326-1-16     Document Type: Article
Times cited : (20)

References (54)
  • 1
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • Brown MS, Ye J, Rawson RB, Goldstein JL: Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 2000, 100(4):391-398.
    • (2000) Cell , vol.100 , Issue.4 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 2
    • 0034671686 scopus 로고    scopus 로고
    • Notch Signaling: From the Outside In
    • Mumm JS, Kopan R: Notch Signaling: From the Outside In. Dev Biol 2000, 228(2): 151-165.
    • (2000) Dev Biol , vol.228 , Issue.2 , pp. 151-165
    • Mumm, J.S.1    Kopan, R.2
  • 3
    • 0035576260 scopus 로고    scopus 로고
    • Intramembrane proteolysis of signal peptides: An essential step in the generation of HLA-E epitopes
    • Lemberg MK, Bland FA, Weihofen A, Braud VM, Martoglio B: Intramembrane proteolysis of signal peptides: an essential step in the generation of HLA-E epitopes. J Immunol 2001, 167(11):6441-6446.
    • (2001) J Immunol , vol.167 , Issue.11 , pp. 6441-6446
    • Lemberg, M.K.1    Bland, F.A.2    Weihofen, A.3    Braud, V.M.4    Martoglio, B.5
  • 4
    • 0035913908 scopus 로고    scopus 로고
    • Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases
    • Urban S, Lee JR, Freeman M: Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases. Cell 2001, 107(2):173-182.
    • (2001) Cell , vol.107 , Issue.2 , pp. 173-182
    • Urban, S.1    Lee, J.R.2    Freeman, M.3
  • 5
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ: Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 2001, 81 (2):741-766.
    • (2001) Physiol Rev , vol.81 , Issue.2 , pp. 741-766
    • Selkoe, D.J.1
  • 8
    • 2642539953 scopus 로고    scopus 로고
    • Intramembrane proteolysis and endoplasmic reticulum retention of hepatitis C virus core protein
    • Okamoto K, Moriishi K, Miyamura T, Matsuura Y: Intramembrane proteolysis and endoplasmic reticulum retention of hepatitis C virus core protein. J Virol 2004, 78(12):6370-6380.
    • (2004) J Virol , vol.78 , Issue.12 , pp. 6370-6380
    • Okamoto, K.1    Moriishi, K.2    Miyamura, T.3    Matsuura, Y.4
  • 10
    • 0036410505 scopus 로고    scopus 로고
    • Novel class of polytopic proteins with domains associated with putative protease activity
    • Grigorenko AP, Moliaka YK, Korovaitseva GI, Rogaev El: Novel class of polytopic proteins with domains associated with putative protease activity. Biochemistry (Mosc) 2002, 67(7):826-835.
    • (2002) Biochemistry (Mosc) , vol.67 , Issue.7 , pp. 826-835
    • Grigorenko, A.P.1    Moliaka, Y.K.2    Korovaitseva, G.I.3    Rogaev, E.4
  • 11
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • Weihofen A, Binns K, Lemberg MK, Ashman K, Martoglio B: Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science 2002, 296(5576):2215-2218.
    • (2002) Science , vol.296 , Issue.5576 , pp. 2215-2218
    • Weihofen, A.1    Binns, K.2    Lemberg, M.K.3    Ashman, K.4    Martoglio, B.5
  • 12
    • 33749327877 scopus 로고    scopus 로고
    • Intramembrane proteolytic cleavage by human signal peptide peptidase like 3 and malaria signal peptide peptidase
    • Nyborg AC, Ladd TB, Jansen K, Kukar T, Golde TE: Intramembrane proteolytic cleavage by human signal peptide peptidase like 3 and malaria signal peptide peptidase. Foseb J 2006, 20(10):1671-1679.
    • (2006) Foseb J , vol.20 , Issue.10 , pp. 1671-1679
    • Nyborg, A.C.1    Ladd, T.B.2    Jansen, K.3    Kukar, T.4    Golde, T.E.5
  • 15
    • 0141994826 scopus 로고    scopus 로고
    • Intramembrane-cleaving aspartic proteases and disease: Presenilins, signal peptide peptidase and their homologs
    • Martoglio B, Golde TE: Intramembrane-cleaving aspartic proteases and disease: presenilins, signal peptide peptidase and their homologs. Hum Mol Genet 2003, 12 Spec No 2:R201-6.
    • (2003) Hum Mol Genet , vol.12 , Issue.SPEC 2
    • Martoglio, B.1    Golde, T.E.2
  • 16
    • 0042671326 scopus 로고    scopus 로고
    • Intramembrane proteolysis by presenilin and presenilin-like proteases
    • Xia W, Wolfe MS: Intramembrane proteolysis by presenilin and presenilin-like proteases. J Cell Sci 2003, 116(Pt 14):2839-2844.
    • (2003) J Cell Sci , vol.116 , Issue.PART 14 , pp. 2839-2844
    • Xia, W.1    Wolfe, M.S.2
  • 18
    • 1842523970 scopus 로고    scopus 로고
    • Conserved "PAL" sequence in presenilins is essential for gamma-secretase activity, but not required for formation or stabilization of gamma-secretase complexes
    • Wang J, Brunkan AL, Hecimovic S, Walker E, Goate A: Conserved "PAL" sequence in presenilins is essential for gamma-secretase activity, but not required for formation or stabilization of gamma-secretase complexes. Neurobiol Dis 2004, 15(3):654-666.
    • (2004) Neurobiol Dis , vol.15 , Issue.3 , pp. 654-666
    • Wang, J.1    Brunkan, A.L.2    Hecimovic, S.3    Walker, E.4    Goate, A.5
  • 19
    • 0037418440 scopus 로고    scopus 로고
    • Physiologic and pathologic events mediated by intramembranous and juxtamembranous proteolysis
    • Golde TE, Eckman CB: Physiologic and pathologic events mediated by intramembranous and juxtamembranous proteolysis. Sci STKE 2003, 2003(172):RE4..
    • (2003) Sci STKE , vol.2003 , Issue.172
    • Golde, T.E.1    Eckman, C.B.2
  • 20
    • 1942436343 scopus 로고    scopus 로고
    • On the mechanism of SPP-catalysed intramembrane proteolysis; conformational control of peptide bond hydrolysis in the plane of the membrane
    • Lemberg MK, Martoglio B: On the mechanism of SPP-catalysed intramembrane proteolysis; conformational control of peptide bond hydrolysis in the plane of the membrane. FEBS Lett 2004, 564(3):213-218.
    • (2004) FEBS Lett , vol.564 , Issue.3 , pp. 213-218
    • Lemberg, M.K.1    Martoglio, B.2
  • 21
    • 0346788899 scopus 로고    scopus 로고
    • Intramembrane proteolysis and post-targeting functions of signal peptides
    • Martoglio B: Intramembrane proteolysis and post-targeting functions of signal peptides. Biochem Soc Trans 2003, 31(Pt 6): 1243-1247.
    • (2003) Biochem Soc Trans , vol.31 , Issue.PART 6 , pp. 1243-1247
    • Martoglio, B.1
  • 22
    • 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 AC, Jansen K, Ladd TB, Fauq A, Golde TE: 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 2004, 279(41 ):43148-43156.
    • (2004) J Biol Chem , vol.279 , Issue.41 , pp. 43148-43156
    • Nyborg, A.C.1    Jansen, K.2    Ladd, T.B.3    Fauq, A.4    Golde, T.E.5
  • 23
    • 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 MK, Weihofen A, Dev KK, Dengler U, Rovelli G. Martoglio B: Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins. J Biol Chem 2004, 279(49):50790-50798.
    • (2004) J Biol Chem , vol.279 , Issue.49 , 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
  • 25
    • 18444417998 scopus 로고    scopus 로고
    • Francis R, McGrath G, Zhang J, Ruddy DA, Sym M, Apfeld J, Nicoll M, Maxwell M, Hai B, Ellis MC, Parks AL, Xu W, Li J, Gurney M, Myers RL, Himes CS, Hiebsch R, Ruble C, NyeJS, Curtis D: aph-1 and pen-2 are required for Notch pathway signaling, gamma- secretase cleavage of betaAPP, and presenilin protein accumulation. Dev Cell 2002, 3(1):85-97.
    • Francis R, McGrath G, Zhang J, Ruddy DA, Sym M, Apfeld J, Nicoll M, Maxwell M, Hai B, Ellis MC, Parks AL, Xu W, Li J, Gurney M, Myers RL, Himes CS, Hiebsch R, Ruble C, NyeJS, Curtis D: aph-1 and pen-2 are required for Notch pathway signaling, gamma- secretase cleavage of betaAPP, and presenilin protein accumulation. Dev Cell 2002, 3(1):85-97.
  • 30
    • 2442446430 scopus 로고    scopus 로고
    • Signal peptide peptidase forms a homodimer that is labeled by an active site-directed gamma-secretase inhibitor
    • Nyborg AC, Kornilova AY, Jansen K, Ladd TB, Wolfe MS, Golde TE: Signal peptide peptidase forms a homodimer that is labeled by an active site-directed gamma-secretase inhibitor. J Biol Chem 2004, 279(15):15153- 15160.
    • (2004) J Biol Chem , vol.279 , Issue.15 , 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
  • 31
    • 4344632844 scopus 로고    scopus 로고
    • Functional implications of the presenilin dimerization: Reconstitution of gamma-secretase activity by assembly of a catalytic site at the dimer interface of two catalytically inactive presenilins
    • Cervantes S, Saura CA, Pomares E, Gonzalez-Duarte R, Marfany G: Functional implications of the presenilin dimerization: reconstitution of gamma-secretase activity by assembly of a catalytic site at the dimer interface of two catalytically inactive presenilins. J Biol Chem 2004, 279(35):36519-36529.
    • (2004) J Biol Chem , vol.279 , Issue.35 , pp. 36519-36529
    • Cervantes, S.1    Saura, C.A.2    Pomares, E.3    Gonzalez-Duarte, R.4    Marfany, G.5
  • 32
    • 0035823039 scopus 로고    scopus 로고
    • Homodimerization of presenilin N-terminal fragments is affected by mutations linked to Alzheimer's disease
    • Cervantes S, Gonzalez-Duarte R, Marfany G: Homodimerization of presenilin N-terminal fragments is affected by mutations linked to Alzheimer's disease. FEBS Lett 2001, 505(1):81-86.
    • (2001) FEBS Lett , vol.505 , Issue.1 , pp. 81-86
    • Cervantes, S.1    Gonzalez-Duarte, R.2    Marfany, G.3
  • 34
    • 0142039025 scopus 로고    scopus 로고
    • Oligomerization of human presenilin-1 fragments
    • Hebert SS, Godin C, Levesque G: Oligomerization of human presenilin-1 fragments. FEBS Lett 2003, 550(1-3):30-34.
    • (2003) FEBS Lett , vol.550 , Issue.1-3 , pp. 30-34
    • Hebert, S.S.1    Godin, C.2    Levesque, G.3
  • 35
    • 0037474505 scopus 로고    scopus 로고
    • Dimerization of presenilin-1 in vivo: Suggestion of novel regulatory mechanisms leading to higher order complexes
    • Hebert SS, Godin C, Tomiyama T, Mori H, Levesque G: Dimerization of presenilin-1 in vivo: suggestion of novel regulatory mechanisms leading to higher order complexes. Biochem Biophys Res Commun 2003, 301 (1): 119-126.
    • (2003) Biochem Biophys Res Commun , vol.301 , Issue.1 , pp. 119-126
    • Hebert, S.S.1    Godin, C.2    Tomiyama, T.3    Mori, H.4    Levesque, G.5
  • 37
    • 33644839624 scopus 로고    scopus 로고
    • C-terminal PAL motif of presenilin and presenilin homologues required for normal active site conformation
    • Wang J, Beher D, Nyborg AC, Shearman MS, Golde TE, Goate A: C-terminal PAL motif of presenilin and presenilin homologues required for normal active site conformation, J Neurochem 2006, 96(1):218-227.
    • (2006) J Neurochem , vol.96 , Issue.1 , pp. 218-227
    • Wang, J.1    Beher, D.2    Nyborg, A.C.3    Shearman, M.S.4    Golde, T.E.5    Goate, A.6
  • 38
    • 28244456207 scopus 로고    scopus 로고
    • Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenlin in homologues SPPL2b and SPPL3
    • Krawitz P, Haffner C, Fluhrer R, Steiner H, Schmid B, Haass C: Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenlin in homologues SPPL2b and SPPL3. J Biol Chem 2005, 280(47):39515-39523.
    • (2005) J Biol Chem , vol.280 , Issue.47 , pp. 39515-39523
    • Krawitz, P.1    Haffner, C.2    Fluhrer, R.3    Steiner, H.4    Schmid, B.5    Haass, C.6
  • 39
    • 33745586176 scopus 로고    scopus 로고
    • Signal peptide peptidase: Biochemical properties and modulation by nonsteroidal antiinflammatory drugs
    • Sato T, Nyborg AC, Iwata N, Diehl TS, Saido TC, Golde TE, Wolfe MS: Signal peptide peptidase: biochemical properties and modulation by nonsteroidal antiinflammatory drugs. Biochemistry 2006, 45(28):8649-8656.
    • (2006) Biochemistry , vol.45 , Issue.28 , 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
  • 40
    • 0038117200 scopus 로고    scopus 로고
    • Amyloid precursor protein associates with a nicastrin-dependent docking site on the presenilin 1-gamma-secretase complex in cells demonstrated by fluorescence lifetime imaging
    • Berezovska O, Randya P, Skoch J, Wolfe MS, Bacskai B, Hyman BT: Amyloid precursor protein associates with a nicastrin-dependent docking site on the presenilin 1-gamma-secretase complex in cells demonstrated by fluorescence lifetime imaging. J Neurosci 2003, 23(11):4560- 4566.
    • (2003) J Neurosci , vol.23 , Issue.11 , pp. 4560-4566
    • Berezovska, O.1    Randya, P.2    Skoch, J.3    Wolfe, M.S.4    Bacskai, B.5    Hyman, B.T.6
  • 41
    • 0141644224 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer determinations using multiphoton fluorescence lifetime imaging microscopy to characterize amyloid-beta plaques
    • Bacskai BJ, Skoch J, Hickey GA, Allen R, Hyman BT: Fluorescence resonance energy transfer determinations using multiphoton fluorescence lifetime imaging microscopy to characterize amyloid-beta plaques. J Biomed Opt 2003, 8(3):368-375.
    • (2003) J Biomed Opt , vol.8 , Issue.3 , pp. 368-375
    • Bacskai, B.J.1    Skoch, J.2    Hickey, G.A.3    Allen, R.4    Hyman, B.T.5
  • 42
    • 22844434140 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein (LRP) interacts with presenilin I and is a competitive substrate of the amyloid precursor protein (APP) for gamma-secretase
    • Lleo A, Waldron E, von Arnim CA, Herl L, Tangredi MM, Peltan ID, Strickland DK, Koo EH, Hyman BT, Pietrzik CD, Berezovska O: Low density lipoprotein receptor-related protein (LRP) interacts with presenilin I and is a competitive substrate of the amyloid precursor protein (APP) for gamma-secretase. J Biol Chem 2005, 280(29):27303-27309.
    • (2005) J Biol Chem , vol.280 , Issue.29 , pp. 27303-27309
    • Lleo, A.1    Waldron, E.2    von Arnim, C.A.3    Herl, L.4    Tangredi, M.M.5    Peltan, I.D.6    Strickland, D.K.7    Koo, E.H.8    Hyman, B.T.9    Pietrzik, C.D.10    Berezovska, O.11
  • 44
    • 20444429794 scopus 로고    scopus 로고
    • Drosophila signal Peptide peptidase is an essential protease for larval development
    • Casso DJ, Tanda S, Biehs B, Martoglio B, Kornberg TB: Drosophila signal Peptide peptidase is an essential protease for larval development. Genetics 2005, 170(1): 139-148.
    • (2005) Genetics , vol.170 , Issue.1 , pp. 139-148
    • Casso, D.J.1    Tanda, S.2    Biehs, B.3    Martoglio, B.4    Kornberg, T.B.5
  • 45
    • 33744543016 scopus 로고    scopus 로고
    • Cell-surface expression of a new splice variant of the mouse signal peptide peptidase
    • Urny J, Hermans-Borgmeyer I, Schaller HC: Cell-surface expression of a new splice variant of the mouse signal peptide peptidase. Biochim Biophys Acta 2006, 1759(3-4):1759-165.
    • (2006) Biochim Biophys Acta , vol.1759 , Issue.3-4 , pp. 1759-1165
    • Urny, J.1    Hermans-Borgmeyer, I.2    Schaller, H.C.3
  • 46
    • 0042786828 scopus 로고    scopus 로고
    • Expression of the presenilin-like signal peptide peptidase (SPP) in mouse adult brain and during development
    • Urny J, Hermans-Borgmeyer I, Gercken G, Chica Schaller H: Expression of the presenilin-like signal peptide peptidase (SPP) in mouse adult brain and during development. Gene Expr Patterns 2003, 3(5):685-691.
    • (2003) Gene Expr Patterns , vol.3 , Issue.5 , pp. 685-691
    • Urny, J.1    Hermans-Borgmeyer, I.2    Gercken, G.3    Chica Schaller, H.4
  • 47
    • 33644585599 scopus 로고    scopus 로고
    • Efficient cleavage by signal peptide peptidase requires residues within the signal peptide between the core and El proteins of hepatitis C virus strain J1
    • Hope RG, McElwee MJ, McLauchlan J: Efficient cleavage by signal peptide peptidase requires residues within the signal peptide between the core and El proteins of hepatitis C virus strain J1. J Gen Virol 2006, 87(Pt 3):623-627.
    • (2006) J Gen Virol , vol.87 , Issue.PART 3 , pp. 623-627
    • Hope, R.G.1    McElwee, M.J.2    McLauchlan, J.3
  • 48
    • 33749406620 scopus 로고    scopus 로고
    • Signal Peptide Peptidase Cleavage of GB Virus B Core Protein Is Required for Productive Infection in Vivo
    • Targett-Adams P, Schaller T, Hope G, Lanford RE, Lemon SM, Martin A, McLauchlan J: Signal Peptide Peptidase Cleavage of GB Virus B Core Protein Is Required for Productive Infection in Vivo. J Biol Chem 2006, 281 (39):29221-29227.
    • (2006) J Biol Chem , vol.281 , Issue.39 , pp. 29221-29227
    • Targett-Adams, P.1    Schaller, T.2    Hope, G.3    Lanford, R.E.4    Lemon, S.M.5    Martin, A.6    McLauchlan, J.7
  • 50
    • 0035407522 scopus 로고    scopus 로고
    • KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: Measurements in living cells using FRET
    • Majoul I, Straub M, Hell SW, Duden R, Soling HD: KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: measurements in living cells using FRET. Dev Cell 2001, 1(1):139-153.
    • (2001) Dev Cell , vol.1 , Issue.1 , pp. 139-153
    • Majoul, I.1    Straub, M.2    Hell, S.W.3    Duden, R.4    Soling, H.D.5
  • 54
    • 15244341378 scopus 로고    scopus 로고
    • Familial Alzheimer's disease presenilin I mutations cause alterations in the conformation of presenilin and interactions with amyloid precursor protein
    • Berezovska O, Lleo A, Herl LD, Frosch MP, Stern EA, Bacskai BJ, Hyman BT: Familial Alzheimer's disease presenilin I mutations cause alterations in the conformation of presenilin and interactions with amyloid precursor protein. J Neurosci 2005, 25(11):3009-3017.
    • (2005) J Neurosci , vol.25 , Issue.11 , pp. 3009-3017
    • Berezovska, O.1    Lleo, A.2    Herl, L.D.3    Frosch, M.P.4    Stern, E.A.5    Bacskai, B.J.6    Hyman, B.T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.