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Volumn 8, Issue 8, 2006, Pages 843-848

SPPL2a and SPPL2b promote intramembrane proteolysis of TNFα in activated dendritic cells to trigger IL-12 production

Author keywords

[No Author keywords available]

Indexed keywords

INTERLEUKIN 12; SIGNAL PEPTIDASE II; SIGNAL PEPTIDASE IIA; SIGNAL PEPTIDASE IIB; SIGNAL PEPTIDE; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 33746618450     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1440     Document Type: Article
Times cited : (176)

References (34)
  • 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. & Goldstein, J. L. Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans. Cell 100, 391-398 (2000).
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 2
    • 0038732581 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: From the endoplasmic reticulum to the nucleus
    • Rawson, R. B. Regulated intramembrane proteolysis: From the endoplasmic reticulum to the nucleus. Essays Biochem. 38, 155-168 (2002).
    • (2002) Essays Biochem. , vol.38 , pp. 155-168
    • Rawson, R.B.1
  • 3
    • 18844378852 scopus 로고    scopus 로고
    • Presenilin function and γ-secretase activity
    • Brunkan, A. L. & Goate, A. M. Presenilin function and γ-secretase activity. J. Neurochem. 93, 769-792 (2005).
    • (2005) J. Neurochem. , vol.93 , pp. 769-792
    • Brunkan, A.L.1    Goate, A.M.2
  • 4
    • 0037304947 scopus 로고    scopus 로고
    • Intramembrane-cleaving proteases: Controlled liberation of proteins and bioactive peptides
    • Weihofen, A. & Martoglio, B. Intramembrane-cleaving proteases: controlled liberation of proteins and bioactive peptides. Trends Cell Biol. 13, 71-78 (2003).
    • (2003) Trends Cell Biol. , vol.13 , pp. 71-78
    • Weihofen, A.1    Martoglio, B.2
  • 5
    • 0036898485 scopus 로고    scopus 로고
    • Alzheimer disease γ-secretase: A complex story of GxGD-type presenilin proteases
    • Haass, C. & Steiner, H. Alzheimer disease γ-secretase: A complex story of GxGD-type presenilin proteases. Trends Cell Biol. 12, 556-562 (2002).
    • (2002) Trends Cell Biol. , vol.12 , pp. 556-562
    • Haass, C.1    Steiner, H.2
  • 6
    • 0031301274 scopus 로고    scopus 로고
    • Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs
    • Rawson, R. B. et al. Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs. Mol. Cell 1, 47-57 (1997).
    • (1997) Mol. Cell , vol.1 , pp. 47-57
    • Rawson, R.B.1
  • 7
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • Ye, J. et al. ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol. Cell 6, 1355-1364 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 1355-1364
    • Ye, J.1
  • 8
    • 4344694114 scopus 로고    scopus 로고
    • Ligands working as receptors: Reverse signaling by members of the TNF superfamily enhance the plasticity of the immune system
    • Eissner, G., Kolch, W. & Scheurich, P. Ligands working as receptors: reverse signaling by members of the TNF superfamily enhance the plasticity of the immune system. Cytokine Growth Factor Rev. 15, 353-366 (2004).
    • (2004) Cytokine Growth Factor Rev. , vol.15 , pp. 353-366
    • Eissner, G.1    Kolch, W.2    Scheurich, P.3
  • 9
    • 27444441308 scopus 로고    scopus 로고
    • A nine-transmembrane domain topology for presenilin 1
    • Laudon, H. et al. A nine-transmembrane domain topology for presenilin 1. J. Biol. Chem. 280, 35352-35360 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 35352-35360
    • Laudon, H.1
  • 10
    • 0141994826 scopus 로고    scopus 로고
    • Intramembrane-cleaving aspartic proteases and disease: Presenilins, signal peptide peptidase and their homologs
    • Martoglio, B. & Golde, T. E. Intramembrane-cleaving aspartic proteases and disease: Presenilins, signal peptide peptidase and their homologs. Hum. Mol. Genet. 12, R201-R206 (2003).
    • (2003) Hum. Mol. Genet. , vol.12
    • Martoglio, B.1    Golde, T.E.2
  • 11
    • 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. et al. 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).
    • (2004) J. Biol. Chem. , vol.279 , pp. 50790-50798
    • Friedmann, E.1
  • 12
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • Weihofen, A., Binns, K., Lemberg, M. K., Ashman, K. & Martoglio, B. Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science 296, 2215-2218 (2002).
    • (2002) Science , vol.296 , pp. 2215-2218
    • Weihofen, A.1    Binns, K.2    Lemberg, M.K.3    Ashman, K.4    Martoglio, B.5
  • 13
    • 0036809216 scopus 로고    scopus 로고
    • Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis
    • Lemberg, M. K. & Martoglio, B. Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis. Mol. Cell 10, 735-744 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 735-744
    • Lemberg, M.K.1    Martoglio, B.2
  • 14
    • 28244456207 scopus 로고    scopus 로고
    • Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin in homologues SPPL2b and SPPL3
    • Krawitz, P. et al. Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin in homologues SPPL2b and SPPL3. J. Biol. Chem. 280, 39515-39523 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 39515-39523
    • Krawitz, P.1
  • 15
    • 85047692516 scopus 로고    scopus 로고
    • Signalling pathways of the TNF superfamily: A double-edged sword
    • Aggarwal, B. B. Signalling pathways of the TNF superfamily: A double-edged sword. Nature Rev. Immunol. 3, 745-756 (2003).
    • (2003) Nature Rev. Immunol. , vol.3 , pp. 745-756
    • Aggarwal, B.B.1
  • 16
    • 0037930851 scopus 로고    scopus 로고
    • Targeting presenilin-type aspartic protease signal peptide peptidase with γ-secretase inhibitors
    • Weihofen, A. et al. Targeting presenilin-type aspartic protease signal peptide peptidase with γ-secretase inhibitors. J. Biol. Chem. 278, 16528-16533 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 16528-16533
    • Weihofen, A.1
  • 17
    • 0033404614 scopus 로고    scopus 로고
    • Soluble TNF-α receptors bind and neutralize over-expressed transmembrane TNF-α on macrophages, but do not inhibit its processing
    • Watts, A. D., Hunt, N. H., Madigan, M. C. & Chaudhri, G. Soluble TNF-α receptors bind and neutralize over-expressed transmembrane TNF-α on macrophages, but do not inhibit its processing. J. Leukoc. Biol. 66, 1005-1013 (1999).
    • (1999) J. Leukoc. Biol. , vol.66 , pp. 1005-1013
    • Watts, A.D.1    Hunt, N.H.2    Madigan, M.C.3    Chaudhri, G.4
  • 18
    • 0032546352 scopus 로고    scopus 로고
    • Dendritic cells and the control of immunity
    • Banchereau, J. & Steinman, R. M. Dendritic cells and the control of immunity. Nature 392, 245-252 (1998).
    • (1998) Nature , vol.392 , pp. 245-252
    • Banchereau, J.1    Steinman, R.M.2
  • 19
    • 0031045622 scopus 로고    scopus 로고
    • Origin, maturation and antigen presenting function of dendritic cells
    • Cella, M., Sallusto, F. & Lanzavecchia, A. Origin, maturation and antigen presenting function of dendritic cells. Curr. Opin. Immunol. 9, 10-16 (1997).
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 10-16
    • Cella, M.1    Sallusto, F.2    Lanzavecchia, A.3
  • 20
    • 0345358584 scopus 로고    scopus 로고
    • The IL-12 family of heterodimeric cytokines: New players in the regulation of T cell responses
    • Trinchieri, G., Pflanz, S. & Kastelein, R. A. The IL-12 family of heterodimeric cytokines: New players in the regulation of T cell responses. Immunity 19, 641-644 (2003).
    • (2003) Immunity , vol.19 , pp. 641-644
    • Trinchieri, G.1    Pflanz, S.2    Kastelein, R.A.3
  • 21
    • 3042545974 scopus 로고    scopus 로고
    • The linkage of innate to adaptive immunity via maturing dendritic cells in vivo requires CD40 ligation in addition to antigen presentation and CD80/86 costimulation
    • Fujii, S., Liu, K., Smith, C., Bonito, A. J. & Steinman, R. M. The linkage of innate to adaptive immunity via maturing dendritic cells in vivo requires CD40 ligation in addition to antigen presentation and CD80/ 86 costimulation. J. Exp. Med. 199, 1607-1618 (2004).
    • (2004) J. Exp. Med. , vol.199 , pp. 1607-1618
    • Fujii, S.1    Liu, K.2    Smith, C.3    Bonito, A.J.4    Steinman, R.M.5
  • 22
    • 0035096681 scopus 로고    scopus 로고
    • TNF-α and IL-12: A balancing act in macrophage functioning
    • Ma, X. TNF-α and IL-12: A balancing act in macrophage functioning. Microbes Infect. 3, 121-129 (2001).
    • (2001) Microbes Infect. , vol.3 , pp. 121-129
    • Ma, X.1
  • 23
    • 23244435548 scopus 로고    scopus 로고
    • State-of-the-art modified RNAi compounds for therapeutics
    • Cartstea, E. D., Hough, S., Wiederholt, K. & Welch, P. J. State-of-the-art modified RNAi compounds for therapeutics. IDrug 8, 642-647 (2005).
    • (2005) IDrug , vol.8 , pp. 642-647
    • Cartstea, E.D.1    Hough, S.2    Wiederholt, K.3    Welch, P.J.4
  • 24
    • 0031028140 scopus 로고    scopus 로고
    • Initiation of liver growth by tumor necrosis factor: Deficient liver regeneration in mice lacking type I tumor necrosis factor receptor
    • Yamada, Y., Kirillova, I., Peschon, J. J. & Fausto, N. Initiation of liver growth by tumor necrosis factor: Deficient liver regeneration in mice lacking type I tumor necrosis factor receptor, Proc. Natl Acad. Sci. USA 94, 1441-1446 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 1441-1446
    • Yamada, Y.1    Kirillova, I.2    Peschon, J.J.3    Fausto, N.4
  • 25
    • 0033778262 scopus 로고    scopus 로고
    • Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases
    • Steiner, H. et al. Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases. Nature Cell Biol. 2, 848-851 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 848-851
    • Steiner, H.1
  • 26
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α
    • Moss, M. L. et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α. Nature 385, 733-736 (1997).
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1
  • 27
    • 0024360816 scopus 로고
    • Cell surface tumor necrosis factor (TNF) accounts for monocyte- and lymphocyte-mediated killing of TNF-resistant target cells
    • Peck, R., Brockhaus, M. & Frey, J. R. Cell surface tumor necrosis factor (TNF) accounts for monocyte- and lymphocyte-mediated killing of TNF-resistant target cells. Cell. Immunol. 122, 1-10 (1989).
    • (1989) Cell. Immunol. , vol.122 , pp. 1-10
    • Peck, R.1    Brockhaus, M.2    Frey, J.R.3
  • 28
    • 0025149247 scopus 로고
    • A nonsecretable cell surface mutant of tumor necrosis factor (TNF) kills by cell-to-cell contact
    • Perez, C. et al. A nonsecretable cell surface mutant of tumor necrosis factor (TNF) kills by cell-to-cell contact. Cell 63, 251-258 (1990).
    • (1990) Cell , vol.63 , pp. 251-258
    • Perez, C.1
  • 29
    • 0028866022 scopus 로고
    • The transmembrane form of tumor necrosis factor is the prime activating ligand of the 80 kDa tumor necrosis factor receptor
    • Grell, M. et al. The transmembrane form of tumor necrosis factor is the prime activating ligand of the 80 kDa tumor necrosis factor receptor. Cell 83, 793-802 (1995).
    • (1995) Cell , vol.83 , pp. 793-802
    • Grell, M.1
  • 30
    • 0034660144 scopus 로고    scopus 로고
    • Reverse signaling through transmembrane TNF confers resistance to lipopolysaccharide in human monocytes and macrophages
    • Eissner, G. et al. Reverse signaling through transmembrane TNF confers resistance to lipopolysaccharide in human monocytes and macrophages. J. Immunol. 164, 6193-6198 (2000).
    • (2000) J. Immunol. , vol.164 , pp. 6193-6198
    • Eissner, G.1
  • 31
    • 0034808209 scopus 로고    scopus 로고
    • Receptor-like properties of the 26 kDa transmembrane form of TNF
    • Domonkos, A., Udvardy, A., Laszlo, L., Nagy, T. & Duda, E. Receptor-like properties of the 26 kDa transmembrane form of TNF. Eur. Cytokine Netw. 12, 411-419 (2001).
    • (2001) Eur. Cytokine Netw. , vol.12 , pp. 411-419
    • Domonkos, A.1    Udvardy, A.2    Laszlo, L.3    Nagy, T.4    Duda, E.5
  • 32
  • 33
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway: Retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus
    • Hammond, C. & Helenius, A. Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus. J. Cell Biol. 126, 41-52 (1994).
    • (1994) J. Cell Biol. , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 34
    • 0030951595 scopus 로고    scopus 로고
    • Improved electrophoretic separation and immunoblotting of β-amyloid (Aβ) peptides 1-40, 1-42, and 1-43
    • Wiltfang, J. et al. Improved electrophoretic separation and immunoblotting of β-amyloid (Aβ) peptides 1-40, 1-42, and 1-43. Electrophoresis 18, 527-532 (1997).
    • (1997) Electrophoresis , vol.18 , pp. 527-532
    • Wiltfang, J.1


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