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Volumn 275, Issue 1, 2008, Pages 34-43

Signal peptide peptidase and its homologs in Arabidopsis thaliana - Plant tissue-specific expression and distinct subcellular localization

Author keywords

Aspartic proteinase; Endoplasmic reticulum; Endosomes; Intramembrane cleaving protease; Signal peptide peptidase

Indexed keywords

GREEN FLUORESCENT PROTEIN; PEPTIDASE; SIGNAL PEPTIDE;

EID: 37349038178     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.06170.x     Document Type: Article
Times cited : (18)

References (33)
  • 1
    • 0345120944 scopus 로고    scopus 로고
    • Plant aspartic proteinases: Enzymes on the way to a function
    • Mutlu A Gal S (1999) Plant aspartic proteinases: enzymes on the way to a function. Physiol Plant 105, 569 576.
    • (1999) Physiol Plant , vol.105 , pp. 569-576
    • Mutlu, A.1    Gal, S.2
  • 2
    • 0029101380 scopus 로고
    • Rice aspartic proteinase, oryzasin, expressed during seed ripening and germination, has a gene organization distinct from those of animal and microbial aspartic proteinases
    • Asakura T, Watanabe H, Abe K Arai S (1995) Rice aspartic proteinase, oryzasin, expressed during seed ripening and germination, has a gene organization distinct from those of animal and microbial aspartic proteinases. Eur J Biochem 232, 77 83.
    • (1995) Eur J Biochem , vol.232 , pp. 77-83
    • Asakura, T.1    Watanabe, H.2    Abe, K.3    Arai, S.4
  • 3
    • 0000979455 scopus 로고    scopus 로고
    • Oryzasin as an aspartic proteinase occurring in rice seeds: Purification, characterization, and application to milk clotting
    • Asakura T, Watanabe H, Abe K Arai S (1997) Oryzasin as an aspartic proteinase occurring in rice seeds: purification, characterization, and application to milk clotting. J Agric Food Chem 45, 1070 1075.
    • (1997) J Agric Food Chem , vol.45 , pp. 1070-1075
    • Asakura, T.1    Watanabe, H.2    Abe, K.3    Arai, S.4
  • 4
    • 1942487289 scopus 로고    scopus 로고
    • Characterization of the genes for two soybean aspartic proteinases and analysis of their different tissue-dependent expression
    • Terauchi K, Asakura T, Nishizawa NK, Matsumoto I Abe K (2004) Characterization of the genes for two soybean aspartic proteinases and analysis of their different tissue-dependent expression. Planta 218, 947 957.
    • (2004) Planta , vol.218 , pp. 947-957
    • Terauchi, K.1    Asakura, T.2    Nishizawa, N.K.3    Matsumoto, I.4    Abe, K.5
  • 6
    • 0033869219 scopus 로고    scopus 로고
    • The plant aspartic proteinase-specific polypeptide insert is not directly related to the activity of oryzasin 1
    • Asakura T, Matsumoto I, Funaki J, Arai S Abe K (2000) The plant aspartic proteinase-specific polypeptide insert is not directly related to the activity of oryzasin 1. Eur J Biochem 267, 5115 5122.
    • (2000) Eur J Biochem , vol.267 , pp. 5115-5122
    • Asakura, T.1    Matsumoto, I.2    Funaki, J.3    Arai, S.4    Abe, K.5
  • 8
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • Brown MS, Ye J, Rawson RB Goldstein JL (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
  • 9
    • 0036777494 scopus 로고    scopus 로고
    • Intramembrane proteolysis controls diverse signalling pathways throughout evolution
    • Urban S Freeman M (2002) Intramembrane proteolysis controls diverse signalling pathways throughout evolution. Curr Opin Genet Dev 12, 512 518.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 512-518
    • Urban, S.1    Freeman, M.2
  • 10
    • 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 (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
  • 12
    • 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 (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
  • 15
    • 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 Schaller HC (2003) Expression of the presenilin-like signal peptide peptidase (SPP) in mouse adult brain and during development. Gene Exp Patterns 3, 685 691.
    • (2003) Gene Exp Patterns , vol.3 , pp. 685-691
    • Urny, J.1    Hermans-Borgmeyer, I.2    Gercken, G.3    Schaller, H.C.4
  • 16
    • 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 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
  • 17
    • 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 (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
  • 18
    • 6944250394 scopus 로고    scopus 로고
    • The Caenorhabditis elegans IMPAS gene, imp-2, is essential for development and is functionally distinct from related presenilins
    • Grigorenko AP, Moliaka YK, Soto MC, Mello CC Rogaev EI (2004) The Caenorhabditis elegans IMPAS gene, imp-2, is essential for development and is functionally distinct from related presenilins. Proc Natl Acad Sci USA 101, 14955 14960.
    • (2004) Proc Natl Acad Sci USA , 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
  • 19
    • 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 (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
  • 20
    • 0036683052 scopus 로고    scopus 로고
    • Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets
    • McLauchlan J, Lemberg MK, Hope G 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
  • 21
    • 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 (2006) Signal peptide peptidase cleavage of GB virus B core protein is required for productive infection in vivo. J Biol Chem 281, 29221 29227.
    • (2006) J Biol Chem , vol.281 , 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
  • 22
    • 32444447231 scopus 로고    scopus 로고
    • Core protein of pestiviruses is processed at the C terminus by signal peptide peptidase
    • Heimann M, Roman-Sosa G, Martoglio B, Thiel HJ Rumenapf T (2006) Core protein of pestiviruses is processed at the C terminus by signal peptide peptidase. J Virol 80, 1915 1921.
    • (2006) J Virol , vol.80 , pp. 1915-1921
    • Heimann, M.1    Roman-Sosa, G.2    Martoglio, B.3    Thiel, H.J.4    Rumenapf, T.5
  • 23
    • 0030732847 scopus 로고    scopus 로고
    • Signal peptide fragments of preprolactin and HIV-1 p-gp160 interact with calmodulin
    • Martoglio B, Graf R Dobberstein B (1997) Signal peptide fragments of preprolactin and HIV-1 p-gp160 interact with calmodulin. EMBO J 16, 6636 6645.
    • (1997) EMBO J , vol.16 , pp. 6636-6645
    • Martoglio, B.1    Graf, R.2    Dobberstein, B.3
  • 25
    • 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 (2006) C-terminal PAL motif of presenilin and presenilin homologues required for normal active site conformation. J Neurochem 96, 218 227.
    • (2006) J Neurochem , vol.96 , pp. 218-227
    • Wang, J.1    Beher, D.2    Nyborg, A.C.3    Shearman, M.S.4    Golde, T.E.5    Goate, A.6
  • 26
    • 0033838323 scopus 로고    scopus 로고
    • A dominant negative mutant of sar1 GTPase inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus in tobacco and Arabidopsis cultured cells
    • Takeuchi M, Ueda T, Sato K, Abe H, Nagata T Nakano A (2000) A dominant negative mutant of sar1 GTPase inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus in tobacco and Arabidopsis cultured cells. Plant J 23, 517 525.
    • (2000) Plant J , vol.23 , pp. 517-525
    • Takeuchi, M.1    Ueda, T.2    Sato, K.3    Abe, H.4    Nagata, T.5    Nakano, A.6
  • 27
    • 0035801358 scopus 로고    scopus 로고
    • Ara6, a plant-unique novel type Rab GTPase, functions in the endocytic pathway of Arabidopsis thaliana
    • Ueda T, Yamaguchi M, Uchimiya H Nakano A (2001) Ara6, a plant-unique novel type Rab GTPase, functions in the endocytic pathway of Arabidopsis thaliana. EMBO J 20, 4730 4741.
    • (2001) EMBO J , vol.20 , pp. 4730-4741
    • Ueda, T.1    Yamaguchi, M.2    Uchimiya, H.3    Nakano, A.4
  • 28
    • 0032444227 scopus 로고    scopus 로고
    • Role of WUSCHEL in regulating stem cell fate in the Arabidopsis shoot meristem
    • Mayer KF, Schoof H, Haecker A, Lenhard M, Jurgens G Laux T (1998) Role of WUSCHEL in regulating stem cell fate in the Arabidopsis shoot meristem. Cell 95, 805 815.
    • (1998) Cell , vol.95 , pp. 805-815
    • Mayer, K.F.1    Schoof, H.2    Haecker, A.3    Lenhard, M.4    Jurgens, G.5    Laux, T.6
  • 29
    • 0030070190 scopus 로고    scopus 로고
    • A member of the KNOTTED class of homeodomain proteins encoded by the STM gene of Arabidopsis
    • Long JA, Moan EI, Medford JI Barton MK (1996) A member of the KNOTTED class of homeodomain proteins encoded by the STM gene of Arabidopsis. Nature 379, 66 69.
    • (1996) Nature , vol.379 , pp. 66-69
    • Long, J.A.1    Moan, E.I.2    Medford, J.I.3    Barton, M.K.4
  • 31
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: An application to display phylogenetic trees on personal computers
    • Page RD (1996) TreeView: an application to display phylogenetic trees on personal computers. Comput Appl Biosci 12, 357 358.
    • (1996) Comput Appl Biosci , vol.12 , pp. 357-358
    • Page, R.D.1
  • 33
    • 4444309237 scopus 로고    scopus 로고
    • Systematic analysis of SNARE molecules in Arabidopsis: Dissection of the post-Golgi network in plant cells
    • Uemura T, Ueda T, Ohniwa RL, Nakano A, Takeyasu K Sato MH (2004) Systematic analysis of SNARE molecules in Arabidopsis: dissection of the post-Golgi network in plant cells. Cell Struct Funct 29, 49 65.
    • (2004) Cell Struct Funct , vol.29 , pp. 49-65
    • Uemura, T.1    Ueda, T.2    Ohniwa, R.L.3    Nakano, A.4    Takeyasu, K.5    Sato, M.H.6


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