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Volumn 8, Issue 2, 2014, Pages

Deletion of Ubiquitin Fold Modifier Protein Ufm1 Processing Peptidase Ufsp in L. donovani Abolishes Ufm1 Processing and Alters Pathogenesis

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; GENOMIC DNA; PEPTIDES AND PROTEINS; RECOMBINANT PROTEIN; SERINE; UBIQUITIN FOLD MODIFIER PROTEIN 1; UBIQUITIN SPECIFIC PEPTIDASE; UNCLASSIFIED DRUG;

EID: 84895768381     PISSN: 19352727     EISSN: 19352735     Source Type: Journal    
DOI: 10.1371/journal.pntd.0002707     Document Type: Article
Times cited : (19)

References (37)
  • 1
    • 84861665791 scopus 로고    scopus 로고
    • Leishmaniasis worldwide and global estimates of its incidence
    • Alvar J, Velez ID, Bern C, Herrero M, Desjeux P, et al. (2012) Leishmaniasis worldwide and global estimates of its incidence. PLoS One 7 (5) (): e35671.
    • (2012) PLoS One , vol.7 , Issue.5
    • Alvar, J.1    Velez, I.D.2    Bern, C.3    Herrero, M.4    Desjeux, P.5
  • 2
    • 84860624028 scopus 로고    scopus 로고
    • Leishmaniasis: current statusof available drugs and new therapeutic drug targets
    • Singh N, Kumar M, Singh RK, (2012) Leishmaniasis: current statusof available drugs and new therapeutic drug targets. Asian Pac J Trop Med 5: 485-497.
    • (2012) Asian Pac J Trop Med , vol.5 , pp. 485-497
    • Singh, N.1    Kumar, M.2    Singh, R.K.3
  • 3
    • 79960392640 scopus 로고    scopus 로고
    • Leishmaniasis: complexity at the host-pathogen interface
    • Kaye P, Scott P, (2011) Leishmaniasis: complexity at the host-pathogen interface. Nat Rev Microbiol 9: 604-615.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 604-615
    • Kaye, P.1    Scott, P.2
  • 4
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • Hochstrasser M, (2009) Origin and function of ubiquitin-like proteins. Nature 458: 422-429.
    • (2009) Nature , vol.458 , pp. 422-429
    • Hochstrasser, M.1
  • 5
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • Kerscher O, Felberbaum R, Hochstrasser M, (2006) Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu Rev Cell Dev Biol 22: 159-180.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 7
    • 59649086030 scopus 로고    scopus 로고
    • Nonproteolytic functions of ubiquitin in cell signaling
    • Chen ZJ, Sun LJ, (2009) Nonproteolytic functions of ubiquitin in cell signaling. Mol Cell 33: 275-286.
    • (2009) Mol Cell , vol.33 , pp. 275-286
    • Chen, Z.J.1    Sun, L.J.2
  • 8
    • 3142519570 scopus 로고    scopus 로고
    • A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier
    • Komatsu M, Chiba T, Tatsumi K, Iemura S, Tanida I, et al. (2004) A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier. EMBO J 23: 1977-1986.
    • (2004) EMBO J , vol.23 , pp. 1977-1986
    • Komatsu, M.1    Chiba, T.2    Tatsumi, K.3    Iemura, S.4    Tanida, I.5
  • 9
    • 34247162291 scopus 로고    scopus 로고
    • Two novel ubiquitin-fold modifier 1 (Ufm1)-specific proteases, UfSP1 and UfSP2
    • Kang SH, Kim GR, Seong M, Baek SH, Seol JH, et al. (2007) Two novel ubiquitin-fold modifier 1 (Ufm1)-specific proteases, UfSP1 and UfSP2. J Biol Chem 282: 5256-5262.
    • (2007) J Biol Chem , vol.282 , pp. 5256-5262
    • Kang, S.H.1    Kim, G.R.2    Seong, M.3    Baek, S.H.4    Seol, J.H.5
  • 10
    • 77949312862 scopus 로고    scopus 로고
    • A novel type of E3 ligase for the Ufm1 conjugation system
    • Tatsumi K, Sou YS, Tada N, Nakamura E, Iemura S, et al. (2010) A novel type of E3 ligase for the Ufm1 conjugation system. J Biol Chem 285: 5417-5427.
    • (2010) J Biol Chem , vol.285 , pp. 5417-5427
    • Tatsumi, K.1    Sou, Y.S.2    Tada, N.3    Nakamura, E.4    Iemura, S.5
  • 11
    • 79953760562 scopus 로고    scopus 로고
    • Ubiquitin fold modifier 1 (UFM1) and its target UFBP1 protect pancreatic beta cells from ER stress-induced apoptosis
    • Lemaire K, Moura RF, Granvik M, Igoillo-Esteve M, Hohmeier HE, et al. (2011) Ubiquitin fold modifier 1 (UFM1) and its target UFBP1 protect pancreatic beta cells from ER stress-induced apoptosis. PLoS One 6: e18517.
    • (2011) PLoS One , vol.6
    • Lemaire, K.1    Moura, R.F.2    Granvik, M.3    Igoillo-Esteve, M.4    Hohmeier, H.E.5
  • 12
    • 84880278483 scopus 로고    scopus 로고
    • The Ufm1-activating enzyme Uba5 is indispensable for erythroid differentiation in mice
    • Tatsumi K, Yamamoto-Mukai H, Shimizu R, Waguri S, Sou YS, et al. (2011) The Ufm1-activating enzyme Uba5 is indispensable for erythroid differentiation in mice. Nat Commun 2: 181.
    • (2011) Nat Commun , vol.2 , pp. 181
    • Tatsumi, K.1    Yamamoto-Mukai, H.2    Shimizu, R.3    Waguri, S.4    Sou, Y.S.5
  • 13
    • 79251534058 scopus 로고    scopus 로고
    • Mitochondrial associated ubiquitin fold modifier-1 mediated protein conjugation in Leishmania donovani
    • Gannavaram S, Sharma P, Duncan RC, Salotra P, Nakhasi HL, (2011) Mitochondrial associated ubiquitin fold modifier-1 mediated protein conjugation in Leishmania donovani. PLoS One 6: e16156.
    • (2011) PLoS One , vol.6
    • Gannavaram, S.1    Sharma, P.2    Duncan, R.C.3    Salotra, P.4    Nakhasi, H.L.5
  • 14
    • 84867055834 scopus 로고    scopus 로고
    • Deletion of mitochondrial associated ubiquitin fold modifier protein Ufm1 in Leishmania donovani results in loss of beta-oxidation of fatty acids and blocks cell division in the amastigote stage
    • Gannavaram S, Connelly PS, Daniels MP, Duncan R, Salotra P, et al. (2012) Deletion of mitochondrial associated ubiquitin fold modifier protein Ufm1 in Leishmania donovani results in loss of beta-oxidation of fatty acids and blocks cell division in the amastigote stage. Mol Microbiol 86: 187-198.
    • (2012) Mol Microbiol , vol.86 , pp. 187-198
    • Gannavaram, S.1    Connelly, P.S.2    Daniels, M.P.3    Duncan, R.4    Salotra, P.5
  • 15
    • 81555195734 scopus 로고    scopus 로고
    • Immunity to visceral leishmaniasis using genetically defined live-attenuated parasites
    • Selvapandiyan A, Dey R, Gannavaram S, Lakhal-Naouar I, Duncan R, et al. (2012) Immunity to visceral leishmaniasis using genetically defined live-attenuated parasites. J Trop Med 2012: 631460.
    • (2012) J Trop Med , vol.2012 , pp. 631460
    • Selvapandiyan, A.1    Dey, R.2    Gannavaram, S.3    Lakhal-Naouar, I.4    Duncan, R.5
  • 16
    • 0027461089 scopus 로고
    • Cloning and characterization of differentially expressed genes from in vitro-grown 'amastigotes' of Leishmania donovani
    • Joshi M, Dwyer DM, Nakhasi HL, (1993) Cloning and characterization of differentially expressed genes from in vitro-grown 'amastigotes' of Leishmania donovani. Mol Biochem Parasitol 58: 345-354.
    • (1993) Mol Biochem Parasitol , vol.58 , pp. 345-354
    • Joshi, M.1    Dwyer, D.M.2    Nakhasi, H.L.3
  • 17
    • 1242294372 scopus 로고    scopus 로고
    • Generation of Leishmania donovani axenic amastigotes: their growth and biological characteristics
    • Debrabant A, Joshi MB, Pimenta PF, Dwyer DM, (2004) Generation of Leishmania donovani axenic amastigotes: their growth and biological characteristics. Int J Parasitol 34: 205-217.
    • (2004) Int J Parasitol , vol.34 , pp. 205-217
    • Debrabant, A.1    Joshi, M.B.2    Pimenta, P.F.3    Dwyer, D.M.4
  • 18
    • 59249089075 scopus 로고    scopus 로고
    • FRET-based in vitro assays for the analysis of SUMO protease activities
    • Tatham MH, Hay RT, (2009) FRET-based in vitro assays for the analysis of SUMO protease activities. Methods Mol Biol 497: 253-268.
    • (2009) Methods Mol Biol , vol.497 , pp. 253-268
    • Tatham, M.H.1    Hay, R.T.2
  • 19
    • 39449083014 scopus 로고    scopus 로고
    • Conservation of the pro-apoptotic nuclease activity of endonuclease G in unicellular trypanosomatid parasites
    • Gannavaram S, Vedvyas C, Debrabant A, (2008) Conservation of the pro-apoptotic nuclease activity of endonuclease G in unicellular trypanosomatid parasites. J Cell Sci 121: 99-109.
    • (2008) J Cell Sci , vol.121 , pp. 99-109
    • Gannavaram, S.1    Vedvyas, C.2    Debrabant, A.3
  • 20
    • 0030014943 scopus 로고    scopus 로고
    • Identification and overexpression of the A2 amastigote-specific protein in Leishmania donovani
    • Zhang WW, Charest H, Ghedin E, Matlashewski G, (1996) Identification and overexpression of the A2 amastigote-specific protein in Leishmania donovani. Mol Biochem Parasitol 78: 79-90.
    • (1996) Mol Biochem Parasitol , vol.78 , pp. 79-90
    • Zhang, W.W.1    Charest, H.2    Ghedin, E.3    Matlashewski, G.4
  • 21
    • 84857358759 scopus 로고    scopus 로고
    • Involvement of TatD nuclease during programmed cell death in the protozoan parasite Trypanosoma brucei
    • Gannavaram S, Debrabant A, (2012) Involvement of TatD nuclease during programmed cell death in the protozoan parasite Trypanosoma brucei. Mol Microbiol 83: 926-935.
    • (2012) Mol Microbiol , vol.83 , pp. 926-935
    • Gannavaram, S.1    Debrabant, A.2
  • 22
    • 79953194770 scopus 로고    scopus 로고
    • Structure of ubiquitin-fold modifier 1-specific protease UfSP2
    • Ha BH, Jeon YJ, Shin SC, Tatsumi K, Komatsu M, et al. (2011) Structure of ubiquitin-fold modifier 1-specific protease UfSP2. J Biol Chem 286: 10248-10257.
    • (2011) J Biol Chem , vol.286 , pp. 10248-10257
    • Ha, B.H.1    Jeon, Y.J.2    Shin, S.C.3    Tatsumi, K.4    Komatsu, M.5
  • 23
    • 33750507275 scopus 로고    scopus 로고
    • In vitro antiprotozoal activity of the lipophilic extracts of different parts of Turkish Pistacia vera L
    • Orhan I, Aslan M, Sener B, Kaiser M, Tasdemir D, (2006) In vitro antiprotozoal activity of the lipophilic extracts of different parts of Turkish Pistacia vera L. Phytomedicine 13: 735-739.
    • (2006) Phytomedicine , vol.13 , pp. 735-739
    • Orhan, I.1    Aslan, M.2    Sener, B.3    Kaiser, M.4    Tasdemir, D.5
  • 24
    • 84863535618 scopus 로고    scopus 로고
    • In vitro antitrypanosomal activity of bis(bibenzyls)s and bibenzyls from liverworts against Trypanosoma brucei
    • Otoguro K, Ishiyama A, Iwatsuki M, Namatame M, Nishihara-Tukashima A, et al. (2012) In vitro antitrypanosomal activity of bis(bibenzyls)s and bibenzyls from liverworts against Trypanosoma brucei. J Nat Med 66: 377-382.
    • (2012) J Nat Med , vol.66 , pp. 377-382
    • Otoguro, K.1    Ishiyama, A.2    Iwatsuki, M.3    Namatame, M.4    Nishihara-Tukashima, A.5
  • 25
    • 84866425729 scopus 로고    scopus 로고
    • Prophylactic or therapeutic administration of Agaricus blazei Murill is effective in treatment of murine visceral leishmaniasis
    • Valadares DG, Duarte MC, Ramirez L, Chavez-Fumagalli MA, Martins VT, et al. (2012) Prophylactic or therapeutic administration of Agaricus blazei Murill is effective in treatment of murine visceral leishmaniasis. Exp Parasitol 132: 228-236.
    • (2012) Exp Parasitol , vol.132 , pp. 228-236
    • Valadares, D.G.1    Duarte, M.C.2    Ramirez, L.3    Chavez-Fumagalli, M.A.4    Martins, V.T.5
  • 28
    • 56449118262 scopus 로고    scopus 로고
    • Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis
    • Pearce MJ, Mintseris J, Ferreyra J, Gygi SP, Darwin KH, (2008) Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis. Science 322: 1104-1107.
    • (2008) Science , vol.322 , pp. 1104-1107
    • Pearce, M.J.1    Mintseris, J.2    Ferreyra, J.3    Gygi, S.P.4    Darwin, K.H.5
  • 29
    • 49049086135 scopus 로고    scopus 로고
    • Complete cure of experimental visceral leishmaniasis with Amphotericin B in stearylamine-bearing cationic liposomes involves down-regulation of IL-10 and favorable T cell responses
    • Banerjee A, De M, Ali N, (2008) Complete cure of experimental visceral leishmaniasis with Amphotericin B in stearylamine-bearing cationic liposomes involves down-regulation of IL-10 and favorable T cell responses. J Immunol 181: 1386-1398.
    • (2008) J Immunol , vol.181 , pp. 1386-1398
    • Banerjee, A.1    De, M.2    Ali, N.3
  • 30
    • 33747032806 scopus 로고    scopus 로고
    • Identification by functional proteomics of a deubiquitinating/deNeddylating enzyme in Plasmodium falciparum
    • Artavanis-Tsakonas K, Misaghi S, Comeaux CA, Catic A, Spooner E, et al. (2006) Identification by functional proteomics of a deubiquitinating/deNeddylating enzyme in Plasmodium falciparum. Mol Microbiol 61: 1187-1195.
    • (2006) Mol Microbiol , vol.61 , pp. 1187-1195
    • Artavanis-Tsakonas, K.1    Misaghi, S.2    Comeaux, C.A.3    Catic, A.4    Spooner, E.5
  • 31
    • 77949901727 scopus 로고    scopus 로고
    • Characterization and structural studies of the Plasmodium falciparum ubiquitin and Nedd8 hydrolase UCHL3
    • Artavanis-Tsakonas K, Weihofen WA, Antos JM, Coleman BI, Comeaux CA, et al. (2010) Characterization and structural studies of the Plasmodium falciparum ubiquitin and Nedd8 hydrolase UCHL3. J Biol Chem 285: 6857-6866.
    • (2010) J Biol Chem , vol.285 , pp. 6857-6866
    • Artavanis-Tsakonas, K.1    Weihofen, W.A.2    Antos, J.M.3    Coleman, B.I.4    Comeaux, C.A.5
  • 32
    • 77953731056 scopus 로고    scopus 로고
    • Targeting the Plasmodium ubiquitin/proteasome system with anti-malarial compounds: promises for the future
    • Chung DW, Le Roch KG, (2010) Targeting the Plasmodium ubiquitin/proteasome system with anti-malarial compounds: promises for the future. Infect Disord Drug Targets 10: 158-164.
    • (2010) Infect Disord Drug Targets , vol.10 , pp. 158-164
    • Chung, D.W.1    Le Roch, K.G.2
  • 33
    • 79959523531 scopus 로고    scopus 로고
    • Functional characterization of a SUMO deconjugating protease of Plasmodium falciparum using newly identified small molecule inhibitors
    • Ponder EL, Albrow VE, Leader BA, Bekes M, Mikolajczyk J, et al. (2011) Functional characterization of a SUMO deconjugating protease of Plasmodium falciparum using newly identified small molecule inhibitors. Chem Biol 18: 711-721.
    • (2011) Chem Biol , vol.18 , pp. 711-721
    • Ponder, E.L.1    Albrow, V.E.2    Leader, B.A.3    Bekes, M.4    Mikolajczyk, J.5
  • 34
    • 65649126339 scopus 로고    scopus 로고
    • Ubiquitin C-terminal electrophiles are activity-based probes for identification and mechanistic study of ubiquitin conjugating machinery
    • Love KR, Pandya RK, Spooner E, Ploegh HL, (2009) Ubiquitin C-terminal electrophiles are activity-based probes for identification and mechanistic study of ubiquitin conjugating machinery. ACS Chem Biol 4: 275-287.
    • (2009) ACS Chem Biol , vol.4 , pp. 275-287
    • Love, K.R.1    Pandya, R.K.2    Spooner, E.3    Ploegh, H.L.4
  • 35
    • 77649196421 scopus 로고    scopus 로고
    • Secretory protein with RING finger domain (SPRING) specific to Trypanosoma cruzi is directed, as a ubiquitin ligase related protein, to the nucleus of host cells
    • Hashimoto M, Murata E, Aoki T, (2010) Secretory protein with RING finger domain (SPRING) specific to Trypanosoma cruzi is directed, as a ubiquitin ligase related protein, to the nucleus of host cells. Cell Microbiol 12: 19-30.
    • (2010) Cell Microbiol , vol.12 , pp. 19-30
    • Hashimoto, M.1    Murata, E.2    Aoki, T.3
  • 36
    • 83055163826 scopus 로고    scopus 로고
    • SUMOylation pathway in Trypanosoma cruzi: functional characterization and proteomic analysis of target proteins
    • M110 007369
    • Bayona JC, Nakayasu ES, Laverriere M, Aguilar C, Sobreira TJ, et al. (2011) SUMOylation pathway in Trypanosoma cruzi: functional characterization and proteomic analysis of target proteins. Mol Cell Proteomics 10: M110 007369.
    • (2011) Mol Cell Proteomics , vol.10
    • Bayona, J.C.1    Nakayasu, E.S.2    Laverriere, M.3    Aguilar, C.4    Sobreira, T.J.5
  • 37
    • 84861219968 scopus 로고    scopus 로고
    • SUMOylation of paraflagellar rod protein, PFR1, and its stage-specific localization in Trypanosoma cruzi
    • Annoura T, Makiuchi T, Sariego I, Aoki T, Nara T, (2012) SUMOylation of paraflagellar rod protein, PFR1, and its stage-specific localization in Trypanosoma cruzi. PLoS One 7: e37183.
    • (2012) PLoS One , vol.7
    • Annoura, T.1    Makiuchi, T.2    Sariego, I.3    Aoki, T.4    Nara, T.5


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