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Volumn 12, Issue 2, 2013, Pages 356-367

Novel bilobe components in Trypanosoma brucei identified using proximity-dependent biotinylation

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSKELETON PROTEIN; PROTOZOAL PROTEIN;

EID: 84873149805     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00326-12     Document Type: Article
Times cited : (110)

References (30)
  • 1
    • 0032724638 scopus 로고    scopus 로고
    • The cytoskeleton of trypanosomatid parasites
    • doi:10.1146/annurev.micro.53.1.629
    • Gull K. 1999. The cytoskeleton of trypanosomatid parasites. Annu. Rev. Microbiol. 53:629-655. doi:10.1146/annurev.micro.53.1.629.
    • (1999) Annu. Rev. Microbiol. , vol.53 , pp. 629-655
    • Gull, K.1
  • 2
    • 0028935746 scopus 로고
    • Microtubule polarity and dynamics in the control of organelle positioning, segregation, and cytokinesis in the trypanosome cell cycle
    • Robinson DR, Sherwin T, Ploubidou A, Byard EH, Gull K. 1995. Microtubule polarity and dynamics in the control of organelle positioning, segregation, and cytokinesis in the trypanosome cell cycle. J. Cell Biol. 128:1163-1172.
    • (1995) J. Cell Biol. , vol.128 , pp. 1163-1172
    • Robinson, D.R.1    Sherwin, T.2    Ploubidou, A.3    Byard, E.H.4    Gull, K.5
  • 3
    • 66849128079 scopus 로고    scopus 로고
    • Three-dimensional cellular architecture of the flagellar pocket and associated cytoskeleton in trypanosomes revealed by electron microscope tomography
    • doi:10.1242/jcs.045740
    • Lacomble S, Vaughan S, Gadelha C, Morphew MK, Shaw MK, McIntosh JR, Gull K. 2009. Three-dimensional cellular architecture of the flagellar pocket and associated cytoskeleton in trypanosomes revealed by electron microscope tomography. J. Cell Sci. 122:1081-1090. doi:10.1242/jcs.045740.
    • (2009) J. Cell Sci. , vol.122 , pp. 1081-1090
    • Lacomble, S.1    Vaughan, S.2    Gadelha, C.3    Morphew, M.K.4    Shaw, M.K.5    McIntosh, J.R.6    Gull, K.7
  • 4
    • 1842531211 scopus 로고    scopus 로고
    • Kinetics of endocytosis and recycling of the GPIanchored variant surface glycoprotein in Trypanosoma brucei
    • doi:10.1242/jcs.00938
    • Engstler M, Thilo L, Weise F, Grunfelder CG, Schwarz H, Boshart M, Overath P. 2004. Kinetics of endocytosis and recycling of the GPIanchored variant surface glycoprotein in Trypanosoma brucei. J. Cell Sci. 117:1105-1115. doi:10.1242/jcs.00938.
    • (2004) J. Cell Sci. , vol.117 , pp. 1105-1115
    • Engstler, M.1    Thilo, L.2    Weise, F.3    Grunfelder, C.G.4    Schwarz, H.5    Boshart, M.6    Overath, P.7
  • 5
    • 77956939582 scopus 로고    scopus 로고
    • Basal body movements orchestrate membrane organelle division and cell morphogenesis in Trypanosoma brucei
    • doi:10.1242/jcs.074161
    • Lacomble S, Vaughan S, Gadelha C, Morphew MK, Shaw MK, McIntosh JR, Gull K. 2010. Basal body movements orchestrate membrane organelle division and cell morphogenesis in Trypanosoma brucei. J. Cell Sci. 123:2884-2891. doi:10.1242/jcs.074161.
    • (2010) J. Cell Sci. , vol.123 , pp. 2884-2891
    • Lacomble, S.1    Vaughan, S.2    Gadelha, C.3    Morphew, M.K.4    Shaw, M.K.5    McIntosh, J.R.6    Gull, K.7
  • 6
    • 0042195176 scopus 로고    scopus 로고
    • Host-parasite interactions and trypanosome morphogenesis: A flagellar pocketful of goodies
    • Gull K. 2003. Host-parasite interactions and trypanosome morphogenesis: a flagellar pocketful of goodies. Curr. Opin. Microbiol. 6:365-370.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 365-370
    • Gull, K.1
  • 7
    • 0018194153 scopus 로고
    • Electron microscopy observations on Trypanosoma brucei: Freeze-cleaving and thin-sectioning study of the apical part of the flagellar pocket
    • Henley GL, Lee CM, Takeuchi A. 1978. Electron microscopy observations on Trypanosoma brucei: freeze-cleaving and thin-sectioning study of the apical part of the flagellar pocket. Z Parasitenkd. 55:181-187.
    • (1978) Z Parasitenkd. , vol.55 , pp. 181-187
    • Henley, G.L.1    Lee, C.M.2    Takeuchi, A.3
  • 8
    • 0024967876 scopus 로고
    • The cell division cycle of Trypanosoma brucei brucei: Timing of event markers and cytoskeletal modulations
    • Sherwin T, Gull K. 1989. The cell division cycle of Trypanosoma brucei brucei: timing of event markers and cytoskeletal modulations. Philos. Trans. R. Soc. Lond. B Biol. Sci. 323:573-588.
    • (1989) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.323 , pp. 573-588
    • Sherwin, T.1    Gull, K.2
  • 9
    • 0014534896 scopus 로고
    • On the surface coat and flagellar adhesion in trypanosomes
    • Vickerman K. 1969. On the surface coat and flagellar adhesion in trypanosomes. J. Cell Sci. 5:163-193.
    • (1969) J. Cell Sci. , vol.5 , pp. 163-193
    • Vickerman, K.1
  • 11
    • 79960127168 scopus 로고    scopus 로고
    • Structure-function analysis of dynein light chain 1 identifies viable motility mutants in bloodstreamform Trypanosoma brucei
    • doi:10.1128/EC.00298-10
    • Ralston KS, Kisalu NK, Hill KL. 2011. Structure-function analysis of dynein light chain 1 identifies viable motility mutants in bloodstreamform Trypanosoma brucei. Eukaryot. Cell 10:884-894. doi:10.1128/EC.00298-10.
    • (2011) Eukaryot. Cell , vol.10 , pp. 884-894
    • Ralston, K.S.1    Kisalu, N.K.2    Hill, K.L.3
  • 12
    • 84863032195 scopus 로고    scopus 로고
    • A coiled-coil-and C2-domaincontaining protein is required for FAZ assembly and cell morphology in Trypanosoma brucei
    • doi:10.1242/jcs.087676
    • Zhou Q, Liu B, Sun Y, He CY. 2011. A coiled-coil-and C2-domaincontaining protein is required for FAZ assembly and cell morphology in Trypanosoma brucei. J. Cell Sci. 124:3848-3858. doi:10.1242/jcs.087676.
    • (2011) J. Cell Sci. , vol.124 , pp. 3848-3858
    • Zhou, Q.1    Liu, B.2    Sun, Y.3    He, C.Y.4
  • 13
    • 84858864387 scopus 로고    scopus 로고
    • The Trypanosoma brucei AIR9-like protein is cytoskeleton-associated and is required for nucleus positioning and accurate cleavage furrow placement
    • doi:10.1111/j.1365-2958.2012.08008.x
    • May SF, Peacock L, Almeida Costa CI, Gibson WC, Tetley L, Robinson DR, Hammarton TC. 2012. The Trypanosoma brucei AIR9-like protein is cytoskeleton-associated and is required for nucleus positioning and accurate cleavage furrow placement. Mol. Microbiol. 84:77-92. doi:10.1111/j.1365-2958.2012.08008.x.
    • (2012) Mol. Microbiol. , vol.84 , pp. 77-92
    • May, S.F.1    Peacock, L.2    Almeida Costa, C.I.3    Gibson, W.C.4    Tetley, L.5    Robinson, D.R.6    Hammarton, T.C.7
  • 14
    • 27944451395 scopus 로고    scopus 로고
    • Golgi duplication in Trypanosoma brucei requires Centrin2
    • doi:10.1126/science.1119969
    • He CY, Pypaert M, Warren G. 2005. Golgi duplication in Trypanosoma brucei requires Centrin2. Science 310:1196-1198. doi:10.1126/science.1119969.
    • (2005) Science , vol.310 , pp. 1196-1198
    • He, C.Y.1    Pypaert, M.2    Warren, G.3
  • 15
    • 67649359323 scopus 로고    scopus 로고
    • The bilobe structure of Trypanosoma brucei contains a MORN-repeat protein
    • doi:10.1016/j.molbiopara.2009.05.001
    • Morriswood B, He CY, Sealey-Cardona M, Yelinek J, Pypaert M, Warren G. 2009. The bilobe structure of Trypanosoma brucei contains a MORN-repeat protein. Mol. Biochem. Parasitol. 167:95-103. doi:10.1016/j.molbiopara.2009.05.001.
    • (2009) Mol. Biochem. Parasitol. , vol.167 , pp. 95-103
    • Morriswood, B.1    He, C.Y.2    Sealey-Cardona, M.3    Yelinek, J.4    Pypaert, M.5    Warren, G.6
  • 16
    • 79952116623 scopus 로고    scopus 로고
    • A comparative proteomic analysis reveals a new bi-lobe protein required for bi-lobe duplication and cell division in Trypanosoma brucei
    • doi:10.1371/journal.pone.0009660
    • Zhou Q, Gheiratmand L, Chen Y, Lim TK, Zhang J, Li S, Xia N, Liu B, Lin Q, He CY. 2010. A comparative proteomic analysis reveals a new bi-lobe protein required for bi-lobe duplication and cell division in Trypanosoma brucei. PLoS One 5:e9660. doi:10.1371/journal.pone.0009660.
    • (2010) PLoS One , vol.5
    • Zhou, Q.1    Gheiratmand, L.2    Chen, Y.3    Lim, T.K.4    Zhang, J.5    Li, S.6    Xia, N.7    Liu, B.8    Lin, Q.9    He, C.Y.10
  • 17
    • 55049099058 scopus 로고    scopus 로고
    • Centrin4 coordinates cell and nuclear division in T. brucei
    • doi:10.1242/jcs.030643
    • Shi J, Franklin JB, Yelinek JT, Ebersberger I, Warren G, He CY. 2008. Centrin4 coordinates cell and nuclear division in T. brucei. J. Cell Sci. 121:3062-3070. doi:10.1242/jcs.030643.
    • (2008) J. Cell Sci. , vol.121 , pp. 3062-3070
    • Shi, J.1    Franklin, J.B.2    Yelinek, J.T.3    Ebersberger, I.4    Warren, G.5    He, C.Y.6
  • 18
    • 84862789592 scopus 로고    scopus 로고
    • An interplay between Centrin2 and Centrin4 on the bi-lobed structure in Trypanosoma brucei
    • doi:10.1111/j.1365-2958.2012.07998.x
    • Wang M, Gheiratmand L, He CY. 2012. An interplay between Centrin2 and Centrin4 on the bi-lobed structure in Trypanosoma brucei. Mol. Microbiol. 83:1153-1161. doi:10.1111/j.1365-2958.2012.07998.x.
    • (2012) Mol. Microbiol. , vol.83 , pp. 1153-1161
    • Wang, M.1    Gheiratmand, L.2    He, C.Y.3
  • 19
    • 84861687977 scopus 로고    scopus 로고
    • Morphology of the trypanosome bilobe, a novel cytoskeletal structure
    • doi:10.1128/EC.05287-11
    • Esson HJ, Morriswood B, Yavuz S, Vidilaseris K, Dong G, Warren G. 2012. Morphology of the trypanosome bilobe, a novel cytoskeletal structure. Eukaryot. Cell 11:761-772. doi:10.1128/EC.05287-11.
    • (2012) Eukaryot. Cell , vol.11 , pp. 761-772
    • Esson, H.J.1    Morriswood, B.2    Yavuz, S.3    Vidilaseris, K.4    Dong, G.5    Warren, G.6
  • 20
    • 84860270506 scopus 로고    scopus 로고
    • A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells
    • doi:10.1083/jcb.201112098
    • Roux KJ, Kim DI, Raida M, Burke B. 2012. A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells. J. Cell Biol. 196:801-810. doi:10.1083/jcb.201112098.
    • (2012) J. Cell Biol. , vol.196 , pp. 801-810
    • Roux, K.J.1    Kim, D.I.2    Raida, M.3    Burke, B.4
  • 21
    • 0011859364 scopus 로고
    • The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and (+)-biotin. I. Purification of the apoenzyme and synthetase; characteristics of the reaction
    • Lane MD, Young DL, Lynen F. 1964. The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and (+)-biotin. I. Purification of the apoenzyme and synthetase; characteristics of the reaction. J. Biol. Chem. 239:2858-2864.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2858-2864
    • Lane, M.D.1    Young, D.L.2    Lynen, F.3
  • 22
    • 0033846484 scopus 로고    scopus 로고
    • Function of a conserved sequence motif in biotin holoenzyme synthetases
    • doi:10.1110/ps.9.8.1530
    • Kwon K, Beckett D. 2000. Function of a conserved sequence motif in biotin holoenzyme synthetases. Protein Sci. 9:1530-1539. doi:10.1110/ps.9.8.1530.
    • (2000) Protein Sci. , vol.9 , pp. 1530-1539
    • Kwon, K.1    Beckett, D.2
  • 23
    • 0033525524 scopus 로고    scopus 로고
    • A tightly regulated inducible expression system for conditional gene knock-outs and dominantnegative genetics in Trypanosoma brucei
    • Wirtz E, Leal S, Ochatt C, Cross GA. 1999. A tightly regulated inducible expression system for conditional gene knock-outs and dominantnegative genetics in Trypanosoma brucei. Mol. Biochem. Parasitol. 99: 89-101.
    • (1999) Mol. Biochem. Parasitol. , vol.99 , pp. 89-101
    • Wirtz, E.1    Leal, S.2    Ochatt, C.3    Cross, G.A.4
  • 25
    • 79955602637 scopus 로고    scopus 로고
    • High-throughput phenotyping using parallel sequencing of RNA interference targets in the African trypanosome
    • doi:10.1101/gr.115089.110
    • Alsford S, Turner DJ, Obado SO, Sanchez-Flores A, Glover L, Berriman M, Hertz-Fowler C, Horn D. 2011. High-throughput phenotyping using parallel sequencing of RNA interference targets in the African trypanosome. Genome Res. 21:915-924. doi:10.1101/gr.115089.110.
    • (2011) Genome Res. , vol.21 , pp. 915-924
    • Alsford, S.1    Turner, D.J.2    Obado, S.O.3    Sanchez-Flores, A.4    Glover, L.5    Berriman, M.6    Hertz-Fowler, C.7    Horn, D.8
  • 26
    • 41649095182 scopus 로고    scopus 로고
    • Intraflagellar transport and functional analysis of genes required for flagellum formation in trypanosomes
    • doi:10.1091/mbc.E07-08-0749
    • Absalon S, Blisnick T, Kohl L, Toutirais G, Dore G, Julkowska D, Tavenet A, Bastin P. 2008. Intraflagellar transport and functional analysis of genes required for flagellum formation in trypanosomes. Mol. Biol. Cell 19:929-944. doi:10.1091/mbc.E07-08-0749.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 929-944
    • Absalon, S.1    Blisnick, T.2    Kohl, L.3    Toutirais, G.4    Dore, G.5    Julkowska, D.6    Tavenet, A.7    Bastin, P.8
  • 27
    • 45149102845 scopus 로고    scopus 로고
    • Biogenesis of the trypanosome endo-exocytotic organelle is cytoskeleton mediated
    • doi:10.1371/journal.pbio.0060105
    • Bonhivers M, Nowacki S, Landrein N, Robinson DR. 2008. Biogenesis of the trypanosome endo-exocytotic organelle is cytoskeleton mediated. PLoS Biol. 6:e105. doi:10.1371/journal.pbio.0060105.
    • (2008) PLoS Biol. , vol.6
    • Bonhivers, M.1    Nowacki, S.2    Landrein, N.3    Robinson, D.R.4
  • 28
    • 65549110811 scopus 로고    scopus 로고
    • Combining RNA interference mutants and comparative proteomics to identify protein components and dependences in a eukaryotic flagellum
    • doi:10.1074/jbc.M808859200
    • Portman N, Lacomble S, Thomas B, McKean PG, Gull K. 2009. Combining RNA interference mutants and comparative proteomics to identify protein components and dependences in a eukaryotic flagellum. J. Biol. Chem. 284:5610-5619. doi:10.1074/jbc.M808859200.
    • (2009) J. Biol. Chem. , vol.284 , pp. 5610-5619
    • Portman, N.1    Lacomble, S.2    Thomas, B.3    McKean, P.G.4    Gull, K.5
  • 29
    • 36749050931 scopus 로고    scopus 로고
    • A repetitive protein essential for the flagellum attachment zone filament structure and function in Trypanosoma brucei
    • doi:10.1016/j.protis.2007.08.005
    • Vaughan S, Kohl L, Ngai I, Wheeler RJ, Gull K. 2008. A repetitive protein essential for the flagellum attachment zone filament structure and function in Trypanosoma brucei. Protist 159:127-136. doi:10.1016/j.protis.2007.08.005.
    • (2008) Protist , vol.159 , pp. 127-136
    • Vaughan, S.1    Kohl, L.2    Ngai, I.3    Wheeler, R.J.4    Gull, K.5
  • 30
    • 21344456996 scopus 로고    scopus 로고
    • Targeted and proximity-dependent promiscuous protein biotinylation by a mutant Escherichia coli biotin protein ligase
    • doi:10.1016/j.jnutbio.2005.03.017
    • Cronan JE. 2005. Targeted and proximity-dependent promiscuous protein biotinylation by a mutant Escherichia coli biotin protein ligase. J. Nutr. Biochem. 16:416-418. doi:10.1016/j.jnutbio.2005.03.017.
    • (2005) J. Nutr. Biochem. , vol.16 , pp. 416-418
    • Cronan, J.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.