메뉴 건너뛰기




Volumn 203, Issue 3, 2013, Pages 537-550

Lysosomal sorting receptors are essential for secretory granule biogenesis in Tetrahymena

Author keywords

[No Author keywords available]

Indexed keywords

SORTILIN;

EID: 84890172313     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201305086     Document Type: Article
Times cited : (42)

References (86)
  • 1
    • 0002061701 scopus 로고
    • Exocytosis: biogenesis, transport and secretion of trichocysts
    • H.-D. Görtz, editor. Springer-Verlag, Berlin.
    • Adoutte, A. 1988. Exocytosis: biogenesis, transport and secretion of trichocysts. In Paramecium. H.-D. Görtz, editor. Springer-Verlag, Berlin. 325-362.
    • (1988) Paramecium , pp. 325-362
    • Adoutte, A.1
  • 2
    • 0036701575 scopus 로고    scopus 로고
    • Lumenal protein multimerization in the distal secretory pathway/secretory granules
    • Arvan, P., B.Y. Zhang, L. Feng, M. Liu, and R. Kuliawat. 2002. Lumenal protein multimerization in the distal secretory pathway/secretory granules. Curr. Opin. Cell Biol. 14:448-453. http://dx.doi.org/10.1016/S0955-0674(02)00344-7
    • (2002) Curr. Opin. Cell Biol , vol.14 , pp. 448-453
    • Arvan, P.1    Zhang, B.Y.2    Feng, L.3    Liu, M.4    Kuliawat, R.5
  • 3
    • 78650152707 scopus 로고    scopus 로고
    • RNAi screen identifies a role for adaptor protein AP-3 in sorting to the regulated secretory pathway
    • Asensio, C.S., D.W. Sirkis, and R.H. Edwards. 2010. RNAi screen identifies a role for adaptor protein AP-3 in sorting to the regulated secretory pathway. J. Cell Biol. 191:1173-1187. http://dx.doi.org/10.1083/jcb.201006131
    • (2010) J. Cell Biol , vol.191 , pp. 1173-1187
    • Asensio, C.S.1    Sirkis, D.W.2    Edwards, R.H.3
  • 4
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • Bolte, S., and F.P. Cordelières. 2006. A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc. 224:213-232. http://dx.doi.org/10.1111/j.1365-2818.2006.01706.x
    • (2006) J. Microsc , vol.224 , pp. 213-232
    • Bolte, S.1    Cordelières, F.P.2
  • 5
    • 15844398287 scopus 로고    scopus 로고
    • Core formation and the acquisition of fusion competence are linked during secretory granule maturation in Tetrahymena
    • Bowman, G.R., N.C. Elde, G. Morgan, M. Winey, and A.P. Turkewitz. 2005a. Core formation and the acquisition of fusion competence are linked during secretory granule maturation in Tetrahymena. Traffic. 6:303-323. http://dx.doi.org/10.1111/j.1600-0854.2005.00273.x
    • (2005) Traffic , vol.6 , pp. 303-323
    • Bowman, G.R.1    Elde, N.C.2    Morgan, G.3    Winey, M.4    Turkewitz, A.P.5
  • 6
    • 27244452149 scopus 로고    scopus 로고
    • Genomic and proteomic evidence for a second family of dense core granule cargo proteins in Tetrahymena thermophila
    • Bowman, G.R., D.G. Smith, K.W. Michael Siu, R.E. Pearlman, and A.P. Turkewitz. 2005b. Genomic and proteomic evidence for a second family of dense core granule cargo proteins in Tetrahymena thermophila. J. Eukaryot. Microbiol. 52:291-297. http://dx.doi.org/10.1111/j.1550-7408.2005.00045.x
    • (2005) J. Eukaryot. Microbiol , vol.52 , pp. 291-297
    • Bowman, G.R.1    Smith, D.G.2    Michael Siu, K.W.3    Pearlman, R.E.4    Turkewitz, A.P.5
  • 7
    • 63149193317 scopus 로고    scopus 로고
    • Sorting of lysosomal proteins
    • Braulke, T., and J.S. Bonifacino. 2009. Sorting of lysosomal proteins. Biochim. Biophys. Acta. 1793:605-614. http://dx.doi.org/10.1016/j.bbamcr.2008.10.016
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 605-614
    • Braulke, T.1    Bonifacino, J.S.2
  • 8
    • 78449255389 scopus 로고    scopus 로고
    • Comprehensive analysis reveals dynamic and evolutionary plasticity of Rab GTPases and membrane traffic in Tetrahymena thermophila
    • Bright, L.J., N. Kambesis, S.B. Nelson, B. Jeong, and A.P. Turkewitz. 2010. Comprehensive analysis reveals dynamic and evolutionary plasticity of Rab GTPases and membrane traffic in Tetrahymena thermophila. PLoS Genet. 6:e1001155. http://dx.doi.org/10.1371/journal.pgen.1001155
    • (2010) PLoS Genet , vol.6
    • Bright, L.J.1    Kambesis, N.2    Nelson, S.B.3    Jeong, B.4    Turkewitz, A.P.5
  • 10
    • 63449103189 scopus 로고    scopus 로고
    • The interactomics of sortilin: an ancient lysosomal receptor evolving new functions
    • Canuel, M., Y. Libin, and C.R. Morales. 2009. The interactomics of sortilin: an ancient lysosomal receptor evolving new functions. Histol. Histopathol. 24:481-492.
    • (2009) Histol. Histopathol , vol.24 , pp. 481-492
    • Canuel, M.1    Libin, Y.2    Morales, C.R.3
  • 12
    • 0026338163 scopus 로고
    • Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network
    • Chanat, E., and W.B. Huttner. 1991. Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network. J. Cell Biol. 115:1505-1519. http://dx.doi.org/10.1083/jcb.115.6.1505
    • (1991) J. Cell Biol , vol.115 , pp. 1505-1519
    • Chanat, E.1    Huttner, W.B.2
  • 13
    • 21544461501 scopus 로고    scopus 로고
    • Sortilin controls intracellular sorting of brain-derived neurotrophic factor to the regulated secretory pathway
    • Chen, Z.Y., A. Ieraci, H. Teng, H. Dall, C.X. Meng, D.G. Herrera, A. Nykjaer, B.L. Hempstead, and F.S. Lee. 2005. Sortilin controls intracellular sorting of brain-derived neurotrophic factor to the regulated secretory pathway. J. Neurosci. 25:6156-6166. http://dx.doi.org/10.1523/JNEUROSCI.1017-05.2005
    • (2005) J. Neurosci , vol.25 , pp. 6156-6166
    • Chen, Z.Y.1    Ieraci, A.2    Teng, H.3    Dall, H.4    Meng, C.X.5    Herrera, D.G.6    Nykjaer, A.7    Hempstead, B.L.8    Lee, F.S.9
  • 14
    • 0019888460 scopus 로고
    • Post-translational cleavage of mucocyst precursors in Tetrahymena
    • Collins, T., and J.M. Wilhelm. 1981. Post-translational cleavage of mucocyst precursors in Tetrahymena. J. Biol. Chem. 256:10475-10484.
    • (1981) J. Biol. Chem , vol.256 , pp. 10475-10484
    • Collins, T.1    Wilhelm, J.M.2
  • 15
    • 24344486424 scopus 로고    scopus 로고
    • Genetic, genomic, and functional analysis of the granule lattice proteins in Tetrahymena secretory granules
    • Cowan, A.T., G.R. Bowman, K.F. Edwards, J.J. Emerson, and A.P. Turkewitz. 2005. Genetic, genomic, and functional analysis of the granule lattice proteins in Tetrahymena secretory granules. Mol. Biol. Cell. 16:4046-4060. http://dx.doi.org/10.1091/mbc. E05-01-0028
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4046-4060
    • Cowan, A.T.1    Bowman, G.R.2    Edwards, K.F.3    Emerson, J.J.4    Turkewitz, A.P.5
  • 16
    • 70349919803 scopus 로고    scopus 로고
    • Impaired dense core vesicle maturation in Caenorhabditis elegans mutants lacking Rab2
    • Edwards, S.L., N.K. Charlie, J.E. Richmond, J. Hegermann, S. Eimer, and K.G. Miller. 2009. Impaired dense core vesicle maturation in Caenorhabditis elegans mutants lacking Rab2. J. Cell Biol. 186:881-895. http://dx.doi.org/10.1083/jcb.200902095
    • (2009) J. Cell Biol , vol.186 , pp. 881-895
    • Edwards, S.L.1    Charlie, N.K.2    Richmond, J.E.3    Hegermann, J.4    Eimer, S.5    Miller, K.G.6
  • 17
    • 55449130503 scopus 로고    scopus 로고
    • Elucidation of clathrin-mediated endocytosis in tetrahymena reveals an evolutionarily convergent recruitment of dynamin
    • Elde, N.C., G. Morgan, M. Winey, L. Sperling, and A.P. Turkewitz. 2005. Elucidation of clathrin-mediated endocytosis in tetrahymena reveals an evolutionarily convergent recruitment of dynamin. PLoS Genet. 1:e52. http://dx.doi.org/10.1371/journal.pgen.0010052
    • (2005) PLoS Genet , vol.1
    • Elde, N.C.1    Morgan, G.2    Winey, M.3    Sperling, L.4    Turkewitz, A.P.5
  • 18
    • 33947726724 scopus 로고    scopus 로고
    • A role for convergent evolution in the secretory life of cells
    • Elde, N.C., M. Long, and A.P. Turkewitz. 2007. A role for convergent evolution in the secretory life of cells. Trends Cell Biol. 17:157-164. http://dx.doi.org/10.1016/j.tcb.2007.02.007
    • (2007) Trends Cell Biol , vol.17 , pp. 157-164
    • Elde, N.C.1    Long, M.2    Turkewitz, A.P.3
  • 19
    • 78349308399 scopus 로고    scopus 로고
    • Unique biological function of cathepsin L in secretory vesicles for biosynthesis of neuropeptides
    • Funkelstein, L., M. Beinfeld, A. Minokadeh, J. Zadina, and V. Hook. 2010. Unique biological function of cathepsin L in secretory vesicles for biosynthesis of neuropeptides. Neuropeptides. 44:457-466. http://dx.doi.org/10.1016/j.npep.2010.08.003
    • (2010) Neuropeptides , vol.44 , pp. 457-466
    • Funkelstein, L.1    Beinfeld, M.2    Minokadeh, A.3    Zadina, J.4    Hook, V.5
  • 20
    • 0002172130 scopus 로고
    • Early steps of the secretory pathway in Paramecium
    • H. Plattner, editor. JAI Press, Greenwich, CT.
    • Garreau de Loubresse, N. 1993. Early steps of the secretory pathway in Paramecium. In Membrane Traffic in Protozoa. Vol. 2. H. Plattner, editor. JAI Press, Greenwich, CT. 27-60.
    • (1993) Membrane Traffic in Protozoa , vol.2 , pp. 27-60
    • de Loubresse, N.G.1
  • 21
    • 33745589255 scopus 로고    scopus 로고
    • Regulation of large dense-core vesicle volume and neurotransmitter content mediated by adaptor protein 3
    • Grabner, C.P., S.D. Price, A. Lysakowski, A.L. Cahill, and A.P. Fox. 2006. Regulation of large dense-core vesicle volume and neurotransmitter content mediated by adaptor protein 3. Proc. Natl. Acad. Sci. USA. 103:10035-10040. http://dx.doi.org/10.1073/pnas.0509844103
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10035-10040
    • Grabner, C.P.1    Price, S.D.2    Lysakowski, A.3    Cahill, A.L.4    Fox, A.P.5
  • 22
    • 4444265485 scopus 로고    scopus 로고
    • Molecular defects that affect platelet dense granules
    • Gunay-Aygun, M., M. Huizing, and W.A. Gahl. 2004. Molecular defects that affect platelet dense granules. Semin. Thromb. Hemost. 30:537-547. http://dx.doi.org/10.1055/s-2004-835674
    • (2004) Semin. Thromb. Hemost , vol.30 , pp. 537-547
    • Gunay-Aygun, M.1    Huizing, M.2    Gahl, W.A.3
  • 23
    • 23044472125 scopus 로고    scopus 로고
    • Large-scale profiling of Rab GTPase trafficking networks: the membrome
    • Gurkan, C., H. Lapp, C. Alory, A.I. Su, J.B. Hogenesch, and W.E. Balch. 2005. Large-scale profiling of Rab GTPase trafficking networks: the membrome. Mol. Biol. Cell. 16:3847-3864. http://dx.doi.org/10.1091/mbc. E05-01-0062
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3847-3864
    • Gurkan, C.1    Lapp, H.2    Alory, C.3    Su, A.I.4    Hogenesch, J.B.5    Balch, W.E.6
  • 24
    • 0030886205 scopus 로고    scopus 로고
    • Analysis of exocytosis mutants indicates close coupling between regulated secretion and transcription activation in Tetrahymena
    • Haddad, A., and A.P. Turkewitz. 1997. Analysis of exocytosis mutants indicates close coupling between regulated secretion and transcription activation in Tetrahymena. Proc. Natl. Acad. Sci. USA. 94:10675-10680. http://dx.doi.org/10.1073/pnas.94.20.10675
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10675-10680
    • Haddad, A.1    Turkewitz, A.P.2
  • 25
    • 0036690508 scopus 로고    scopus 로고
    • New class of cargo protein in Tetrahymena thermophila dense core secretory granules
    • Haddad, A., G.R. Bowman, and A.P. Turkewitz. 2002. New class of cargo protein in Tetrahymena thermophila dense core secretory granules. Eukaryot. Cell. 1:583-593. http://dx.doi.org/10.1128/EC.1.4.583-593.2002
    • (2002) Eukaryot. Cell , vol.1 , pp. 583-593
    • Haddad, A.1    Bowman, G.R.2    Turkewitz, A.P.3
  • 26
    • 15844398287 scopus 로고    scopus 로고
    • Core formation and the acquisition of fusion competence are linked during secretory granule maturation in Tetrahymena
    • Bowman, G.R., N.C. Elde, G. Morgan, M. Winey, and A.P. Turkewitz. 2005a. Core formation and the acquisition of fusion competence are linked during secretory granule maturation in Tetrahymena. Traffic. 6:303-323. http://dx.doi.org/10.1111/j.1600-0854.2005.00273.x
    • (2005) Traffic , vol.6 , pp. 303-323
    • Bowman, G.R.1    Elde, N.C.2    Morgan, G.3    Winey, M.4    Turkewitz, A.P.5
  • 27
    • 27244452149 scopus 로고    scopus 로고
    • Genomic and proteomic evidence for a second family of dense core granule cargo proteins in Tetrahymena thermophila
    • Bowman, G.R., D.G. Smith, K.W. Michael Siu, R.E. Pearlman, and A.P. Turkewitz. 2005b. Genomic and proteomic evidence for a second family of dense core granule cargo proteins in Tetrahymena thermophila. J. Eukaryot. Microbiol. 52:291-297. http://dx.doi.org/10.1111/j.1550-7408.2005.00045.x
    • (2005) J. Eukaryot. Microbiol , vol.52 , pp. 291-297
    • Bowman, G.R.1    Smith, D.G.2    Michael Siu, K.W.3    Pearlman, R.E.4    Turkewitz, A.P.5
  • 28
    • 63149193317 scopus 로고    scopus 로고
    • Sorting of lysosomal proteins
    • Braulke, T., and J.S. Bonifacino. 2009. Sorting of lysosomal proteins. Biochim. Biophys. Acta. 1793:605-614. http://dx.doi.org/10.1016/j.bbamcr.2008.10.016
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 605-614
    • Braulke, T.1    Bonifacino, J.S.2
  • 29
    • 78449255389 scopus 로고    scopus 로고
    • Comprehensive analysis reveals dynamic and evolutionary plasticity of Rab GTPases and membrane traffic in Tetrahymena thermophila
    • Bright, L.J., N. Kambesis, S.B. Nelson, B. Jeong, and A.P. Turkewitz. 2010. Comprehensive analysis reveals dynamic and evolutionary plasticity of Rab GTPases and membrane traffic in Tetrahymena thermophila. PLoS Genet. 6:e1001155. http://dx.doi.org/10.1371/journal.pgen.1001155
    • (2010) PLoS Genet , vol.6
    • Bright, L.J.1    Kambesis, N.2    Nelson, S.B.3    Jeong, B.4    Turkewitz, A.P.5
  • 31
    • 63449103189 scopus 로고    scopus 로고
    • The interactomics of sortilin: an ancient lysosomal receptor evolving new functions
    • Canuel, M., Y. Libin, and C.R. Morales. 2009. The interactomics of sortilin: an ancient lysosomal receptor evolving new functions. Histol. Histopathol. 24:481-492.
    • (2009) Histol. Histopathol , vol.24 , pp. 481-492
    • Canuel, M.1    Libin, Y.2    Morales, C.R.3
  • 33
    • 0026338163 scopus 로고
    • Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network
    • Chanat, E., and W.B. Huttner. 1991. Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network. J. Cell Biol. 115:1505-1519. http://dx.doi.org/10.1083/jcb.115.6.1505
    • (1991) J. Cell Biol , vol.115 , pp. 1505-1519
    • Chanat, E.1    Huttner, W.B.2
  • 34
    • 21544461501 scopus 로고    scopus 로고
    • Sortilin controls intracellular sorting of brain-derived neurotrophic factor to the regulated secretory pathway
    • Chen, Z.Y., A. Ieraci, H. Teng, H. Dall, C.X. Meng, D.G. Herrera, A. Nykjaer, B.L. Hempstead, and F.S. Lee. 2005. Sortilin controls intracellular sorting of brain-derived neurotrophic factor to the regulated secretory pathway. J. Neurosci. 25:6156-6166. http://dx.doi.org/10.1523/JNEUROSCI.1017-05.2005
    • (2005) J. Neurosci , vol.25 , pp. 6156-6166
    • Chen, Z.Y.1    Ieraci, A.2    Teng, H.3    Dall, H.4    Meng, C.X.5    Herrera, D.G.6    Nykjaer, A.7    Hempstead, B.L.8    Lee, F.S.9
  • 35
    • 0019888460 scopus 로고
    • Post-translational cleavage of mucocyst precursors in Tetrahymena
    • Collins, T., and J.M. Wilhelm. 1981. Post-translational cleavage of mucocyst precursors in Tetrahymena. J. Biol. Chem. 256:10475-10484.
    • (1981) J. Biol. Chem , vol.256 , pp. 10475-10484
    • Collins, T.1    Wilhelm, J.M.2
  • 36
    • 24344486424 scopus 로고    scopus 로고
    • Genetic, genomic, and functional analysis of the granule lattice proteins in Tetrahymena secretory granules
    • Cowan, A.T., G.R. Bowman, K.F. Edwards, J.J. Emerson, and A.P. Turkewitz. 2005. Genetic, genomic, and functional analysis of the granule lattice proteins in Tetrahymena secretory granules. Mol. Biol. Cell. 16:4046-4060. http://dx.doi.org/10.1091/mbc. E05-01-0028
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4046-4060
    • Cowan, A.T.1    Bowman, G.R.2    Edwards, K.F.3    Emerson, J.J.4    Turkewitz, A.P.5
  • 37
    • 70349919803 scopus 로고    scopus 로고
    • Impaired dense core vesicle maturation in Caenorhabditis elegans mutants lacking Rab2
    • Edwards, S.L., N.K. Charlie, J.E. Richmond, J. Hegermann, S. Eimer, and K.G. Miller. 2009. Impaired dense core vesicle maturation in Caenorhabditis elegans mutants lacking Rab2. J. Cell Biol. 186:881-895. http://dx.doi.org/10.1083/jcb.200902095
    • (2009) J. Cell Biol , vol.186 , pp. 881-895
    • Edwards, S.L.1    Charlie, N.K.2    Richmond, J.E.3    Hegermann, J.4    Eimer, S.5    Miller, K.G.6
  • 38
    • 55449130503 scopus 로고    scopus 로고
    • Elucidation of clathrin-mediated endocytosis in tetrahymena reveals an evolutionarily convergent recruitment of dynamin
    • Elde, N.C., G. Morgan, M. Winey, L. Sperling, and A.P. Turkewitz. 2005. Elucidation of clathrin-mediated endocytosis in tetrahymena reveals an evolutionarily convergent recruitment of dynamin. PLoS Genet. 1:e52. http://dx.doi.org/10.1371/journal.pgen.0010052
    • (2005) PLoS Genet , vol.1
    • Elde, N.C.1    Morgan, G.2    Winey, M.3    Sperling, L.4    Turkewitz, A.P.5
  • 39
    • 33947726724 scopus 로고    scopus 로고
    • A role for convergent evolution in the secretory life of cells
    • Elde, N.C., M. Long, and A.P. Turkewitz. 2007. A role for convergent evolution in the secretory life of cells. Trends Cell Biol. 17:157-164. http://dx.doi.org/10.1016/j.tcb.2007.02.007
    • (2007) Trends Cell Biol , vol.17 , pp. 157-164
    • Elde, N.C.1    Long, M.2    Turkewitz, A.P.3
  • 40
    • 78349308399 scopus 로고    scopus 로고
    • Unique biological function of cathepsin L in secretory vesicles for biosynthesis of neuropeptides
    • Funkelstein, L., M. Beinfeld, A. Minokadeh, J. Zadina, and V. Hook. 2010. Unique biological function of cathepsin L in secretory vesicles for biosynthesis of neuropeptides. Neuropeptides. 44:457-466. http://dx.doi.org/10.1016/j.npep.2010.08.003
    • (2010) Neuropeptides , vol.44 , pp. 457-466
    • Funkelstein, L.1    Beinfeld, M.2    Minokadeh, A.3    Zadina, J.4    Hook, V.5
  • 41
    • 0002172130 scopus 로고
    • Early steps of the secretory pathway in Paramecium
    • H. Plattner, editor. JAI Press, Greenwich, CT.
    • Garreau de Loubresse, N. 1993. Early steps of the secretory pathway in Paramecium. In Membrane Traffic in Protozoa. Vol. 2. H. Plattner, editor. JAI Press, Greenwich, CT. 27-60.
    • (1993) Membrane Traffic in Protozoa , vol.2 , pp. 27-60
    • de Loubresse, N.G.1
  • 42
    • 33745589255 scopus 로고    scopus 로고
    • Regulation of large dense-core vesicle volume and neurotransmitter content mediated by adaptor protein 3
    • Grabner, C.P., S.D. Price, A. Lysakowski, A.L. Cahill, and A.P. Fox. 2006. Regulation of large dense-core vesicle volume and neurotransmitter content mediated by adaptor protein 3. Proc. Natl. Acad. Sci. USA. 103:10035-10040. http://dx.doi.org/10.1073/pnas.0509844103
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10035-10040
    • Grabner, C.P.1    Price, S.D.2    Lysakowski, A.3    Cahill, A.L.4    Fox, A.P.5
  • 43
    • 4444265485 scopus 로고    scopus 로고
    • Molecular defects that affect platelet dense granules
    • Gunay-Aygun, M., M. Huizing, and W.A. Gahl. 2004. Molecular defects that affect platelet dense granules. Semin. Thromb. Hemost. 30:537-547. http://dx.doi.org/10.1055/s-2004-835674
    • (2004) Semin. Thromb. Hemost , vol.30 , pp. 537-547
    • Gunay-Aygun, M.1    Huizing, M.2    Gahl, W.A.3
  • 44
    • 23044472125 scopus 로고    scopus 로고
    • Large-scale profiling of Rab GTPase trafficking networks: the membrome
    • Gurkan, C., H. Lapp, C. Alory, A.I. Su, J.B. Hogenesch, and W.E. Balch. 2005. Large-scale profiling of Rab GTPase trafficking networks: the membrome. Mol. Biol. Cell. 16:3847-3864. http://dx.doi.org/10.1091/mbc. E05-01-0062
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3847-3864
    • Gurkan, C.1    Lapp, H.2    Alory, C.3    Su, A.I.4    Hogenesch, J.B.5    Balch, W.E.6
  • 45
    • 0030886205 scopus 로고    scopus 로고
    • Analysis of exocytosis mutants indicates close coupling between regulated secretion and transcription activation in Tetrahymena
    • Haddad, A., and A.P. Turkewitz. 1997. Analysis of exocytosis mutants indicates close coupling between regulated secretion and transcription activation in Tetrahymena. Proc. Natl. Acad. Sci. USA. 94:10675-10680. http://dx.doi.org/10.1073/pnas.94.20.10675
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10675-10680
    • Haddad, A.1    Turkewitz, A.P.2
  • 46
    • 0036690508 scopus 로고    scopus 로고
    • New class of cargo protein in Tetrahymena thermophila dense core secretory granules
    • Haddad, A., G.R. Bowman, and A.P. Turkewitz. 2002. New class of cargo protein in Tetrahymena thermophila dense core secretory granules. Eukaryot. Cell. 1:583-593. http://dx.doi.org/10.1128/EC.1.4.583-593.2002
    • (2002) Eukaryot. Cell , vol.1 , pp. 583-593
    • Haddad, A.1    Bowman, G.R.2    Turkewitz, A.P.3
  • 47
    • 68549128595 scopus 로고    scopus 로고
    • The Vps10p-domain receptor family
    • Hermey, G. 2009. The Vps10p-domain receptor family. Cell. Mol. Life Sci. 66:2677-2689. http://dx.doi.org/10.1007/s00018-009-0043-1
    • (2009) Cell. Mol. Life Sci , vol.66 , pp. 2677-2689
    • Hermey, G.1
  • 48
    • 0026753044 scopus 로고
    • Genetic characterization of the secretory mutant MS-1 of Tetrahymena thermophila: vacuolarization and block in secretion of lysosomal hydrolases are caused by a single gene mutation
    • Hünseler, P., and A. Tiedtke. 1992. Genetic characterization of the secretory mutant MS-1 of Tetrahymena thermophila: vacuolarization and block in secretion of lysosomal hydrolases are caused by a single gene mutation. Dev. Genet. 13:167-173. http://dx.doi.org/10.1002/dvg.1020130211
    • (1992) Dev. Genet , vol.13 , pp. 167-173
    • Hünseler, P.1    Tiedtke, A.2
  • 49
    • 0023386996 scopus 로고
    • Isolation and characterization of a mutant of Tetrahymena thermophila blocked in secretion of lysosomal enzymes
    • Hünseler, P., G. Scheidgen-Kleyboldt, and A. Tiedtke. 1987. Isolation and characterization of a mutant of Tetrahymena thermophila blocked in secretion of lysosomal enzymes. J. Cell Sci. 88:47-55.
    • (1987) J. Cell Sci , vol.88 , pp. 47-55
    • Hünseler, P.1    Scheidgen-Kleyboldt, G.2    Tiedtke, A.3
  • 50
    • 0023933578 scopus 로고
    • Biosynthesis of secreted betahexosaminidase in Tetrahymena thermophila. A comparison of the wild type with a secretory mutant
    • Hünseler, P., A. Tiedtke, and K. von Figura. 1988. Biosynthesis of secreted betahexosaminidase in Tetrahymena thermophila. A comparison of the wild type with a secretory mutant. Biochem. J. 252:837-842.
    • (1988) Biochem. J , vol.252 , pp. 837-842
    • Hünseler, P.1    Tiedtke, A.2    von Figura, K.3
  • 53
    • 79955548766 scopus 로고    scopus 로고
    • Evolutionary reconstruction of the retromer complex and its function in Trypanosoma brucei
    • Koumandou, V.L., M.J. Klute, E.K. Herman, R. Nunez-Miguel, J.B. Dacks, and M.C. Field. 2011. Evolutionary reconstruction of the retromer complex and its function in Trypanosoma brucei. J. Cell Sci. 124:1496-1509. http://dx.doi.org/10.1242/jcs.081596
    • (2011) J. Cell Sci , vol.124 , pp. 1496-1509
    • Koumandou, V.L.1    Klute, M.J.2    Herman, E.K.3    Nunez-Miguel, R.4    Dacks, J.B.5    Field, M.C.6
  • 55
    • 0026695156 scopus 로고
    • Protein targeting via the "constitutive-like" secretory pathway in isolated pancreatic islets: passive sorting in the immature granule compartment
    • Kuliawat, R., and P. Arvan. 1992. Protein targeting via the "constitutive-like" secretory pathway in isolated pancreatic islets: passive sorting in the immature granule compartment. J. Cell Biol. 118:521-529. http://dx.doi.org/10.1083/jcb.118.3.521
    • (1992) J. Cell Biol , vol.118 , pp. 521-529
    • Kuliawat, R.1    Arvan, P.2
  • 56
    • 0027351866 scopus 로고
    • The Golgi apparatus of Tetrahymena thermophila
    • Kurz, S., and A. Tiedtke. 1993. The Golgi apparatus of Tetrahymena thermophila. J. Eukaryot. Microbiol. 40:10-13. http://dx.doi.org/10.1111/j.1550-7408.1993.tb04874.x
    • (1993) J. Eukaryot. Microbiol , vol.40 , pp. 10-13
    • Kurz, S.1    Tiedtke, A.2
  • 57
    • 0026586401 scopus 로고
    • Secretory organelles of Paramecium cells (trichocysts) are not remarkably acidic compartments
    • Lumpert, C.J., R. Glas-Albrecht, E. Eisenmann, and H. Plattner. 1992. Secretory organelles of Paramecium cells (trichocysts) are not remarkably acidic compartments. J. Histochem. Cytochem. 40:153-160. http://dx.doi.org/10.1177/40.1.1370309
    • (1992) J. Histochem. Cytochem , vol.40 , pp. 153-160
    • Lumpert, C.J.1    Glas-Albrecht, R.2    Eisenmann, E.3    Plattner, H.4
  • 58
    • 0029019520 scopus 로고
    • A large multigene family codes for the polypeptides of the crystalline trichocyst matrix in Paramecium
    • Madeddu, L., M.C. Gautier, L. Vayssié, A. Houari, and L. Sperling. 1995. A large multigene family codes for the polypeptides of the crystalline trichocyst matrix in Paramecium. Mol. Biol. Cell. 6:649-659. http://dx.doi.org/10.1091/mbc.6.6.649
    • (1995) Mol. Biol. Cell , vol.6 , pp. 649-659
    • Madeddu, L.1    Gautier, M.C.2    Vayssié, L.3    Houari, A.4    Sperling, L.5
  • 59
    • 0028332917 scopus 로고
    • The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene
    • Marcusson, E.G., B.F. Horazdovsky, J.L. Cereghino, E. Gharakhanian, and S.D. Emr. 1994. The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene. Cell. 77:579-586. http://dx.doi.org/10.1016/0092-8674(94)90219-4
    • (1994) Cell , vol.77 , pp. 579-586
    • Marcusson, E.G.1    Horazdovsky, B.F.2    Cereghino, J.L.3    Gharakhanian, E.4    Emr, S.D.5
  • 60
    • 0347915585 scopus 로고    scopus 로고
    • Requirements for the identification of dense-core granules
    • Meldolesi, J., E. Chieregatti, and M. Luisa Malosio. 2004. Requirements for the identification of dense-core granules. Trends Cell Biol. 14:13-19. http://dx.doi.org/10.1016/j.tcb.2003.11.006
    • (2004) Trends Cell Biol , vol.14 , pp. 13-19
    • Meldolesi, J.1    Chieregatti, E.2    Luisa Malosio, M.3
  • 61
    • 0031985394 scopus 로고    scopus 로고
    • Mutational analysis of regulated exocytosis in Tetrahymena
    • Melia, S.M., E.S. Cole, and A.P. Turkewitz. 1998. Mutational analysis of regulated exocytosis in Tetrahymena. J. Cell Sci. 111:131-140.
    • (1998) J. Cell Sci , vol.111 , pp. 131-140
    • Melia, S.M.1    Cole, E.S.2    Turkewitz, A.P.3
  • 62
    • 39849096993 scopus 로고    scopus 로고
    • Discovery and progress in our understanding of the regulated secretory pathway in neuroendocrine cells
    • Morvan, J., and S.A. Tooze. 2008. Discovery and progress in our understanding of the regulated secretory pathway in neuroendocrine cells. Histochem. Cell Biol. 129:243-252. http://dx.doi.org/10.1007/s00418-008-0377-z
    • (2008) Histochem. Cell Biol , vol.129 , pp. 243-252
    • Morvan, J.1    Tooze, S.A.2
  • 63
    • 3042557931 scopus 로고    scopus 로고
    • Are rhoptries in Apicomplexan parasites secretory granules or secretory lysosomal granules?
    • Ngô, H.M., M. Yang, and K.A. Joiner. 2004. Are rhoptries in Apicomplexan parasites secretory granules or secretory lysosomal granules? Mol. Microbiol. 52:1531-1541. http://dx.doi.org/10.1111/j.1365-2958.2004.04056.x
    • (2004) Mol. Microbiol , vol.52 , pp. 1531-1541
    • Ngô, H.M.1    Yang, M.2    Joiner, K.A.3
  • 64
    • 84858722452 scopus 로고    scopus 로고
    • Conservation and innovation in Tetrahymena membrane traffic: proteins, lipids, and compartments
    • Nusblat, A.D., L.J. Bright, and A.P. Turkewitz. 2012. Conservation and innovation in Tetrahymena membrane traffic: proteins, lipids, and compartments. Methods Cell Biol. 109:141-175. http://dx.doi.org/10.1016/B978-0-12-385967-9.00006-2
    • (2012) Methods Cell Biol , vol.109 , pp. 141-175
    • Nusblat, A.D.1    Bright, L.J.2    Turkewitz, A.P.3
  • 65
    • 0032404443 scopus 로고    scopus 로고
    • The AP-3 complex: a coat of many colours
    • Odorizzi, G., C.R. Cowles, and S.D. Emr. 1998. The AP-3 complex: a coat of many colours. Trends Cell Biol. 8:282-288. http://dx.doi.org/10.1016/S0962-8924(98)01295-1
    • (1998) Trends Cell Biol , vol.8 , pp. 282-288
    • Odorizzi, G.1    Cowles, C.R.2    Emr, S.D.3
  • 66
    • 0020855138 scopus 로고
    • Isolation and ultrastructural characterization of secretory mutants of Tetrahymena thermophila
    • Orias, E., M. Flacks, and B.H. Satir. 1983. Isolation and ultrastructural characterization of secretory mutants of Tetrahymena thermophila. J. Cell Sci. 64:49-67.
    • (1983) J. Cell Sci , vol.64 , pp. 49-67
    • Orias, E.1    Flacks, M.2    Satir, B.H.3
  • 67
    • 0345084625 scopus 로고
    • Involvement of the trans-Golgi network, coated vesicles, vesicle fusion, and secretory product condensation in the biogenesis of Pseudomicrothorax trichocysts
    • H. Plattner, editor. JAI Press, Greenwich, CT.
    • Peck, R.K., B. Swiderski, and A.M. Tourmel. 1993. Involvement of the trans-Golgi network, coated vesicles, vesicle fusion, and secretory product condensation in the biogenesis of Pseudomicrothorax trichocysts. In Membrane Traffic in Protozoa. Vol. 2. H. Plattner, editor. JAI Press, Greenwich, CT. 1-26.
    • (1993) Membrane Traffic in Protozoa , vol.2 , pp. 1-26
    • Peck, R.K.1    Swiderski, B.2    Tourmel, A.M.3
  • 68
    • 70349696856 scopus 로고    scopus 로고
    • Independent transport and sorting of functionally distinct protein families in Tetrahymena thermophila dense core secretory granules
    • Rahaman, A., W. Miao, and A.P. Turkewitz. 2009. Independent transport and sorting of functionally distinct protein families in Tetrahymena thermophila dense core secretory granules. Eukaryot. Cell. 8:1575-1583. http://dx.doi.org/10.1128/EC.00151-09
    • (2009) Eukaryot. Cell , vol.8 , pp. 1575-1583
    • Rahaman, A.1    Miao, W.2    Turkewitz, A.P.3
  • 69
    • 0347694809 scopus 로고    scopus 로고
    • Extrusomes in ciliates: diversification, distribution, and phylogenetic implications
    • Rosati, G., and L. Modeo. 2003. Extrusomes in ciliates: diversification, distribution, and phylogenetic implications. J. Eukaryot. Microbiol. 50:383-402. http://dx.doi.org/10.1111/j.1550-7408.2003.tb00260.x
    • (2003) J. Eukaryot. Microbiol , vol.50 , pp. 383-402
    • Rosati, G.1    Modeo, L.2
  • 70
    • 0017369897 scopus 로고
    • Dibucaine-induced synchronous mucocyst secretion in Tetrahymena
    • Satir, B. 1977. Dibucaine-induced synchronous mucocyst secretion in Tetrahymena. Cell Biol. Int. Rep. 1:69-73. http://dx.doi.org/10.1016/0309-1651(77)90012-1
    • (1977) Cell Biol. Int. Rep , vol.1 , pp. 69-73
    • Satir, B.1
  • 71
    • 0037133578 scopus 로고    scopus 로고
    • A robust inducible-repressible promoter greatly facilitates gene knockouts, conditional expression, and overexpression of homologous and heterologous genes in Tetrahymena thermophila
    • Shang, Y., X. Song, J. Bowen, R. Corstanje, Y. Gao, J. Gaertig, and M.A. Gorovsky. 2002. A robust inducible-repressible promoter greatly facilitates gene knockouts, conditional expression, and overexpression of homologous and heterologous genes in Tetrahymena thermophila. Proc. Natl. Acad. Sci. USA. 99:3734-3739. http://dx.doi.org/10.1073/pnas.052016199
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3734-3739
    • Shang, Y.1    Song, X.2    Bowen, J.3    Corstanje, R.4    Gao, Y.5    Gaertig, J.6    Gorovsky, M.A.7
  • 73
    • 0041955201 scopus 로고    scopus 로고
    • Phylogenetic analysis of eukaryotes using heat-shock protein Hsp90
    • Stechmann, A., and T. Cavalier-Smith. 2003. Phylogenetic analysis of eukaryotes using heat-shock protein Hsp90. J. Mol. Evol. 57:408-419. http://dx.doi.org/10.1007/s00239-003-2490-x
    • (2003) J. Mol. Evol , vol.57 , pp. 408-419
    • Stechmann, A.1    Cavalier-Smith, T.2
  • 74
    • 70349916647 scopus 로고    scopus 로고
    • UNC-108/RAB-2 and its effector RIC-19 are involved in dense core vesicle maturation in Caenorhabditis elegans
    • Sumakovic, M., J. Hegermann, L. Luo, S.J. Husson, K. Schwarze, C. Olendrowitz, L. Schoofs, J. Richmond, and S. Eimer. 2009. UNC-108/RAB-2 and its effector RIC-19 are involved in dense core vesicle maturation in Caenorhabditis elegans. J. Cell Biol. 186:897-914. http://dx.doi.org/10.1083/jcb.200902096
    • (2009) J. Cell Biol , vol.186 , pp. 897-914
    • Sumakovic, M.1    Hegermann, J.2    Luo, L.3    Husson, S.J.4    Schwarze, K.5    Olendrowitz, C.6    Schoofs, L.7    Richmond, J.8    Eimer, S.9
  • 75
    • 0016924064 scopus 로고
    • Capsule shedding in tetrahymena
    • Tiedtke, A. 1976. Capsule shedding in tetrahymena. Naturwissenschaften. 63:93. http://dx.doi.org/10.1007/BF00622415
    • (1976) Naturwissenschaften , vol.63 , pp. 93
    • Tiedtke, A.1
  • 76
    • 0025248051 scopus 로고
    • Cell-free protein sorting to the regulated and constitutive secretory pathways
    • Tooze, S.A., and W.B. Huttner. 1990. Cell-free protein sorting to the regulated and constitutive secretory pathways. Cell. 60:837-847. http://dx.doi.org/10.1016/0092-8674(90)90097-X
    • (1990) Cell , vol.60 , pp. 837-847
    • Tooze, S.A.1    Huttner, W.B.2
  • 77
    • 1042268889 scopus 로고    scopus 로고
    • Out with a bang! Tetrahymena as a model system to study secretory granule biogenesis
    • Turkewitz, A.P. 2004. Out with a bang! Tetrahymena as a model system to study secretory granule biogenesis. Traffic. 5:63-68. http://dx.doi.org/10.1046/j.1600-0854.2003.00155.x
    • (2004) Traffic , vol.5 , pp. 63-68
    • Turkewitz, A.P.1
  • 78
    • 0025815320 scopus 로고
    • Maturation of dense core granules in wild type and mutant Tetrahymena thermophila
    • Turkewitz, A.P., L. Madeddu, and R.B. Kelly. 1991. Maturation of dense core granules in wild type and mutant Tetrahymena thermophila. EMBO J. 10:1979-1987.
    • (1991) EMBO J , vol.10 , pp. 1979-1987
    • Turkewitz, A.P.1    Madeddu, L.2    Kelly, R.B.3
  • 79
    • 84859745968 scopus 로고    scopus 로고
    • Biochemically distinct vesicles from the endoplasmic reticulum fuse to form peroxisomes
    • van der Zand, A., J. Gent, I. Braakman, and H.F. Tabak. 2012. Biochemically distinct vesicles from the endoplasmic reticulum fuse to form peroxisomes. Cell. 149:397-409. http://dx.doi.org/10.1016/j.cell.2012.01.054
    • (2012) Cell , vol.149 , pp. 397-409
    • van der Zand, A.1    Gent, J.2    Braakman, I.3    Tabak, H.F.4
  • 80
    • 0035065377 scopus 로고    scopus 로고
    • Growth and form of secretory granules involves stepwise assembly but not differential sorting of a family of secretory proteins in Paramecium
    • Vayssié, L., N. Garreau de Loubresse, and L. Sperling. 2001. Growth and form of secretory granules involves stepwise assembly but not differential sorting of a family of secretory proteins in Paramecium. J. Cell Sci. 114:875-886.
    • (2001) J. Cell Sci , vol.114 , pp. 875-886
    • Vayssié, L.1    de Loubresse, N.G.2    Sperling, L.3
  • 81
    • 0031594225 scopus 로고    scopus 로고
    • Proteolytic processing and Ca2+-binding activity of dense-core vesicle polypeptides in Tetrahymena
    • Verbsky, J.W., and A.P. Turkewitz. 1998. Proteolytic processing and Ca2+-binding activity of dense-core vesicle polypeptides in Tetrahymena. Mol. Biol. Cell. 9:497-511. http://dx.doi.org/10.1091/mbc.9.2.497
    • (1998) Mol. Biol. Cell , vol.9 , pp. 497-511
    • Verbsky, J.W.1    Turkewitz, A.P.2
  • 82
    • 78751660222 scopus 로고    scopus 로고
    • Tetrahymena Gene Expression Database (TGED): a resource of microarray data and co-expression analyses for Tetrahymena
    • Xiong, J., X. Lu, Y. Lu, H. Zeng, D. Yuan, L. Feng, Y. Chang, J. Bowen, M. Gorovsky, C. Fu, and W. Miao. 2011. Tetrahymena Gene Expression Database (TGED): a resource of microarray data and co-expression analyses for Tetrahymena. Sci China Life Sci. 54:65-67. http://dx.doi.org/10.1007/s11427-010-4114-1
    • (2011) Sci China Life Sci , vol.54 , pp. 65-67
    • Xiong, J.1    Lu, X.2    Lu, Y.3    Zeng, H.4    Yuan, D.5    Feng, L.6    Chang, Y.7    Bowen, J.8    Gorovsky, M.9    Fu, C.10    Miao, W.11
  • 83
    • 0026046407 scopus 로고
    • Transformation of Tetrahymena to cycloheximide resistance with a ribosomal protein gene through sequence replacement
    • Yao, M.C., and C.H. Yao. 1991. Transformation of Tetrahymena to cycloheximide resistance with a ribosomal protein gene through sequence replacement. Proc. Natl. Acad. Sci. USA. 88:9493-9497. http://dx.doi.org/10.1073/pnas.88.21.9493
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9493-9497
    • Yao, M.C.1    Yao, C.H.2
  • 84
    • 84867744264 scopus 로고    scopus 로고
    • Evolution of the cancer genome
    • Yates, L.R., and P.J. Campbell. 2012. Evolution of the cancer genome. Nat. Rev. Genet. 13:795-806. http://dx.doi.org/10.1038/nrg3317
    • (2012) Nat. Rev. Genet , vol.13 , pp. 795-806
    • Yates, L.R.1    Campbell, P.J.2
  • 85
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias, D.A., J.D. Violin, A.C. Newton, and R.Y. Tsien. 2002. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science. 296:913-916. http://dx.doi.org/10.1126/science.1068539
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 86
    • 84866152524 scopus 로고    scopus 로고
    • Adaptive evolution of voltage-gated sodium channels: the first 800 million years
    • Zakon, H.H. 2012. Adaptive evolution of voltage-gated sodium channels: the first 800 million years. Proc. Natl. Acad. Sci. USA. 109(Suppl 1):10619-10625. http://dx.doi.org/10.1073/pnas.1201884109
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , Issue.SUPPL. 1 , pp. 10619-10625
    • Zakon, H.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.