메뉴 건너뛰기




Volumn 81, Issue 9, 2002, Pages 485-495

Targeting of the GRIP domain to the trans-Golgi network is conserved from protists to animals

Author keywords

GRIP domain; Leishmania mexicana; trans Golgi network; Trypanosoma brucei; Vesicular transport

Indexed keywords

GREEN FLUORESCENT PROTEIN; GRIP PROTEIN; MEMBRANE PROTEIN; TYROSINE; UNCLASSIFIED DRUG; SIGNAL PEPTIDE;

EID: 0036750509     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1078/0171-9335-00268     Document Type: Article
Times cited : (45)

References (44)
  • 1
    • 0033535617 scopus 로고    scopus 로고
    • A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-coil proteins
    • Barr, F. A. (1999): A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-coil proteins. Curr. Biol. 9, 381-384.
    • (1999) Curr. Biol , vol.9 , pp. 381-384
    • Barr, F.A.1
  • 2
    • 0033620656 scopus 로고    scopus 로고
    • Molecular basis for the recognition of tryosine-based sorting signals
    • Bonifacino, J. S., Dell'Angelica, E. C. (1999): Molecular basis for the recognition of tryosine-based sorting signals. J. Cell Biol. 145, 923-926.
    • (1999) J. Cell Biol , vol.145 , pp. 923-926
    • Bonifacino, J.S.1    Dell'Angelica, E.C.2
  • 3
    • 0035013167 scopus 로고    scopus 로고
    • The GRIP domain is a specific targeting sequence for a population of trans-Golgi network derived tubulo-vesicular carriers
    • Brown, D. L., Heimann, K., Lock, J., Kjer-Nielsen, L., van Vliet, C., Stow, J. L., Gleeson, P. A. (2001): The GRIP domain is a specific targeting sequence for a population of trans-Golgi network derived tubulo-vesicular carriers. Traffic 2, 336-344.
    • (2001) Traffic , vol.2 , pp. 336-344
    • Brown, D.L.1    Heimann, K.2    Lock, J.3    Kjer-Nielsen, L.4    van Vliet, C.5    Stow, J.L.6    Gleeson, P.A.7
  • 4
    • 0027378869 scopus 로고
    • Cloning and characterization of a Golgi-associated GTP-binding protein homologue from Leishmania major
    • Cappai, R., Osborn, A. H., Gleeson, P. A., Handman, E. (1993): Cloning and characterization of a Golgi-associated GTP-binding protein homologue from Leishmania major Mol. Biochem. Parasitol. 62, 73-82.
    • (1993) Mol. Biochem. Parasitol , vol.62 , pp. 73-82
    • Cappai, R.1    Osborn, A.H.2    Gleeson, P.A.3    Handman, E.4
  • 5
    • 0035166326 scopus 로고    scopus 로고
    • Yeast Gga coat proteins function with clathrin in Golgi to endosome transport
    • Costaguta, G., Stefan, C. J., Bensen, E. S., Emr, S. D., Payne, G. S. (2001): Yeast Gga coat proteins function with clathrin in Golgi to endosome transport. Mol. Biol. Cell 12, 1885-1896.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1885-1896
    • Costaguta, G.1    Stefan, C.J.2    Bensen, E.S.3    Emr, S.D.4    Payne, G.S.5
  • 6
    • 0035975965 scopus 로고    scopus 로고
    • Modular phosphoinositide-binding domains - Their role in signalling and membrane trafficking
    • Cullen, P. J., Cozier, G. E., Banting, G., Mellor, H. (2001): Modular phosphoinositide-binding domains - their role in signalling and membrane trafficking. Curr. Biol. 11, R882-R893.
    • (2001) Curr. Biol , vol.11
    • Cullen, P.J.1    Cozier, G.E.2    Banting, G.3    Mellor, H.4
  • 7
    • 0023928669 scopus 로고
    • Intracellular transport of a variant surface glycoprotein in Trypanosoma brucei
    • Duszenko, M., Ivanov, I. E., Ferguson, M. A., Plesken, H., Cross, G. A. (1988): Intracellular transport of a variant surface glycoprotein in Trypanosoma brucei. J. Cell Biol. 106, 77-86.
    • (1988) J. Cell Biol , vol.106 , pp. 77-86
    • Duszenko, M.1    Ivanov, I.E.2    Ferguson, M.A.3    Plesken, H.4    Cross, G.A.5
  • 8
    • 0021341229 scopus 로고
    • Surface membrane localization of 3′-and 5′-nucleotidase activities in Leishmania donovani promastigotes
    • Dwyer, D. M., Gottlieb, M. (1984): Surface membrane localization of 3′-and 5′-nucleotidase activities in Leishmania donovani promastigotes. Mol. Biochem. Parasitol. 10, 139-150.
    • (1984) Mol. Biochem. Parasitol , vol.10 , pp. 139-150
    • Dwyer, D.M.1    Gottlieb, M.2
  • 9
    • 0033033248 scopus 로고    scopus 로고
    • TbRab2p, a marker for the endoplasmic reticulum of Trypanosoma brucei, localises to the ERGIC in mammalian cells
    • Field, H., Ali, B. R. S., Sherwin, T., Gull, K., Croft, S. L., Field, M. C. (1999): TbRab2p, a marker for the endoplasmic reticulum of Trypanosoma brucei, localises to the ERGIC in mammalian cells. J. Cell Sci. 112, 147-156.
    • (1999) J. Cell Sci , vol.112 , pp. 147-156
    • Field, H.1    Ali, B.R.S.2    Sherwin, T.3    Gull, K.4    Croft, S.L.5    Field, M.C.6
  • 10
    • 0033962667 scopus 로고    scopus 로고
    • Cell-cycle and developmental regulation of TbRAB31 localisation, a GTP-locked Rab protein from Trypanosoma brucei
    • Field, H., Sherwin, T., Smith, A. C., Gull, K., Field, M. C. (2000): Cell-cycle and developmental regulation of TbRAB31 localisation, a GTP-locked Rab protein from Trypanosoma brucei. Mol. Biochem. Parasitol. 106, 21-35.
    • (2000) Mol. Biochem. Parasitol , vol.106 , pp. 21-35
    • Field, H.1    Sherwin, T.2    Smith, A.C.3    Gull, K.4    Field, M.C.5
  • 12
    • 0035012676 scopus 로고    scopus 로고
    • Secretory and endocytic pathways converge in a dynamic endosomal system in a primitive protozoan
    • Ghedin, E., Debrabant, A., Engel, J. C., Dwyer, D. M. (2001): Secretory and endocytic pathways converge in a dynamic endosomal system in a primitive protozoan. Traffic 2, 175-188.
    • (2001) Traffic , vol.2 , pp. 175-188
    • Ghedin, E.1    Debrabant, A.2    Engel, J.C.3    Dwyer, D.M.4
  • 15
    • 0343267840 scopus 로고    scopus 로고
    • Use of the green fluorescent protein as a marker in transfected Leishmania
    • Ha, D. S., Schwarz, J. K., Turco, S. J., Beverley, S. M. (1996): Use of the green fluorescent protein as a marker in transfected Leishmania. Mol. Biochem. Parasitol. 77, 57-64.
    • (1996) Mol. Biochem. Parasitol , vol.77 , pp. 57-64
    • Ha, D.S.1    Schwarz, J.K.2    Turco, S.J.3    Beverley, S.M.4
  • 16
    • 0033169025 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol biosynthetic enzymes are localized to a stable tubular subcompartment of the endoplasmic reticulum in Leishmania mexicana
    • Ilgoutz, S. C., Mullin, K. A., Southwell, B. R., McConville, M. J. (1999): Glycosylphosphatidylinositol biosynthetic enzymes are localized to a stable tubular subcompartment of the endoplasmic reticulum in Leishmania mexicana. EMBO J. 18, 3643-3654.
    • (1999) EMBO J , vol.18 , pp. 3643-3654
    • Ilgoutz, S.C.1    Mullin, K.A.2    Southwell, B.R.3    McConville, M.J.4
  • 17
    • 0025122367 scopus 로고
    • Stable transfection of the human parasite Leishmania major delineates a 30-kilobase region sufficient for extrachromosomal replication and expression
    • Kapler, G. M., Coburn, C. M., Berverley, S. M. (1990): Stable transfection of the human parasite Leishmania major delineates a 30-kilobase region sufficient for extrachromosomal replication and expression. Mol. Cell. Biol. 19, 1084-1094.
    • (1990) Mol. Cell. Biol , vol.19 , pp. 1084-1094
    • Kapler, G.M.1    Coburn, C.M.2    Berverley, S.M.3
  • 18
    • 0031457805 scopus 로고    scopus 로고
    • Post-Golgi biosynthetic trafficking
    • Keller, P., Simons, K. (1997): Post-Golgi biosynthetic trafficking. J. Cell Sci. 110, 3001-3009.
    • (1997) J. Cell Sci , vol.110 , pp. 3001-3009
    • Keller, P.1    Simons, K.2
  • 19
    • 0033535542 scopus 로고    scopus 로고
    • A novel Golgi-localisation domain shared by a class of coiled-coil peripheral membrane proteins
    • Kjer-Nielsen, L., Teasdale, R. D., van Vliet, C., Gleeson, P. A. (1999a): A novel Golgi-localisation domain shared by a class of coiled-coil peripheral membrane proteins. Curr. Biol. 9, 385-388.
    • (1999) Curr. Biol , vol.9 , pp. 385-388
    • Kjer-Nielsen, L.1    Teasdale, R.D.2    van Vliet, C.3    Gleeson, P.A.4
  • 20
    • 0032981705 scopus 로고    scopus 로고
    • The Golgi-targeting sequence of the peripheral membrane protein p230
    • Kjer-Nielsen, L., van Vliet, C., Erlich, R., Toh, B. H., Gleeson, P. A. (1999b): The Golgi-targeting sequence of the peripheral membrane protein p230. J. Cell Sci. 112, 1645-1654.
    • (1999) J. Cell Sci , vol.112 , pp. 1645-1654
    • Kjer-Nielsen, L.1    van Vliet, C.2    Erlich, R.3    Toh, B.H.4    Gleeson, P.A.5
  • 21
    • 0035002194 scopus 로고    scopus 로고
    • The flagellum and flagellar pocket of trypanosomatids
    • Landfear, S. M., Ignatushchenko, M. (2001): The flagellum and flagellar pocket of trypanosomatids. Mol. Biochem. Parasitol. 115, 1-17.
    • (2001) Mol. Biochem. Parasitol , vol.115 , pp. 1-17
    • Landfear, S.M.1    Ignatushchenko, M.2
  • 22
    • 0025650360 scopus 로고
    • Development of a stable Leishmania expression vector and application to the study of parasite surface antigen genes
    • LeBowitz, J. H., Coburn, C. M., McMahon-Pratt, D., Beverley, S. M. (1990): Development of a stable Leishmania expression vector and application to the study of parasite surface antigen genes. Proc. Natl. Acad. Sci. USA 87, 9736-9740.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9736-9740
    • LeBowitz, J.H.1    Coburn, C.M.2    McMahon-Pratt, D.3    Beverley, S.M.4
  • 23
    • 0035163224 scopus 로고    scopus 로고
    • Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction
    • Levine, T. P., Munro, S. (2001): Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction. Mol. Biol. Cell 12, 1633-1644.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1633-1644
    • Levine, T.P.1    Munro, S.2
  • 24
    • 0032543562 scopus 로고    scopus 로고
    • The pleckstrin homology domain of oxysterol-binding protein recognises a determinant specific to Golgi membranes
    • Levine, T. P., Munro, S. (1998): The pleckstrin homology domain of oxysterol-binding protein recognises a determinant specific to Golgi membranes. Curr. Biol. 8, 729-739.
    • (1998) Curr. Biol , vol.8 , pp. 729-739
    • Levine, T.P.1    Munro, S.2
  • 26
    • 0029904263 scopus 로고    scopus 로고
    • Mutation of the rab6 homologue of Saccharomyces cerevisiae, Ypt6, inhibits both early Golgi function and ribosome biogenesis
    • Li, B., Warner, J. R. (1996): Mutation of the rab6 homologue of Saccharomyces cerevisiae, Ypt6, inhibits both early Golgi function and ribosome biogenesis. J. Biol. Chem. 271, 16813-16819.
    • (1996) J. Biol. Chem , vol.271 , pp. 16813-16819
    • Li, B.1    Warner, J.R.2
  • 27
    • 0030004228 scopus 로고    scopus 로고
    • Prediction and analysis of coiled-coil structures
    • Lupas, A. (1996): Prediction and analysis of coiled-coil structures. Methods Enzymol. 266, 513-525.
    • (1996) Methods Enzymol , vol.266 , pp. 513-525
    • Lupas, A.1
  • 28
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., Van Dyke, M., Stock, J. (1991): Predicting coiled coils from protein sequences. Science 252, 1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 30
    • 0035168055 scopus 로고    scopus 로고
    • Regulated degradation of ER membrane proteins in a novel tubular lysosome in Leishmania mexicana
    • Mullin, K. A., Foth, B., Ilgoutz, S. M., Callaghan, J., McFadden, G. M., McConville, M. J. (2001): Regulated degradation of ER membrane proteins in a novel tubular lysosome in Leishmania mexicana. Mol. Biol. Cell 12, 2364-2377.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2364-2377
    • Mullin, K.A.1    Foth, B.2    Ilgoutz, S.M.3    Callaghan, J.4    McFadden, G.M.5    McConville, M.J.6
  • 31
    • 0033535585 scopus 로고    scopus 로고
    • The GRIP domain - A novel Golgi-targeting domain found in several coiled-coil proteins
    • Munro, S., Nichols, B. J. (1999): The GRIP domain - a novel Golgi-targeting domain found in several coiled-coil proteins. Curr. Biol. 9, 377-380.
    • (1999) Curr. Biol , vol.9 , pp. 377-380
    • Munro, S.1    Nichols, B.J.2
  • 32
    • 0031016286 scopus 로고    scopus 로고
    • Endocytosis and secretion in trypanosomatid parasites - Tumultuous traffic in a pocket
    • Overath, P., Stierhof, Y.-D., Weise, M. (1997): Endocytosis and secretion in trypanosomatid parasites - tumultuous traffic in a pocket. Trends Cell Biol. 7, 27-33.
    • (1997) Trends Cell Biol , vol.7 , pp. 27-33
    • Overath, P.1    Stierhof, Y.-D.2    Weise, M.3
  • 33
    • 0026109543 scopus 로고
    • The comparative fine structure and surface glycoconjugate expression of three life stages of Leishmania major Exp
    • Pimenta, P. F., Saraiva, E. M., Sacks, D. L. (1991): The comparative fine structure and surface glycoconjugate expression of three life stages of Leishmania major Exp. Parasitol. 72, 191-204.
    • (1991) Parasitol , vol.72 , pp. 191-204
    • Pimenta, P.F.1    Saraiva, E.M.2    Sacks, D.L.3
  • 34
    • 0034941051 scopus 로고    scopus 로고
    • FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes
    • Raiborg, C., Bremnes, B., Mehlum, A., Gillooly, D. J., D'Arrigo, A., Stang, E., Stenmark, H. (2001): FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes J. Cell Sci. 114, 2255-2263.
    • (2001) J. Cell Sci , vol.114 , pp. 2255-2263
    • Raiborg, C.1    Bremnes, B.2    Mehlum, A.3    Gillooly, D.J.4    D'Arrigo, A.5    Stang, E.6    Stenmark, H.7
  • 36
    • 0035976622 scopus 로고    scopus 로고
    • Location, location, location: Membrane targeting directed by PX domains
    • Sato, T. K., Overduin, M., Mer, S. D. (2001): Location, location, location: membrane targeting directed by PX domains. Science 294, 1881-1885.
    • (2001) Science , vol.294 , pp. 1881-1885
    • Sato, T.K.1    Overduin, M.2    Mer, S.D.3
  • 38
    • 0031574072 scopus 로고    scopus 로고
    • CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., Bibson, T. J., Plewniak, F., Jeanmougin, F., Higgins, D. G. (1997): CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Bibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 39
    • 0034896518 scopus 로고    scopus 로고
    • Greasing the wheels of secretory transport
    • Thorner, J. W. (2001): Greasing the wheels of secretory transport. Nature Cell Biol. 3, E196-E198.
    • (2001) Nature Cell Biol , vol.3
    • Thorner, J.W.1
  • 40
    • 0030816038 scopus 로고    scopus 로고
    • The trans-Golgi network: A late secretory sorting station
    • Traub, L. M., Kornfeld, S. (1997): The trans-Golgi network: a late secretory sorting station. Curr. Opin. Cell Biol. 9, 527-533.
    • (1997) Curr. Opin. Cell Biol , vol.9 , pp. 527-533
    • Traub, L.M.1    Kornfeld, S.2
  • 41
    • 0032948290 scopus 로고    scopus 로고
    • Structural and functional analysis of a novel coiled coil protein involved in Ypt6 GTPase-regulated protein transport in yeast
    • Tsukada, M., Will, E., Gallwitz, D. (1999): Structural and functional analysis of a novel coiled coil protein involved in Ypt6 GTPase-regulated protein transport in yeast. Mol. Biol. Cell 10, 63-75.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 63-75
    • Tsukada, M.1    Will, E.2    Gallwitz, D.3
  • 42
    • 0024434231 scopus 로고
    • Endocytosis by African trypanosomes. I. Three-dimensional structure of the endocytic organelles in Trypanosoma brucei and T. congolense
    • Webster, P. (1989): Endocytosis by African trypanosomes. I. Three-dimensional structure of the endocytic organelles in Trypanosoma brucei and T. congolense. Eur. J. Cell Biol. 49, 295-302.
    • (1989) Eur. J. Cell Biol , vol.49 , pp. 295-302
    • Webster, P.1
  • 43
    • 0034496239 scopus 로고    scopus 로고
    • Distribution of GPI-anchored proteins in the protozoan parasite Leishmania, based on an improved ultrastructural description using high-pressure frozen cells
    • Weise, F., Stierhof, Y. D., Kuhn, C., Wiese, M., Overath, P. (2000): Distribution of GPI-anchored proteins in the protozoan parasite Leishmania, based on an improved ultrastructural description using high-pressure frozen cells. J. Cell Sci. 113, 4587-4603.
    • (2000) J. Cell Sci , vol.113 , pp. 4587-4603
    • Weise, F.1    Stierhof, Y.D.2    Kuhn, C.3    Wiese, M.4    Overath, P.5
  • 44
    • 0035967888 scopus 로고    scopus 로고
    • Phoxy lipids: Revealing PX domains as phosphoinositide-binding modules
    • Wishart, M. J., Taylor, G. S., Dixon, J. E. (2001): Phoxy lipids: revealing PX domains as phosphoinositide-binding modules. Cell 105, 817-820.
    • (2001) Cell , vol.105 , pp. 817-820
    • Wishart, M.J.1    Taylor, G.S.2    Dixon, J.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.