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Volumn 15, Issue 4, 2004, Pages 1487-1505

Phylogenetic Analysis of Sec7-Domain-containing Arf Nucleotide Exchangers

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; GUANOSINE TRIPHOSPHATASE;

EID: 1642464740     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E03-06-0443     Document Type: Review
Times cited : (131)

References (111)
  • 2
    • 0030891289 scopus 로고    scopus 로고
    • N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange
    • Antonny, B., Beraud-Dufour, S., Chardin, P., and Chabre, M. (1997). N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange. Biochemistry 36, 4675-4684.
    • (1997) Biochemistry , vol.36 , pp. 4675-4684
    • Antonny, B.1    Beraud-Dufour, S.2    Chardin, P.3    Chabre, M.4
  • 3
    • 0029819318 scopus 로고    scopus 로고
    • The root of the universal tree and the origin of eukaryotes based on elongation factor phylogeny
    • Baldauf, S.L., Palmer, J.D., and Doolittle, W.F. (1996). The root of the universal tree and the origin of eukaryotes based on elongation factor phylogeny. Proc. Natl. Acad. Sci. USA 93, 7749-7754.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7749-7754
    • Baldauf, S.L.1    Palmer, J.D.2    Doolittle, W.F.3
  • 4
    • 0027500969 scopus 로고
    • SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER
    • Barlowe, C., and Schekman, R. (1993). SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER. Nature 365, 347-349.
    • (1993) Nature , vol.365 , pp. 347-349
    • Barlowe, C.1    Schekman, R.2
  • 5
    • 0035788652 scopus 로고    scopus 로고
    • A point mutation in an unusual Sec7 domain is linked to brefeldin A resistance in a Plasmodium falciparum line generated by drug selection
    • Baumgartner, F., Wiek, S., Paprotka, K., Zauner, S., and Lingelbach, K. (2001). A point mutation in an unusual Sec7 domain is linked to brefeldin A resistance in a Plasmodium falciparum line generated by drug selection. Mol. Microbiol. 41, 1151-1158.
    • (2001) Mol. Microbiol. , vol.41 , pp. 1151-1158
    • Baumgartner, F.1    Wiek, S.2    Paprotka, K.3    Zauner, S.4    Lingelbach, K.5
  • 7
    • 0040411317 scopus 로고    scopus 로고
    • Dual interaction of ADP ribosylation factor 1 with Sec7 domain and with lipid membranes during catalysis of guanine nucleotide exchange
    • Beraud-Dufour, S., Paris, S., Chabre, M., and Antonny, B. (1999). Dual interaction of ADP ribosylation factor 1 with Sec7 domain and with lipid membranes during catalysis of guanine nucleotide exchange. J. Biol. Chem. 274, 37629-37636.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37629-37636
    • Beraud-Dufour, S.1    Paris, S.2    Chabre, M.3    Antonny, B.4
  • 8
    • 0039818755 scopus 로고    scopus 로고
    • A glutamic finger in the guanine nucleotide exchange factor ARNO displaces Mg2+ and the beta-phosphate to destabilize GDP on ARF1
    • Beraud-Dufour, S., Robineau, S., Chardin, P., Paris, S., Chabre, M., Cherfils, J., and Antonny, B. (1998). A glutamic finger in the guanine nucleotide exchange factor ARNO displaces Mg2+ and the beta-phosphate to destabilize GDP on ARF1. EMBO J. 17, 3651-3659.
    • (1998) EMBO J. , vol.17 , pp. 3651-3659
    • Beraud-Dufour, S.1    Robineau, S.2    Chardin, P.3    Paris, S.4    Chabre, M.5    Cherfils, J.6    Antonny, B.7
  • 10
    • 0007724488 scopus 로고    scopus 로고
    • The PH superfold: A structural scaffold for multiple functions
    • Blomberg, N., Baraldi, E., Nilges, M., and Saraste, M. (1999). The PH superfold: a structural scaffold for multiple functions. Trends Biochem. Sci. 24, 441-445.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 441-445
    • Blomberg, N.1    Baraldi, E.2    Nilges, M.3    Saraste, M.4
  • 11
    • 0037462451 scopus 로고    scopus 로고
    • Endosome-specific localization and function of the ARF activator GNOM
    • Bonifacino, J.S., and Jackson, C.L. (2003). Endosome-specific localization and function of the ARF activator GNOM. Cell 112, 141-142.
    • (2003) Cell , vol.112 , pp. 141-142
    • Bonifacino, J.S.1    Jackson, C.L.2
  • 12
    • 0028941917 scopus 로고
    • Root of the universal tree of life based on ancient aminoacyl-tRNA synthetase gene duplications
    • Brown, J.R., and Doolittle, W.F. (1995). Root of the universal tree of life based on ancient aminoacyl-tRNA synthetase gene duplications. Proc. Natl. Acad. Sci. USA 92, 2441-2445.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2441-2445
    • Brown, J.R.1    Doolittle, W.F.2
  • 13
    • 0029832697 scopus 로고    scopus 로고
    • Intracellular distribution of Arf proteins in mammalian cells. Arf6 is uniquely localized to the plasma membrane
    • Cavenagh, M.M., Whitney, J.A., Carroll, K., Zhang, C., Boman, A.L., Rosenwald, A.G., Mellman, I., and Kahn, R.A. (1996). Intracellular distribution of Arf proteins in mammalian cells. Arf6 is uniquely localized to the plasma membrane. J. Biol. Chem. 271, 21767-21774.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21767-21774
    • Cavenagh, M.M.1    Whitney, J.A.2    Carroll, K.3    Zhang, C.4    Boman, A.L.5    Rosenwald, A.G.6    Mellman, I.7    Kahn, R.A.8
  • 14
    • 0032509302 scopus 로고    scopus 로고
    • Genome sequence of the nematode C. elegans: A platform for investigating biology
    • The C. elegans Sequencing Consortium (1998). Genome sequence of the nematode C. elegans: a platform for investigating biology. Science 282, 2012-2018.
    • (1998) Science , vol.282 , pp. 2012-2018
  • 15
    • 0012340085 scopus 로고    scopus 로고
    • Finishing a whole-genome shotgun: Release 3 of the Drosophila melanogaster euchromatic genome sequence
    • RESEARCH0079.1-14
    • Celniker, S.E., et al. (2002). Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster euchromatic genome sequence. Genome Biol. 3, RESEARCH0079.1-14.
    • (2002) Genome Biol. , vol.3
    • Celniker, S.E.1
  • 19
    • 0035834775 scopus 로고    scopus 로고
    • beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis
    • Claing, A., Chen, W., Miller, W.E., Vitale, N., Moss, J., Premont, R.T., and Lefkowitz, R.J. (2001). beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis. J. Biol. Chem. 276, 42509-42513.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42509-42513
    • Claing, A.1    Chen, W.2    Miller, W.E.3    Vitale, N.4    Moss, J.5    Premont, R.T.6    Lefkowitz, R.J.7
  • 20
    • 0033549576 scopus 로고    scopus 로고
    • GBF 1, A novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5
    • Claude, A., Zhao, B.P., Kuziemsky, C.E., Dahan, S., Berger, S.J., Yan, J.P., Armold, A.D., Sullivan, E.M., and Melancon, P. (1999). GBF 1, A novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5. J. Cell Biol. 146, 71-84.
    • (1999) J. Cell Biol. , vol.146 , pp. 71-84
    • Claude, A.1    Zhao, B.P.2    Kuziemsky, C.E.3    Dahan, S.4    Berger, S.J.5    Yan, J.P.6    Armold, A.D.7    Sullivan, E.M.8    Melancon, P.9
  • 21
    • 0028914182 scopus 로고
    • A regulatory role for ARF6 in receptor-mediated endocytosis
    • D'Souza-Schorey, C., Li, G., Colombo, M.I., and Stahl, P.D. (1995). A regulatory role for ARF6 in receptor-mediated endocytosis. Science 267, 1175-1178.
    • (1995) Science , vol.267 , pp. 1175-1178
    • D'Souza-Schorey, C.1    Li, G.2    Colombo, M.I.3    Stahl, P.D.4
  • 22
    • 0027953550 scopus 로고
    • Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus
    • Dascher, C., and Balch, W.E. (1994). Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus. J. Biol. Chem. 269, 1437-1448.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1437-1448
    • Dascher, C.1    Balch, W.E.2
  • 23
    • 0037099033 scopus 로고    scopus 로고
    • A conserved C-terminal domain of EFA6-family ARF6-guanine nucleotide exchange factors induces lengthening of microvilli-like membrane protrusions
    • Derrien, V., Couillault, C., Franco, M., Martineau, S., Montcourrier, P., Houlgatte, R., and Chavrier, P. (2002). A conserved C-terminal domain of EFA6-family ARF6-guanine nucleotide exchange factors induces lengthening of microvilli-like membrane protrusions. J. Cell Sci. 115, 2867-2879.
    • (2002) J. Cell Sci. , vol.115 , pp. 2867-2879
    • Derrien, V.1    Couillault, C.2    Franco, M.3    Martineau, S.4    Montcourrier, P.5    Houlgatte, R.6    Chavrier, P.7
  • 25
    • 0142211351 scopus 로고    scopus 로고
    • Multiple roles for Arf 6, sorting, structuring, and signaling at the plasma membrane
    • Donaldson, J.G. (2003). Multiple roles for Arf 6, sorting, structuring, and signaling at the plasma membrane. J. Biol. Chem. 278, 41573-41576.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41573-41576
    • Donaldson, J.G.1
  • 26
    • 0026677375 scopus 로고
    • Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein
    • Donaldson, J.G., Finazzi, D., and Klausner, R.D. (1992). Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein. Nature 360, 350-352.
    • (1992) Nature , vol.360 , pp. 350-352
    • Donaldson, J.G.1    Finazzi, D.2    Klausner, R.D.3
  • 27
    • 0033937941 scopus 로고    scopus 로고
    • Regulators and effectors of the ARF GTPases
    • Donaldson, J.G., and Jackson, C.L. (2000). Regulators and effectors of the ARF GTPases. Curr. Opin. Cell Biol. 12, 475-482.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 475-482
    • Donaldson, J.G.1    Jackson, C.L.2
  • 28
    • 0035953753 scopus 로고    scopus 로고
    • The highly reduced genome of an enslaved algal nucleus
    • Douglas, S., et al. (2001). The highly reduced genome of an enslaved algal nucleus. Nature 410, 1091-1096.
    • (2001) Nature , vol.410 , pp. 1091-1096
    • Douglas, S.1
  • 29
    • 0032544023 scopus 로고    scopus 로고
    • ARNO3, a Sec7-domain guanine nucleotide exchange factor for ADP ribosylation factor 1, is involved in the control of Golgi structure and function
    • Franco, M., Boretto, J., Robineau, S., Monier, S., Goud, B., Chardin, P., and Chavrier, P. (1998). ARNO3, a Sec7-domain guanine nucleotide exchange factor for ADP ribosylation factor 1, is involved in the control of Golgi structure and function. Proc. Natl. Acad. Sci. USA 95, 9926-9931.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9926-9931
    • Franco, M.1    Boretto, J.2    Robineau, S.3    Monier, S.4    Goud, B.5    Chardin, P.6    Chavrier, P.7
  • 30
    • 0033560032 scopus 로고    scopus 로고
    • EFA6, a sec7 domain-containing exchange factor for ARF6, coordinates membrane recycling and actin cytoskeleton organization
    • Franco, M., Peters, P.J., Boretto, J., van Donselaar, E., Neri, A., D'Souza-Schorey, C., and Chavrier, P. (1999). EFA6, a sec7 domain-containing exchange factor for ARF6, coordinates membrane recycling and actin cytoskeleton organization. EMBO J. 18, 1480-1491.
    • (1999) EMBO J. , vol.18 , pp. 1480-1491
    • Franco, M.1    Peters, P.J.2    Boretto, J.3    Van Donselaar, E.4    Neri, A.5    D'Souza-Schorey, C.6    Chavrier, P.7
  • 31
    • 0031982629 scopus 로고    scopus 로고
    • ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor 6
    • Frank, S., Upender, S., Hansen, S.H., and Casanova, J.E. (1998). ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor 6. J. Biol. Chem. 273, 23-27.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23-27
    • Frank, S.1    Upender, S.2    Hansen, S.H.3    Casanova, J.E.4
  • 32
    • 0024433708 scopus 로고
    • Functional compartments of the yeast Golgi apparatus are defined by the sec7 mutation
    • Franzusoff, A., and Schekman, R. (1989). Functional compartments of the yeast Golgi apparatus are defined by the sec7 mutation. EMBO J. 8, 2695-2702.
    • (1989) EMBO J. , vol.8 , pp. 2695-2702
    • Franzusoff, A.1    Schekman, R.2
  • 33
    • 0037464589 scopus 로고    scopus 로고
    • The genome sequence of the filamentous fungus Neurospora crassa
    • Galagan, J.E., et al. (2003). The genome sequence of the filamentous fungus Neurospora crassa. Nature 422, 859-868.
    • (2003) Nature , vol.422 , pp. 859-868
    • Galagan, J.E.1
  • 34
    • 17344391184 scopus 로고    scopus 로고
    • ADP-ribosylation factor/COPI-dependent events at the endoplasmic reticulum-Golgi interface are regulated by the guanine nucleotide exchange factor GBF1
    • Garcia-Mata, R., Szul, T., Alvarez, C., and Sztul, E. (2003). ADP-ribosylation factor/COPI-dependent events at the endoplasmic reticulum-Golgi interface are regulated by the guanine nucleotide exchange factor GBF1. Mol. Biol. Cell 14, 2250-2261.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2250-2261
    • Garcia-Mata, R.1    Szul, T.2    Alvarez, C.3    Sztul, E.4
  • 35
    • 0033538485 scopus 로고    scopus 로고
    • Distribution of ARF6 between membrane and cytosol is regulated by its GTPase cycle
    • Gaschet, J., and Hsu, V.W. (1999). Distribution of ARF6 between membrane and cytosol is regulated by its GTPase cycle. J. Biol. Chem. 274, 20040-20045.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20040-20045
    • Gaschet, J.1    Hsu, V.W.2
  • 36
    • 0031940702 scopus 로고    scopus 로고
    • ARF is required for maintenance of yeast Golgi and endosome structure and function
    • Gaynor, E.C., Chen, C.Y., Emr, S.D., and Graham, T.R. (1998). ARF is required for maintenance of yeast Golgi and endosome structure and function. Mol. Biol. Cell 9, 653-670.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 653-670
    • Gaynor, E.C.1    Chen, C.Y.2    Emr, S.D.3    Graham, T.R.4
  • 37
    • 0037462425 scopus 로고    scopus 로고
    • The Arabidopsis GNOM ARF-GEF mediates endosomal recycling, auxin transport, and auxin-dependent plant growth
    • Geldner, N., et al. (2003). The Arabidopsis GNOM ARF-GEF mediates endosomal recycling, auxin transport, and auxin-dependent plant growth. Cell 112, 219-230.
    • (2003) Cell , vol.112 , pp. 219-230
    • Geldner, N.1
  • 38
    • 0032538317 scopus 로고    scopus 로고
    • Structural basis for activation of ARF GTPase: Mechanisms of guanine nucleotide exchange and GTP-myristoyl switching
    • Goldberg, J. (1998). Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching. Cell 95, 237-248.
    • (1998) Cell , vol.95 , pp. 237-248
    • Goldberg, J.1
  • 39
    • 0034108573 scopus 로고    scopus 로고
    • A conserved domain of the arabidopsis GNOM protein mediates subunit interaction and cyclophilin 5 binding
    • Grebe, M., Gadea, J., Steinmann, T., Kientz, M., Rahfeld, J.U., Salchert, K., Koncz, C., and Jurgens, G. (2000). A conserved domain of the arabidopsis GNOM protein mediates subunit interaction and cyclophilin 5 binding. Plant Cell 12, 343-356.
    • (2000) Plant Cell , vol.12 , pp. 343-356
    • Grebe, M.1    Gadea, J.2    Steinmann, T.3    Kientz, M.4    Rahfeld, J.U.5    Salchert, K.6    Koncz, C.7    Jurgens, G.8
  • 40
    • 0026746713 scopus 로고
    • Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF
    • Helms, J.B., and Rothman, J.E. (1992). Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF. Nature 360, 352-354.
    • (1992) Nature , vol.360 , pp. 352-354
    • Helms, J.B.1    Rothman, J.E.2
  • 41
    • 0036086829 scopus 로고    scopus 로고
    • Annotating the human proteome: The Human Proteome Survey Database (HumanPSD) and an in-depth target database for G protein-coupled receptors (GPCR-PD) from Incyte Genomics
    • Hodges, P.E., Carrico, P.M., Hogan, J.D., O'Neill, K.E., Owen, J.J., Mangan, M., Davis, B.P., Brooks, J.E., and Garrels, J.I. (2002). Annotating the human proteome: the Human Proteome Survey Database (HumanPSD) and an in-depth target database for G protein-coupled receptors (GPCR-PD) from Incyte Genomics. Nucleic Acids Res. 30, 137-141.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 137-141
    • Hodges, P.E.1    Carrico, P.M.2    Hogan, J.D.3    O'Neill, K.E.4    Owen, J.J.5    Mangan, M.6    Davis, B.P.7    Brooks, J.E.8    Garrels, J.I.9
  • 42
    • 0032894060 scopus 로고    scopus 로고
    • The Yeast Proteome Database (YPD): A model for the organization and presentation of genome-wide functional data
    • Hodges, P.E., McKee, A.H., Davis, B.P., Payne, W.E., and Garrels, J.I. (1999). The Yeast Proteome Database (YPD): a model for the organization and presentation of genome-wide functional data. Nucleic Acids Res. 27, 69-73.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 69-73
    • Hodges, P.E.1    McKee, A.H.2    Davis, B.P.3    Payne, W.E.4    Garrels, J.I.5
  • 43
    • 0141521593 scopus 로고    scopus 로고
    • Role for Arf3p in development of polarity, but not endocytosis, in Saccharomyces cerevisiae
    • Huang, C.F., Liu, Y.W., Tung, L., Lin, C.H., and Lee, F.J. (2003). Role for Arf3p in development of polarity, but not endocytosis, in Saccharomyces cerevisiae. Mol. Biol. Cell 14, 3834-3847.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3834-3847
    • Huang, C.F.1    Liu, Y.W.2    Tung, L.3    Lin, C.H.4    Lee, F.J.5
  • 44
    • 0024358140 scopus 로고
    • Evolutionary relationship of archaebacteria, eubacteria, and eukaryotes inferred from phylogenetic trees of duplicated genes
    • Iwabe, N., Kuma, K., Hasegawa, M., Osawa, S., and Miyata, T. (1989). Evolutionary relationship of archaebacteria, eubacteria, and eukaryotes inferred from phylogenetic trees of duplicated genes. Proc. Natl. Acad. Sci. USA 86, 9355-9359.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9355-9359
    • Iwabe, N.1    Kuma, K.2    Hasegawa, M.3    Osawa, S.4    Miyata, T.5
  • 45
    • 0033950864 scopus 로고    scopus 로고
    • Turning on ARF: The Sec7 family of guanine-nucleotide-exchange factors
    • Jackson, C.L., and Casanova, J.E. (2000). Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors. Trends Cell Biol. 10, 60-67.
    • (2000) Trends Cell Biol. , vol.10 , pp. 60-67
    • Jackson, C.L.1    Casanova, J.E.2
  • 46
    • 0345151822 scopus 로고    scopus 로고
    • Genetic interactions in yeast between Ypt GTPases and Arf guanine nucleotide exchangers
    • Jones, S., Jedd, G., Kahn, R.A., Franzusoff, A., Bartolini, F., and Segev, N. (1999). Genetic interactions in yeast between Ypt GTPases and Arf guanine nucleotide exchangers. Genetics 152, 1543-1556.
    • (1999) Genetics , vol.152 , pp. 1543-1556
    • Jones, S.1    Jedd, G.2    Kahn, R.A.3    Franzusoff, A.4    Bartolini, F.5    Segev, N.6
  • 48
    • 0036017789 scopus 로고    scopus 로고
    • GBF1, a guanine nucleotide exchange factor for ADP-ribosylation factors, is localized to the cis-Golgi and involved in membrane association of the COPI coat
    • Kawamoto, K., Yoshida, Y., Tamaki, H., Torii, S., Shinotsuka, C., Yamashina, S., and Nakayama, K. (2002). GBF1, a guanine nucleotide exchange factor for ADP-ribosylation factors, is localized to the cis-Golgi and involved in membrane association of the COPI coat. Traffic 3, 483-495.
    • (2002) Traffic , vol.3 , pp. 483-495
    • Kawamoto, K.1    Yoshida, Y.2    Tamaki, H.3    Torii, S.4    Shinotsuka, C.5    Yamashina, S.6    Nakayama, K.7
  • 49
    • 0034568688 scopus 로고    scopus 로고
    • The F-box protein family
    • REVIEWS3002.1-7
    • Kipreos, E.T., and Pagano, M. (2000). The F-box protein family. Genome Biol. REVIEWS3002.1-7.
    • (2000) Genome Biol.
    • Kipreos, E.T.1    Pagano, M.2
  • 50
    • 0030975196 scopus 로고    scopus 로고
    • Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains
    • Klarlund, J.K., Guilherme, A., Holik, J.J., Virbasius, J.V., Chawla, A., and Czech, M.P. (1997). Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains. Science 275, 1927-1930.
    • (1997) Science , vol.275 , pp. 1927-1930
    • Klarlund, J.K.1    Guilherme, A.2    Holik, J.J.3    Virbasius, J.V.4    Chawla, A.5    Czech, M.P.6
  • 51
    • 0035955613 scopus 로고    scopus 로고
    • Signaling complexes of the FERM domain-containing protein GRSP1 bound to ARF exchange factor GRP1
    • Klarlund, J.K., Holik, J., Chawla, A., Park, J.G., Buxton, J., and Czech, M.P. (2001). Signaling complexes of the FERM domain-containing protein GRSP1 bound to ARF exchange factor GRP1. J. Biol. Chem. 276, 40065-40070.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40065-40070
    • Klarlund, J.K.1    Holik, J.2    Chawla, A.3    Park, J.G.4    Buxton, J.5    Czech, M.P.6
  • 52
    • 0031939743 scopus 로고    scopus 로고
    • Regulation of GRP1-catalyzed ADP ribosylation factor guanine nucleotide exchange by phosphatidylinositol 3,4,5-trisphosphate
    • Klarlund, J.K., Rameh, L.E., Cantley, L.C., Buxton, J.M., Holik, J.J., Sakelis, C., Patki, V., Corvera, S., and Czech, M.P. (1998). Regulation of GRP1-catalyzed ADP ribosylation factor guanine nucleotide exchange by phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273, 1859-1862.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1859-1862
    • Klarlund, J.K.1    Rameh, L.E.2    Cantley, L.C.3    Buxton, J.M.4    Holik, J.J.5    Sakelis, C.6    Patki, V.7    Corvera, S.8    Czech, M.P.9
  • 53
    • 0034693264 scopus 로고    scopus 로고
    • Distinct polyphosphoinositide binding selectivities for pleckstrin homology domains of GRP1-like proteins based on diglycine versus triglycine motifs
    • Klarlund, J.K., Tsiaras, W., Holik, J.J., Chawla, A., and Czech, M.P. (2000). Distinct polyphosphoinositide binding selectivities for pleckstrin homology domains of GRP1-like proteins based on diglycine versus triglycine motifs. J. Biol. Chem. 275, 32816-32821.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32816-32821
    • Klarlund, J.K.1    Tsiaras, W.2    Holik, J.J.3    Chawla, A.4    Czech, M.P.5
  • 54
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • Lander, E.S., et al. (2001). Initial sequencing and analysis of the human genome. Nature 409, 860-921.
    • (2001) Nature , vol.409 , pp. 860-921
    • Lander, E.S.1
  • 55
    • 0034193115 scopus 로고    scopus 로고
    • B2-1, a Sec7- and pleckstrin homology domain-containing protein, localizes to the Golgi complex
    • Lee, S.Y., Mansour, M., and Pohajdak, B. (2000). B2-1, a Sec7- and pleckstrin homology domain-containing protein, localizes to the Golgi complex. Exp. Cell Res. 256, 515-521.
    • (2000) Exp. Cell Res. , vol.256 , pp. 515-521
    • Lee, S.Y.1    Mansour, M.2    Pohajdak, B.3
  • 56
    • 0034663568 scopus 로고    scopus 로고
    • Signal-dependent membrane targeting by pleckstrin homology (PH) domains
    • Lemmon, M.A., and Ferguson, K.M. (2000). Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochem. J. 350 Pt 1, 1-18.
    • (2000) Biochem. J. , vol.350 , Issue.PART 1 , pp. 1-18
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 57
    • 0034872365 scopus 로고    scopus 로고
    • Molecular determinants in pleckstrin homology domains that allow specific recognition of phosphoinositides
    • Lemmon, M.A., and Ferguson, K.M. (2001). Molecular determinants in pleckstrin homology domains that allow specific recognition of phosphoinositides. Biochem. Soc. Trans. 29, 377-384.
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 377-384
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 58
    • 0036086410 scopus 로고    scopus 로고
    • Recent improvements to the SMART domain-based sequence annotation resource
    • Letunic, I., et al. (2002). Recent improvements to the SMART domain-based sequence annotation resource. Nucleic Acids Res. 30, 242-244.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 242-244
    • Letunic, I.1
  • 60
    • 0037452694 scopus 로고    scopus 로고
    • Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2)
    • Li, H., Adamik, R., Pacheco-Rodriguez, G., Moss, J., and Vaughan, M. (2003). Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2). Proc. Natl. Acad. Sci. USA 100, 1627-1632.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1627-1632
    • Li, H.1    Adamik, R.2    Pacheco-Rodriguez, G.3    Moss, J.4    Vaughan, M.5
  • 61
    • 0035816551 scopus 로고    scopus 로고
    • Specificities for the small G proteins ARF1 and ARF6 of the guanine nucleotide exchange factors ARNO and EFA6
    • Macia, E., Chabre, M., and Franco, M. (2001). Specificities for the small G proteins ARF1 and ARF6 of the guanine nucleotide exchange factors ARNO and EFA6. J. Biol. Chem. 276, 24925-24930.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24925-24930
    • Macia, E.1    Chabre, M.2    Franco, M.3
  • 62
    • 0037200124 scopus 로고    scopus 로고
    • The N-terminal coiled coil domain of the cytohesin/ARNO family of guanine nucleotide exchange factors interacts with the scaffolding protein CASP
    • Mansour, M., Lee, S.Y., and Pohajdak, B. (2002). The N-terminal coiled coil domain of the cytohesin/ARNO family of guanine nucleotide exchange factors interacts with the scaffolding protein CASP. J. Biol. Chem. 277, 32302-32309.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32302-32309
    • Mansour, M.1    Lee, S.Y.2    Pohajdak, B.3
  • 63
    • 0033529249 scopus 로고    scopus 로고
    • p200 ARF-GEP 1, a Golgi-localized guanine nucleotide exchange protein whose Sec7 domain is targeted by the drug brefeldin A
    • Mansour, S.J., Skaug, J., Zhao, X.H., Giordano, J., Scherer, S.W., and Melancon, P. (1999). p200 ARF-GEP 1, a Golgi-localized guanine nucleotide exchange protein whose Sec7 domain is targeted by the drug brefeldin A. Proc. Natl. Acad. Sci. USA 96, 7968-7973.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7968-7973
    • Mansour, S.J.1    Skaug, J.2    Zhao, X.H.3    Giordano, J.4    Scherer, S.W.5    Melancon, P.6
  • 64
    • 0037252683 scopus 로고    scopus 로고
    • CDD: A curated Entrez database of conserved domain alignments
    • Marchler-Bauer, A., et al. (2003). CDD: a curated Entrez database of conserved domain alignments. Nucleic Acids Res. 31, 383-387.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 383-387
    • Marchler-Bauer, A.1
  • 65
    • 0031041536 scopus 로고    scopus 로고
    • Cytohesin-1, a cytosolic guanine nucleoticle-exchange protein for ADP-ribosylation factor
    • Meacci, E., Tsai, S.C., Adamik, R., Moss, J., and Vaughan, M. (1997). Cytohesin-1, a cytosolic guanine nucleoticle-exchange protein for ADP-ribosylation factor. Proc. Natl. Acad. Sci. USA 94, 1745-1748.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1745-1748
    • Meacci, E.1    Tsai, S.C.2    Adamik, R.3    Moss, J.4    Vaughan, M.5
  • 66
    • 0034614647 scopus 로고    scopus 로고
    • The road taken: Past and future foundations of membrane traffic
    • Mellman, I., and Warren, G. (2000). The road taken: past and future foundations of membrane traffic. Cell 100, 99-112.
    • (2000) Cell , vol.100 , pp. 99-112
    • Mellman, I.1    Warren, G.2
  • 67
    • 0033580849 scopus 로고    scopus 로고
    • Brefeldin A inhibited activity of the sec7 domain of p200, a mammalian guanine nucleotide-exchange protein for ADP-ribosylation factors
    • Morinaga, N., Adamik, R., Moss, J., and Vaughan, M. (1999). Brefeldin A inhibited activity of the sec7 domain of p200, a mammalian guanine nucleotide-exchange protein for ADP-ribosylation factors. J. Biol. Chem. 274, 17417-17423.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17417-17423
    • Morinaga, N.1    Adamik, R.2    Moss, J.3    Vaughan, M.4
  • 68
    • 0030659646 scopus 로고    scopus 로고
    • Cloning and expression of a cDNA encoding a bovine brain brefeldin A-sensitive guanine nucleotide-exchange protein for ADP-ribosylation factor
    • Morinaga, N., Moss, J., and Vaughan, M. (1997). Cloning and expression of a cDNA encoding a bovine brain brefeldin A-sensitive guanine nucleotide-exchange protein for ADP-ribosylation factor. Proc. Natl. Acad. Sci. USA 94, 12926-12931.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12926-12931
    • Morinaga, N.1    Moss, J.2    Vaughan, M.3
  • 69
    • 0032555493 scopus 로고    scopus 로고
    • Molecules in the ARF orbit
    • Moss, J., and Vaughan, M. (1998). Molecules in the ARF orbit. J. Biol. Chem. 273, 21431-21434.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21431-21434
    • Moss, J.1    Vaughan, M.2
  • 71
    • 0037169078 scopus 로고    scopus 로고
    • A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes
    • Nagai, H., Kagan, J.C., Zhu, X., Kahn, R.A., and Roy, C.R. (2002). A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes. Science 295, 679-682.
    • (2002) Science , vol.295 , pp. 679-682
    • Nagai, H.1    Kagan, J.C.2    Zhu, X.3    Kahn, R.A.4    Roy, C.R.5
  • 72
    • 0032849775 scopus 로고    scopus 로고
    • Direct interaction between the ARF-specific guanine nucleotide exchange factor msec7-1 and presynaptic Munc13-1
    • Neeb, A., Koch, H., Schurmann, A., and Brose, N. (1999). Direct interaction between the ARF-specific guanine nucleotide exchange factor msec7-1 and presynaptic Munc13-1. Eur. J. Cell Biol. 78, 533-538.
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 533-538
    • Neeb, A.1    Koch, H.2    Schurmann, A.3    Brose, N.4
  • 73
    • 0034595664 scopus 로고    scopus 로고
    • Interaction of GRASP, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors
    • Nevrivy, D.J., Peterson, V.J., Avram, D., Ishmael, J.E., Hansen, S.G., Dowell, P., Hruby, D.E., Dawson, M.I., and Leid, M. (2000). Interaction of GRASP, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors. J. Biol. Chem. 275, 16827-16836.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16827-16836
    • Nevrivy, D.J.1    Peterson, V.J.2    Avram, D.3    Ishmael, J.E.4    Hansen, S.G.5    Dowell, P.6    Hruby, D.E.7    Dawson, M.I.8    Leid, M.9
  • 74
    • 0034602992 scopus 로고    scopus 로고
    • Similarities in function and gene structure of cytohesin-4 and cytohesin-1, guanine nucleotide-exchange proteins for ADP-ribosylation factors
    • Ogasawara, M., Kim, S.C., Adamik, R., Togawa, A., Ferrans, V.J., Takeda, K., Kirby, M., Moss, J., and Vaughan, M. (2000). Similarities in function and gene structure of cytohesin-4 and cytohesin-1, guanine nucleotide-exchange proteins for ADP-ribosylation factors. J. Biol. Chem. 275, 3221-3230.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3221-3230
    • Ogasawara, M.1    Kim, S.C.2    Adamik, R.3    Togawa, A.4    Ferrans, V.J.5    Takeda, K.6    Kirby, M.7    Moss, J.8    Vaughan, M.9
  • 75
    • 0032500621 scopus 로고    scopus 로고
    • Guanine nucleotide exchange on ADP-ribosylation factors catalyzed by cytohesin-1 and its Sec7 domain
    • Pacheco-Rodriguez, G., Meacci, E., Vitale, N., Moss, J., and Vaughan, M. (1998). Guanine nucleotide exchange on ADP-ribosylation factors catalyzed by cytohesin-1 and its Sec7 domain. J. Biol. Chem. 273, 26543-26548.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26543-26548
    • Pacheco-Rodriguez, G.1    Meacci, E.2    Vitale, N.3    Moss, J.4    Vaughan, M.5
  • 76
    • 0037418199 scopus 로고    scopus 로고
    • Interaction of FK506-binding protein 13 with brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1): Effects of FK506
    • Padilla, P.I., Chang, M.J., Pacheco-Rodriguez, G., Adamik, R., Moss, J., and Vaughan, M. (2003). Interaction of FK506-binding protein 13 with brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1): effects of FK506. Proc. Natl. Acad. Sci. USA 100, 2322-2327.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2322-2327
    • Padilla, P.I.1    Chang, M.J.2    Pacheco-Rodriguez, G.3    Adamik, R.4    Moss, J.5    Vaughan, M.6
  • 77
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: An application to display phylogenetic trees on personal computers
    • Page, R.D. (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
  • 78
    • 0036866606 scopus 로고    scopus 로고
    • Arf, Arl, Arp and Sar proteins: A family of GTP-binding proteins with a structural device for 'front-back' communication
    • Pasqualato, S., Renault, L., and Cherfils, J. (2002). Arf, Arl, Arp and Sar proteins: a family of GTP-binding proteins with a structural device for 'front-back' communication. EMBO Rep. 3, 1035-1041.
    • (2002) EMBO Rep. , vol.3 , pp. 1035-1041
    • Pasqualato, S.1    Renault, L.2    Cherfils, J.3
  • 79
    • 0028951905 scopus 로고
    • Overexpression of wild-type and mutant ARF1 and ARF 6, distinct perturbations of nonoverlapping membrane compartments
    • Peters, P.J., Hsu, V.W., Ooi, C.E., Finazzi, D., Teal, S.B., Oorschot, V., Donaldson, J.G., and Klausner, R.D. (1995). Overexpression of wild-type and mutant ARF1 and ARF 6, distinct perturbations of nonoverlapping membrane compartments. J. Cell Biol. 128, 1003-1017.
    • (1995) J. Cell Biol. , vol.128 , pp. 1003-1017
    • Peters, P.J.1    Hsu, V.W.2    Ooi, C.E.3    Finazzi, D.4    Teal, S.B.5    Oorschot, V.6    Donaldson, J.G.7    Klausner, R.D.8
  • 80
    • 0002955384 scopus 로고    scopus 로고
    • Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: Involvement of specific residues of the Sec7 domain
    • Peyroche, A., Antonny, B., Robineau, S., Acker, J., Cherfils, J., and Jackson, C.L. (1999). Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain. Mol. Cell 3, 275-285.
    • (1999) Mol. Cell , vol.3 , pp. 275-285
    • Peyroche, A.1    Antonny, B.2    Robineau, S.3    Acker, J.4    Cherfils, J.5    Jackson, C.L.6
  • 81
    • 0034943777 scopus 로고    scopus 로고
    • The ARF exchange factors Gea1p and Gea2p regulate Golgi structure and function in yeast
    • Peyroche, A., Courbeyrette, R., Rambourg, A., and Jackson, C.L. (2001). The ARF exchange factors Gea1p and Gea2p regulate Golgi structure and function in yeast. J. Cell Sci. 114, 2241-2253.
    • (2001) J. Cell Sci. , vol.114 , pp. 2241-2253
    • Peyroche, A.1    Courbeyrette, R.2    Rambourg, A.3    Jackson, C.L.4
  • 82
    • 0029851773 scopus 로고    scopus 로고
    • Nucleotide exchange on ARF mediated by yeast Gea1 protein
    • Peyroche, A., Paris, S., and Jackson, C.L. (1996). Nucleotide exchange on ARF mediated by yeast Gea1 protein. Nature 384, 479-481.
    • (1996) Nature , vol.384 , pp. 479-481
    • Peyroche, A.1    Paris, S.2    Jackson, C.L.3
  • 83
    • 0037252718 scopus 로고    scopus 로고
    • The Proteome Analysis database: A tool for the in silico analysis of whole proteomes
    • Pruess, M., et al. (2003). The Proteome Analysis database: a tool for the in silico analysis of whole proteomes. Nucleic Acids Res. 31, 414-417.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 414-417
    • Pruess, M.1
  • 84
    • 0030816319 scopus 로고    scopus 로고
    • ADP-ribosylation factor 6 regulates a novel plasma membrane recycling pathway
    • Radhakrishna, H., and Donaldson, J.G. (1997). ADP-ribosylation factor 6 regulates a novel plasma membrane recycling pathway. J. Cell Biol. 139, 49-61.
    • (1997) J. Cell Biol. , vol.139 , pp. 49-61
    • Radhakrishna, H.1    Donaldson, J.G.2
  • 85
    • 0034700364 scopus 로고    scopus 로고
    • Molecular aspects of the cellular activities of ADP-ribosylation factors
    • Randazzo, P.A., Nie, Z., Miura, K., and Hsu, V.W. (2000). Molecular aspects of the cellular activities of ADP-ribosylation factors. Sci. STKE 2000, RE1.
    • (2000) Sci. STKE , vol.2000
    • Randazzo, P.A.1    Nie, Z.2    Miura, K.3    Hsu, V.W.4
  • 86
    • 0029007101 scopus 로고
    • The myristoylated amino terminus of ADP-ribosylation factor 1 is a phospholipid- and GTP-sensitive switch
    • Randazzo, P.A., Terui, T., Sturch, S., Fales, H.M., Ferrige, A.G., and Kahn, R.A. (1995). The myristoylated amino terminus of ADP-ribosylation factor 1 is a phospholipid- and GTP-sensitive switch. J. Biol. Chem. 270, 14809-14815.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14809-14815
    • Randazzo, P.A.1    Terui, T.2    Sturch, S.3    Fales, H.M.4    Ferrige, A.G.5    Kahn, R.A.6
  • 87
    • 0027193417 scopus 로고
    • Activation of ADP-ribosylation factor by Golgi membranes. Evidence for a brefeldin A- and protease-sensitive activating factor on Golgi membranes
    • Randazzo, P.A., Yang, Y.C., Rulka, C., and Kahn, R.A. (1993). Activation of ADP-ribosylation factor by Golgi membranes. Evidence for a brefeldin A- and protease-sensitive activating factor on Golgi membranes. J. Biol. Chem. 268, 9555-9563.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9555-9563
    • Randazzo, P.A.1    Yang, Y.C.2    Rulka, C.3    Kahn, R.A.4
  • 88
    • 0037133511 scopus 로고    scopus 로고
    • Mechanism of domain closure of Sec7 domains and role in BFA sensitivity
    • Renault, L., Christova, P., Guibert, B., Pasqualato, S., and Cherfils, J. (2002). Mechanism of domain closure of Sec7 domains and role in BFA sensitivity. Biochemistry 41, 3605-3612.
    • (2002) Biochemistry , vol.41 , pp. 3605-3612
    • Renault, L.1    Christova, P.2    Guibert, B.3    Pasqualato, S.4    Cherfils, J.5
  • 89
    • 0034730123 scopus 로고    scopus 로고
    • Binding site of brefeldin A at the interface between the small G protein ADP-ribosylation factor 1 (ARF1) and the nucleotide-exchange factor Sec7 domain
    • Robineau, S., Chabre, M., and Antonny, B. (2000). Binding site of brefeldin A at the interface between the small G protein ADP-ribosylation factor 1 (ARF1) and the nucleotide-exchange factor Sec7 domain. Proc. Natl. Acad. Sci. USA 97, 9913-9918.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9913-9918
    • Robineau, S.1    Chabre, M.2    Antonny, B.3
  • 91
    • 0022833247 scopus 로고
    • The number of nucleotides required to determine the branching order of three species, with special reference to the human-chimpanzee-gorilla divergence
    • Saitou, N., and Nei, M. (1986). The number of nucleotides required to determine the branching order of three species, with special reference to the human-chimpanzee-gorilla divergence. J. Mol. Evol. 24, 189-204.
    • (1986) J. Mol. Evol. , vol.24 , pp. 189-204
    • Saitou, N.1    Nei, M.2
  • 92
    • 0032515997 scopus 로고    scopus 로고
    • Brefeldin A-inhibited guanine nucleotide-exchange activity of Sec7 domain from yeast Sec7 with yeast and mammalian ADP ribosylation factors
    • Sata, M., Donaldson, J.G., Moss, J., and Vaughan, M. (1998). Brefeldin A-inhibited guanine nucleotide-exchange activity of Sec7 domain from yeast Sec7 with yeast and mammalian ADP ribosylation factors. Proc. Natl. Acad. Sci. USA 95, 4204-4208.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4204-4208
    • Sata, M.1    Donaldson, J.G.2    Moss, J.3    Vaughan, M.4
  • 93
    • 0033049656 scopus 로고    scopus 로고
    • Structural basis for the inhibitory effect of brefeldin A on guanine nucleotide-exchange proteins for ADP-ribosylation factors
    • Sata, M., Moss, J., and Vaughan, M. (1999). Structural basis for the inhibitory effect of brefeldin A on guanine nucleotide-exchange proteins for ADP-ribosylation factors. Proc. Natl. Acad. Sci. USA 96, 2752-2757.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2752-2757
    • Sata, M.1    Moss, J.2    Vaughan, M.3
  • 94
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz, J., Milpetz, F., Bork, P., and Ponting, C.P. (1998). SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl. Acad. Sci. USA 95, 5857-5864.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 95
    • 0036295057 scopus 로고    scopus 로고
    • Dominant-negative mutant of BIG2, an ARF-guanine nucleotide exchange factor, specifically affects membrane trafficking from the trans-Golgi network through inhibiting membrane association of AP-1 and GGA coat proteins
    • Shinotsuka, C., Waguri, S., Wakasugi, M., Uchiyama, Y., and Nakayama, K. (2002a). Dominant-negative mutant of BIG2, an ARF-guanine nucleotide exchange factor, specifically affects membrane trafficking from the trans-Golgi network through inhibiting membrane association of AP-1 and GGA coat proteins. Biochem. Biophys. Res. Commun. 294, 254-260.
    • (2002) Biochem. Biophys. Res. Commun. , vol.294 , pp. 254-260
    • Shinotsuka, C.1    Waguri, S.2    Wakasugi, M.3    Uchiyama, Y.4    Nakayama, K.5
  • 96
    • 0037088675 scopus 로고    scopus 로고
    • Overexpression of an ADP-ribosylation factor-guanine 1nucleotide exchange factor, BIG2, uncouples brefeldin A-induced adaptor protein-1 coat dissociation and membrane tubulation
    • Shinotsuka, C., Yoshida, Y., Kawamoto, K., Takatsu, H., and Nakayama, K. (2002b). Overexpression of an ADP-ribosylation factor-guanine nucleotide exchange factor, BIG2, uncouples brefeldin A-induced adaptor protein-1 coat dissociation and membrane tubulation. J. Biol. Chem. 277, 9468-9473.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9468-9473
    • Shinotsuka, C.1    Yoshida, Y.2    Kawamoto, K.3    Takatsu, H.4    Nakayama, K.5
  • 98
    • 0035172344 scopus 로고    scopus 로고
    • The ADP ribosylation factor-nucleotide exchange factors Gea1p and Gea2p have overlapping, but not redundant functions in retrograde transport from the Golgi to the endoplasmic reticulum
    • Spang, A., Herrmann, J.M., Hamamoto, S., and Schekman, R. (2001). The ADP ribosylation factor-nucleotide exchange factors Gea1p and Gea2p have overlapping, but not redundant functions in retrograde transport from the Golgi to the endoplasmic reticulum. Mol. Biol. Cell 12, 1035-1045.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1035-1045
    • Spang, A.1    Herrmann, J.M.2    Hamamoto, S.3    Schekman, R.4
  • 100
    • 0025174078 scopus 로고
    • ADP-ribosylation factor is functionally and physically associated with the Golgi complex
    • Stearns, T., Willingham, M.C., Botstein, D., and Kahn, R.A. (1990). ADP-ribosylation factor is functionally and physically associated with the Golgi complex. Proc. Natl. Acad. Sci. USA 87, 1238-1242.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1238-1242
    • Stearns, T.1    Willingham, M.C.2    Botstein, D.3    Kahn, R.A.4
  • 104
    • 18344361838 scopus 로고    scopus 로고
    • Cybr, a cytokine-inducible protein that binds cytohesin-1 and regulates its activity
    • Tang, P., et al. (2002). Cybr, a cytokine-inducible protein that binds cytohesin-1 and regulates its activity. Proc. Natl. Acad. Sci. USA 99, 2625-2629.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2625-2629
    • Tang, P.1
  • 105
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994). CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 106
    • 0033617147 scopus 로고    scopus 로고
    • Purification and cloning of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors
    • Togawa, A., Morinaga, N., Ogasawara, M., Moss, J., and Vaughan, M. (1999). Purification and cloning of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors. J. Biol. Chem. 274, 12308-12315.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12308-12315
    • Togawa, A.1    Morinaga, N.2    Ogasawara, M.3    Moss, J.4    Vaughan, M.5
  • 107
    • 0242321942 scopus 로고    scopus 로고
    • Interaction protein for cytohesin exchange factors 1 (IPCEF1) binds cytohesin 2 and modifies its activity
    • Venkateswarlu, K. (2003). Interaction protein for cytohesin exchange factors 1 (IPCEF1) binds cytohesin 2 and modifies its activity. J. Biol. Chem. 278, 43460-43469.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43460-43469
    • Venkateswarlu, K.1
  • 108
    • 0035031966 scopus 로고    scopus 로고
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach
    • Whelan, S., and Goldman, N. (2001). A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach. Mol. Biol. Evol. 18, 691-699.
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 691-699
    • Whelan, S.1    Goldman, N.2
  • 109
    • 0035175981 scopus 로고    scopus 로고
    • Multiple roles of Arf1 GTPase in the yeast exocytic and endocytic pathways
    • Yahara, N., Ueda, T., Sato, K., and Nakano, A. (2001). Multiple roles of Arf1 GTPase in the yeast exocytic and endocytic pathways. Mol. Biol. Cell 12, 221-238.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 221-238
    • Yahara, N.1    Ueda, T.2    Sato, K.3    Nakano, A.4
  • 110
    • 0000645017 scopus 로고    scopus 로고
    • Subcellular distribution and differential expression of endogenous ADP-ribosylation factor 6 in mammalian cells
    • Yang, C.Z., Heimberg, H., D'Souza-Schorey, C., Mueckler, M.M., and Stahl, P.D. (1998). Subcellular distribution and differential expression of endogenous ADP-ribosylation factor 6 in mammalian cells. J. Biol. Chem. 273, 4006-4011.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4006-4011
    • Yang, C.Z.1    Heimberg, H.2    D'Souza-Schorey, C.3    Mueckler, M.M.4    Stahl, P.D.5
  • 111
    • 0036151274 scopus 로고    scopus 로고
    • Localization of large ADP-ribosylation factor-guanine nucleotide exchange factors to different Golgi compartments: Evidence for distinct functions in protein traffic
    • Zhao, X., Lasell, T.K., and Melancon, P. (2002). Localization of large ADP-ribosylation factor-guanine nucleotide exchange factors to different Golgi compartments: evidence for distinct functions in protein traffic. Mol. Biol. Cell 13, 119-133.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 119-133
    • Zhao, X.1    Lasell, T.K.2    Melancon, P.3


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