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Volumn 63, Issue 3, 2000, Pages 400-408

Characterization, chromosomal assignment, and tissue expression of a novel human gene belonging to the ARF GAP family

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; COMPLEMENTARY DNA;

EID: 0034143665     PISSN: 08887543     EISSN: None     Source Type: Journal    
DOI: 10.1006/geno.1999.6095     Document Type: Article
Times cited : (18)

References (47)
  • 3
    • 0030692015 scopus 로고    scopus 로고
    • Activation of ADP-ribosylation factor 1 GTPase-activating protein by phosphatidylcholine-derived diacylglycerols
    • Antonny B., Huber I., Paris S., Chabre M., Cassel D. Activation of ADP-ribosylation factor 1 GTPase-activating protein by phosphatidylcholine-derived diacylglycerols. J. Biol. Chem. 272:1997;30848-30851.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30848-30851
    • Antonny, B.1    Huber, I.2    Paris, S.3    Chabre, M.4    Cassel, D.5
  • 4
    • 0028904466 scopus 로고
    • Arf proteins: The membrane traffic police
    • Boman A. L., Kahn R. A. Arf proteins: The membrane traffic police. Trends Biochem. Sci. 20:1995;147-150.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 147-150
    • Boman, A.L.1    Kahn, R.A.2
  • 5
    • 0031784899 scopus 로고    scopus 로고
    • ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src
    • Brown M. T., Andrade J., Radhakrishna H., Donaldson J. G., Cooper J. A., Randazzo P. A. ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src. Mol. Cell. Biol. 18:1998;7038-7051.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7038-7051
    • Brown, M.T.1    Andrade, J.2    Radhakrishna, H.3    Donaldson, J.G.4    Cooper, J.A.5    Randazzo, P.A.6
  • 6
    • 0027482720 scopus 로고
    • Selective amplification of additional members of the ADP-ribosylation factor (ARF) family: Cloning of additional human and Drosophila ARF-like genes
    • Clark J., Moore L., Krasinskas A., Way J., Battey J., Tamkun J., Kahn R. A. Selective amplification of additional members of the ADP-ribosylation factor (ARF) family: Cloning of additional human and Drosophila ARF-like genes. Proc. Natl. Acad. Sci. USA. 90:1993;8952-8956.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8952-8956
    • Clark, J.1    Moore, L.2    Krasinskas, A.3    Way, J.4    Battey, J.5    Tamkun, J.6    Kahn, R.A.7
  • 8
    • 0029416828 scopus 로고
    • The ARF1 GTPase-activating protein: Zinc finger motif and Golgi complex localization
    • Cukierman E., Huber I., Rotman M., Cassel D. The ARF1 GTPase-activating protein: Zinc finger motif and Golgi complex localization. Science. 270:1995;1999-2002.
    • (1995) Science , vol.270 , pp. 1999-2002
    • Cukierman, E.1    Huber, I.2    Rotman, M.3    Cassel, D.4
  • 10
    • 0028128334 scopus 로고
    • ARF: A key regulatory switch in membrane traffic and organelle structure
    • Donaldson J. G., Klausner R. D. ARF: A key regulatory switch in membrane traffic and organelle structure. Curr. Opin. Cell. Biol. 6:1994;527-532.
    • (1994) Curr. Opin. Cell. Biol. , vol.6 , pp. 527-532
    • Donaldson, J.G.1    Klausner, R.D.2
  • 11
    • 0026623115 scopus 로고
    • ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membrane
    • Donaldson J. G., Cassel D., Kahn R. A., Klausner R. D. ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membrane. Proc. Natl. Acad. Sci. USA. 89:1992;6408-6412.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6408-6412
    • Donaldson, J.G.1    Cassel, D.2    Kahn, R.A.3    Klausner, R.D.4
  • 12
    • 0029890939 scopus 로고    scopus 로고
    • Evidence for expression of vasopressin V2 receptor mRNA in human lung
    • Fay M. J., Du J., Yu X., North W. G. Evidence for expression of vasopressin V2 receptor mRNA in human lung. Peptides. 17:1996;477-481.
    • (1996) Peptides , vol.17 , pp. 477-481
    • Fay, M.J.1    Du, J.2    Yu, X.3    North, W.G.4
  • 13
    • 0033582917 scopus 로고    scopus 로고
    • Structure and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis
    • Goldberg J. Structure and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Cell. 96:1999;893-902.
    • (1999) Cell , vol.96 , pp. 893-902
    • Goldberg, J.1
  • 14
    • 0026347535 scopus 로고
    • Structure and promoter activity of the gene for the erythroid transcription factor GATA-1
    • Hannon R., Evans T., Felsenfeld G., Gould H. Structure and promoter activity of the gene for the erythroid transcription factor GATA-1. Proc. Natl. Acad. Sci. USA. 88:1991;3004-3008.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3004-3008
    • Hannon, R.1    Evans, T.2    Felsenfeld, G.3    Gould, H.4
  • 15
    • 0027512321 scopus 로고
    • Human hepatic stimulator substance: A product of gene expression of human fetal liver tissue
    • He F., Wu C., Tu Q., Xing G. Human hepatic stimulator substance: A product of gene expression of human fetal liver tissue. Hepatology. 17:1993;225-229.
    • (1993) Hepatology , vol.17 , pp. 225-229
    • He, F.1    Wu, C.2    Tu, Q.3    Xing, G.4
  • 17
    • 0028017275 scopus 로고
    • A member of a novel family of yeast 'zn-finger' proteins mediates the transition from stationary phase to cell proliferation
    • Ireland L. S., Johnston G. C., Drebot M. A., Dhillon N., Demaggio A. J., Hoekstra M. F., Singer R. A. A member of a novel family of yeast 'zn-finger' proteins mediates the transition from stationary phase to cell proliferation. EMBO J. 13:1994;3812-3821.
    • (1994) EMBO J. , vol.13 , pp. 3812-3821
    • Ireland, L.S.1    Johnston, G.C.2    Drebot, M.A.3    Dhillon, N.4    Demaggio, A.J.5    Hoekstra, M.F.6    Singer, R.A.7
  • 18
    • 0022978533 scopus 로고
    • The protein cofactor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP binding protein
    • Kahn R. A., Gilman A. G. The protein cofactor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP binding protein. J. Biol. Chem. 261:1986;7906-7911.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7906-7911
    • Kahn, R.A.1    Gilman, A.G.2
  • 19
    • 0023928057 scopus 로고
    • Chemical and immunological characterization of the 21-kDa ADP-ribosylation factor of adenylate cyclase
    • Kahn R. A., Goddard C., Newkirk M. Chemical and immunological characterization of the 21-kDa ADP-ribosylation factor of adenylate cyclase. J. Biol. Chem. 263:1988;8282-8287.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8282-8287
    • Kahn, R.A.1    Goddard, C.2    Newkirk, M.3
  • 20
    • 0030975196 scopus 로고    scopus 로고
    • Signaling by phosphoinositide-3,4,5-triphosphate through proteins containing pleckstrin and Sec7 homology domains
    • Klarlund J. K., Guilherme A., Holik J. J., Virbasius J. V., Chawla A., Czech M. P. Signaling by phosphoinositide-3,4,5-triphosphate through proteins containing pleckstrin and Sec7 homology domains. Science. 275:1997;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
  • 21
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak M. An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res. 15:1987;8125-8131.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8125-8131
    • Kozak, M.1
  • 22
    • 0027984138 scopus 로고
    • GAPs for rho-related GTPases
    • Lamarche N., Hall A. GAPs for rho-related GTPases. Trends Genet. 10:1994;436-440.
    • (1994) Trends Genet. , vol.10 , pp. 436-440
    • Lamarche, N.1    Hall, A.2
  • 25
    • 0031041536 scopus 로고    scopus 로고
    • Cytohesin-1, a cytosolic guanine nucleotide-exchange protein for ADP-ribosylation factor
    • Meacci E., Tsai S. C., Adamik R., Moss J., Vaughan M. Cytohesin-1, a cytosolic guanine nucleotide-exchange protein for ADP-ribosylation factor. Proc. Natl. Acad. Sci. USA. 94:1997;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
  • 26
    • 0031743659 scopus 로고    scopus 로고
    • Overexpression of the ARF1 exchange factor ARNO inhibits the early secretory pathway and causes the disassembly of the Golgi complex
    • Monier S., Chardin P., Robineau S., Goud B. Overexpression of the ARF1 exchange factor ARNO inhibits the early secretory pathway and causes the disassembly of the Golgi complex. J. Cell Sci. 111:1998;3427-3436.
    • (1998) J. Cell Sci. , vol.111 , pp. 3427-3436
    • Monier, S.1    Chardin, P.2    Robineau, S.3    Goud, B.4
  • 27
    • 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., Vaughan M. 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. 94:1997;12926-12931.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12926-12931
    • Morinaga, N.1    Moss, J.2    Vaughan, M.3
  • 28
    • 0032555493 scopus 로고    scopus 로고
    • Molecules in the ARF orbit
    • Moss J., Vaughan M. Molecules in the ARF orbit. J. Biol. Chem. 273:1998;21431-21434.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21431-21434
    • Moss, J.1    Vaughan, M.2
  • 29
    • 0027291429 scopus 로고
    • Coated vesicles assembly in the Golgi requires only coatomer and ARF proteins from the cytosol
    • Orci L., Palmer D. J., Amherdt M., Rothman J. E. Coated vesicles assembly in the Golgi requires only coatomer and ARF proteins from the cytosol. Nature. 364:1993;732-734.
    • (1993) Nature , vol.364 , pp. 732-734
    • Orci, L.1    Palmer, D.J.2    Amherdt, M.3    Rothman, J.E.4
  • 30
    • 0024999474 scopus 로고
    • Preferential suppression of low molecular weight natural tumor suppressor of human fetal liver origin on the growth of leukemic cells in vitro
    • Pei X. T., Wu C. T. Preferential suppression of low molecular weight natural tumor suppressor of human fetal liver origin on the growth of leukemic cells in vitro. Exp. Hematol. 18:1990;927-931.
    • (1990) Exp. Hematol. , vol.18 , pp. 927-931
    • Pei, X.T.1    Wu, C.T.2
  • 31
    • 0029851773 scopus 로고    scopus 로고
    • Nucleotide exchange on ARF mediated by yeast Gea1 protein
    • Peyroche A., Paris S., Jackson C. L. Nucleotide exchange on ARF mediated by yeast Gea1 protein. Nature. 384:1996;479-481.
    • (1996) Nature , vol.384 , pp. 479-481
    • Peyroche, A.1    Paris, S.2    Jackson, C.L.3
  • 32
    • 0033081078 scopus 로고    scopus 로고
    • Retrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function
    • Poon P. P., Cassel D., Spang A., Rotman M., Pick E., Singer R. A., Johnston G. C. Retrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function. EMBO J. 18:1999;555-564.
    • (1999) EMBO J. , vol.18 , pp. 555-564
    • Poon, P.P.1    Cassel, D.2    Spang, A.3    Rotman, M.4    Pick, E.5    Singer, R.A.6    Johnston, G.C.7
  • 35
    • 0026713293 scopus 로고
    • The small GTP-binding proteins in the cytosol of insulin-secreting cells are complexed to GDP dissociation inhibitor proteins
    • Regazzi R., Kikuchi A., Takai Y., Wollheim C. B. The small GTP-binding proteins in the cytosol of insulin-secreting cells are complexed to GDP dissociation inhibitor proteins. J. Biol. Chem. 267:1992;17512-17519.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17512-17519
    • Regazzi, R.1    Kikuchi, A.2    Takai, Y.3    Wollheim, C.B.4
  • 36
    • 0028952289 scopus 로고
    • Optimization and troubleshooting in PCR
    • Roux K. H. Optimization and troubleshooting in PCR. PCR Methods Appl. 4:1995;5185-5194.
    • (1995) PCR Methods Appl. , vol.4 , pp. 5185-5194
    • Roux, K.H.1
  • 37
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman R., Orci L. Coat proteins and vesicle budding. Science. 271:1996;1526-1533.
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 38
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz J., Milpetz F., Bork P., Ponting C. P. SMART, a simple modular architecture research tool: Identification of signaling domains. Proc. Natl. Acad. Sci. USA. 95:1998;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
  • 39
    • 0026001029 scopus 로고
    • ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein
    • Serafini T., Orci L., Amherdt M., Brunner M., Kahn R. A., Rothman J. E. ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein. Cell. 67:1991;239-253.
    • (1991) Cell , vol.67 , pp. 239-253
    • Serafini, T.1    Orci, L.2    Amherdt, M.3    Brunner, M.4    Kahn, R.A.5    Rothman, J.E.6
  • 40
    • 0030033390 scopus 로고    scopus 로고
    • Purification and characterization of a guanine nucleotide-exchange protein for ADP-ribosylation factor from spleen cytosol
    • Tsai S. C., Adamik R., Moss J., Vaughan M. Purification and characterization of a guanine nucleotide-exchange protein for ADP-ribosylation factor from spleen cytosol. Proc. Natl. Acad. Sci. USA. 93:1996;305-309.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 305-309
    • Tsai, S.C.1    Adamik, R.2    Moss, J.3    Vaughan, M.4
  • 41
    • 0031054516 scopus 로고    scopus 로고
    • Interaction of the GTP-binding and GTPase-activating domains of ARD1 involves the effector region of the ADP-ribosylation factor domain
    • Vitale N., Moss J., Vaughan M. Interaction of the GTP-binding and GTPase-activating domains of ARD1 involves the effector region of the ADP-ribosylation factor domain. J. Biol. Chem. 272:1997a;3897-3904.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3897-3904
    • Vitale, N.1    Moss, J.2    Vaughan, M.3
  • 42
    • 0030764887 scopus 로고    scopus 로고
    • Characterization of a GDP dissociation inhibitory region of ADP-ribosylation factor domain protein ARD1
    • Vitale N., Moss J., Vaughan M. Characterization of a GDP dissociation inhibitory region of ADP-ribosylation factor domain protein ARD1. J. Biol. Chem. 272:1997b;25077-25082.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25077-25082
    • Vitale, N.1    Moss, J.2    Vaughan, M.3
  • 44
    • 0030294808 scopus 로고    scopus 로고
    • Purging effect of dibutyl phthalate on leukemic cells associated with apoptosis
    • Wang L. S., Wu C. T., Pei X. T., Cao J. R., He F. C. Purging effect of dibutyl phthalate on leukemic cells associated with apoptosis. Leukocyte Res. 20:1996;989-992.
    • (1996) Leukocyte Res. , vol.20 , pp. 989-992
    • Wang, L.S.1    Wu, C.T.2    Pei, X.T.3    Cao, J.R.4    He, F.C.5
  • 46
    • 0024577218 scopus 로고
    • Effects of human fetal liver extract on the growth of HL-60 cells
    • Wu C. T., Pei X. T., Cong P. J. Effects of human fetal liver extract on the growth of HL-60 cells. Exp. Hematol. 17:1989;304-308.
    • (1989) Exp. Hematol. , vol.17 , pp. 304-308
    • Wu, C.T.1    Pei, X.T.2    Cong, P.J.3
  • 47
    • 0025150763 scopus 로고
    • Comparison of the hemopoietic growth factors produced during in vitro culture of murine and human fetal liver cells
    • Zhao S. F., Wu C. T. Comparison of the hemopoietic growth factors produced during in vitro culture of murine and human fetal liver cells. Exp. Hematol. 18:1990;367-371.
    • (1990) Exp. Hematol. , vol.18 , pp. 367-371
    • Zhao, S.F.1    Wu, C.T.2


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