메뉴 건너뛰기




Volumn 426, Issue 6966, 2003, Pages 525-530

Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CATALYSIS; DISSOCIATION;

EID: 0346243924     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02197     Document Type: Review
Times cited : (270)

References (45)
  • 1
    • 0037142034 scopus 로고    scopus 로고
    • Mice deficient in the RAc activator Tiam1 are resistant to Ras-induced skin tumours
    • Malliri, A. et al. Mice deficient in the RAc activator Tiam1 are resistant to Ras-induced skin tumours. Nature 417, 867-871 (2002).
    • (2002) Nature , vol.417 , pp. 867-871
    • Malliri, A.1
  • 2
    • 0026677375 scopus 로고
    • Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein
    • Donaldson, J. G., Finazzi, D. & Klausner, R. D. Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein. Nature 360, 350-352 (1992).
    • (1992) Nature , vol.360 , pp. 350-352
    • Donaldson, J.G.1    Finazzi, D.2    Klausner, R.D.3
  • 3
    • 0026746713 scopus 로고
    • Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF
    • Helms, J. B. & Rothman, J. E. Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF. Nature 360, 352-354 (1992).
    • (1992) Nature , vol.360 , pp. 352-354
    • Helms, J.B.1    Rothman, J.E.2
  • 4
    • 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. et al. 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).
    • (1999) Mol. Cell , vol.3 , pp. 275-285
    • Peyroche, A.1
  • 5
    • 0035942221 scopus 로고    scopus 로고
    • Controlling small guanine-nucleotide-exchange factor function through cytoplasmic RNA intramers
    • Mayer, G. et al. Controlling small guanine-nucleotide-exchange factor function through cytoplasmic RNA intramers. Proc. Natl Acad. Sci. USA 98, 4961-4965 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4961-4965
    • Mayer, G.1
  • 6
    • 0037125232 scopus 로고    scopus 로고
    • Identification of the first Rho-GEF inhibitor, TRIPα, which targets the RhoA-specific GEF domain of Trio
    • Schmidt, S., Diriong, S., Mery, J., Fabbrizio, E. & Debant, A. Identification of the first Rho-GEF inhibitor, TRIPα, which targets the RhoA-specific GEF domain of Trio. FEBS Lett. 523, 35-42 (2002).
    • (2002) FEBS Lett. , vol.523 , pp. 35-42
    • Schmidt, S.1    Diriong, S.2    Mery, J.3    Fabbrizio, E.4    Debant, A.5
  • 7
    • 0028801195 scopus 로고
    • The kinetic mechanism of Ran-nucleotide exchange catalyzed by RCC1
    • Klebe, C., Prinz, H., Wittinghofer, A. & Goody, R. S. The kinetic mechanism of Ran-nucleotide exchange catalyzed by RCC1. Biochemistry 34, 12543-12552 (1995).
    • (1995) Biochemistry , vol.34 , pp. 12543-12552
    • Klebe, C.1    Prinz, H.2    Wittinghofer, A.3    Goody, R.S.4
  • 8
    • 0032546533 scopus 로고    scopus 로고
    • Kinetic analysis by fluorescence of the interaction between Ras and the catalytic domain of the guanine nucleotide exchange factor Cdc25Mm
    • Lenzen, C., Cool, R. H., Prinz, H., Kuhlmann, J. & Wittinghofer, A. Kinetic analysis by fluorescence of the interaction between Ras and the catalytic domain of the guanine nucleotide exchange factor Cdc25Mm. Biochemistry 37, 7420-7430 (1998).
    • (1998) Biochemistry , vol.37 , pp. 7420-7430
    • Lenzen, C.1    Cool, R.H.2    Prinz, H.3    Kuhlmann, J.4    Wittinghofer, A.5
  • 9
    • 0036656168 scopus 로고    scopus 로고
    • Exchange factors, effectors, GAPs and motor proteins: Common thermodynamic and kinetic principles for different functions
    • Goody, R. S. & Hofmann-Goody, W. Exchange factors, effectors, GAPs and motor proteins: common thermodynamic and kinetic principles for different functions. Eur. Biophys. J. 31, 268-274 (2002).
    • (2002) Eur. Biophys. J. , vol.31 , pp. 268-274
    • Goody, R.S.1    Hofmann-Goody, W.2
  • 11
    • 0032538317 scopus 로고    scopus 로고
    • Structural basis for activation of ARF GTPase: Mechanisms of guanine nucleotide exchange and GTP-myristoyl switching
    • Goldberg, J. Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching. Cell 95, 237-248 (1998).
    • (1998) Cell , vol.95 , pp. 237-248
    • Goldberg, J.1
  • 12
    • 0034619877 scopus 로고    scopus 로고
    • Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1
    • Worthylakej D. K., Rossman, K. L. & Sondek, J. Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1. Nature 408, 682-688 (2000).
    • (2000) Nature , vol.408 , pp. 682-688
    • Worthylakej, D.K.1    Rossman, K.L.2    Sondek, J.3
  • 13
    • 0035917523 scopus 로고    scopus 로고
    • Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1)
    • Renault, L., Kuhlmann, J., Henkel, A. & Wittinghofer, A. Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1). Cell 105, 245-255 (2001).
    • (2001) Cell , vol.105 , pp. 245-255
    • Renault, L.1    Kuhlmann, J.2    Henkel, A.3    Wittinghofer, A.4
  • 15
    • 0039818755 scopus 로고    scopus 로고
    • 2+ and the β-phosphate to destabilize GDP on ARF1
    • 2+ and the β-phosphate to destabilize GDP on ARF1. EMBO J. 17, 3651-3659 (1998).
    • (1998) EMBO J. , vol.17 , pp. 3651-3659
    • Beraud-Dufour, S.1
  • 16
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter, I. R. & Wittinghofer, A. The guanine nucleotide-binding switch in three dimensions. Science 294, 1299-1304 (2001).
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 17
    • 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. & Cherfils, J. 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).
    • (2002) EMBO Rep. , vol.3 , pp. 1035-1041
    • Pasqualato, S.1    Renault, L.2    Cherfils, J.3
  • 18
    • 0028556994 scopus 로고
    • Structure of the human ADP-ribosylation factor I complexed with GDP
    • Amor, J. C., Harrison, D. H., Kahn, R. A. & Ringe, D. Structure of the human ADP-ribosylation factor I complexed with GDP. Nature 372, 704-708 (1994).
    • (1994) Nature , vol.372 , pp. 704-708
    • Amor, J.C.1    Harrison, D.H.2    Kahn, R.A.3    Ringe, D.4
  • 19
    • 0142097228 scopus 로고    scopus 로고
    • Structure of Arf6-GDP suggests a basis for guanine nucleotide exchange factors specificity
    • Menetrey, J., Macia, E., Pasqualato, S., Franco, M. & Cherfils, J. Structure of Arf6-GDP suggests a basis for guanine nucleotide exchange factors specificity. Nature Struct. Biol. 7, 466-469 (2000).
    • (2000) Nature Struct. Biol. , vol.7 , pp. 466-469
    • Menetrey, J.1    Macia, E.2    Pasqualato, S.3    Franco, M.4    Cherfils, J.5
  • 20
    • 0030891289 scopus 로고    scopus 로고
    • N-terminnal 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. & Chabre, M. N-terminnal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange. Biochemistry 36, 4675-4684 (1997).
    • (1997) Biochemistry , vol.36 , pp. 4675-4684
    • Antonny, B.1    Beraud-Dufour, S.2    Chardin, P.3    Chabre, M.4
  • 21
    • 0033950864 scopus 로고    scopus 로고
    • Turning on ARF: The Sec7 family of guanine-nucleotide-exchange factors
    • Jackson, C. L. & Casanova, J. E. Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors. Trends Cell Biol. 10, 60-67 (2000).
    • (2000) Trends Cell Biol. , vol.10 , pp. 60-67
    • Jackson, C.L.1    Casanova, J.E.2
  • 22
    • 0032485074 scopus 로고    scopus 로고
    • Structure of the Sec7 domain of the Arf exchange factor ARNO
    • Cherfils, J. et al. Structure of the Sec7 domain of the Arf exchange factor ARNO. Nature 392, 101-105 (1998).
    • (1998) Nature , vol.392 , pp. 101-105
    • Cherfils, J.1
  • 23
    • 0033529249 scopus 로고    scopus 로고
    • p200 ARF-GEP1: A Golgi-localized guanine nucleotide exchange protein whose Sec7 domain is targeted by the drug brefeldin A
    • Mansour, S. J. et al. p200 ARF-GEP1: 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).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7968-7973
    • Mansour, S.J.1
  • 24
    • 0033644364 scopus 로고    scopus 로고
    • Brefeldin A revealing the fundamental principles governing membrane dynamics and protein transport
    • Jackson, C. L. Brefeldin A revealing the fundamental principles governing membrane dynamics and protein transport. Subcell. Biochem. 34, 233-272 (2000).
    • (2000) Subcell. Biochem. , vol.34 , pp. 233-272
    • Jackson, C.L.1
  • 25
    • 0033998897 scopus 로고    scopus 로고
    • Elucidation of strict structural requirements of brefeldin A as an inducer of differentiation and apoptosis
    • Zhu, J. W. et al. Elucidation of strict structural requirements of brefeldin A as an inducer of differentiation and apoptosis. Bioorg. Med. Chem. 8, 455-463 (2000).
    • (2000) Bioorg. Med. Chem. , vol.8 , pp. 455-463
    • Zhu, J.W.1
  • 26
    • 0029844904 scopus 로고    scopus 로고
    • A human exchange factor for ARF contains Sec7- and pleckstrin-homology domains
    • Chardin, P. et al. A human exchange factor for ARF contains Sec7- and pleckstrin-homology domains. Nature 384, 481-484 (1996).
    • (1996) Nature , vol.384 , pp. 481-484
    • Chardin, P.1
  • 27
    • 0033549576 scopus 로고    scopus 로고
    • GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5
    • Claude, A. et al. GBF1: 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).
    • (1999) J. Cell Biol. , vol.146 , pp. 71-84
    • Claude, A.1
  • 28
    • 0033937941 scopus 로고    scopus 로고
    • Regulators and effectors of the ARF GTPases
    • Donaldson, J. G. & Jackson, C. L. Regulators and effectors of the ARF GTPases. Curr. Opin. Cell Biol. 12, 475-482 (2000).
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 475-482
    • Donaldson, J.G.1    Jackson, C.L.2
  • 29
    • 0142211351 scopus 로고    scopus 로고
    • Multiple roles for Arf6: Sorting, structuring, and signaling at the plasma membrane
    • Donaldson, J. G. Multiple roles for Arf6: Sorting, structuring, and signaling at the plasma membrane. J. Biol. Chem. 11, 41573-41576 (2003).
    • (2003) J. Biol. Chem. , vol.11 , pp. 41573-41576
    • Donaldson, J.G.1
  • 30
    • 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. & Vaughan, M. 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).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2752-2757
    • Sata, M.1    Moss, J.2    Vaughan, M.3
  • 31
    • 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., Wick, S., Paprotka, K., Zauner, S. & Lingelbach, K. 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).
    • (2001) Mol. Microbiol. , vol.41 , pp. 1151-1158
    • Baumgartner, F.1    Wick, S.2    Paprotka, K.3    Zauner, S.4    Lingelbach, K.5
  • 32
    • 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. & Antonny, B. 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).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9913-9918
    • Robineau, S.1    Chabre, M.2    Antonny, B.3
  • 33
    • 0033574449 scopus 로고    scopus 로고
    • Brefeldin A: The advantage of being uncompetitive
    • Chardin, P. & McCormick, F. Brefeldin A: the advantage of being uncompetitive. Cell 97, 153-155 (1999).
    • (1999) Cell , vol.97 , pp. 153-155
    • Chardin, P.1    McCormick, F.2
  • 34
    • 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. & Antonny, B. 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).
    • (1999) J. Biol. Chem. , vol.274 , pp. 37629-37636
    • Beraud-Dufour, S.1    Paris, S.2    Chabre, M.3    Antonny, B.4
  • 35
    • 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. & Cherfils, J. Mechanism of domain closure of Sec7 domains and role in BFA sensitivity. Biochemistry 41, 3605-3612 (2002).
    • (2002) Biochemistry , vol.41 , pp. 3605-3612
    • Renault, L.1    Christova, P.2    Guibert, B.3    Pasqualato, S.4    Cherfils, J.5
  • 37
    • 0029051356 scopus 로고
    • Cytotoxicity of brefeldin A correlates with its inhibitory effect on membrane binding of COP coat proteins
    • Torii, S. et al. Cytotoxicity of brefeldin A correlates with its inhibitory effect on membrane binding of COP coat proteins. J. Biol. Chem. 270, 11574-11580 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 11574-11580
    • Torii, S.1
  • 38
    • 0347385415 scopus 로고    scopus 로고
    • (ed. Kahn, R. A.) Ch. 3 (Kluwer Academic, Dordrecht, in the press)
    • Pasqualato, S., Renault, L. & Cherfils, J. in The ARF Book (ed. Kahn, R. A.) Ch. 3 (Kluwer Academic, Dordrecht, in the press).
    • The ARF Book
    • Pasqualato, S.1    Renault, L.2    Cherfils, J.3
  • 39
    • 0033636402 scopus 로고    scopus 로고
    • Small-molecule inhibitors of cell signaling
    • McCormick, F. Small-molecule inhibitors of cell signaling. Curr. Opin. Biotechnol. 11, 593-597 (2000).
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 593-597
    • McCormick, F.1
  • 40
    • 0037416221 scopus 로고    scopus 로고
    • Structural view of a fungal toxin acting on a 14-3-3 regulatory complex
    • Wurtele, M., Jclich-Ottmann, C., Wittinghofer, A. & Oecking, C. Structural view of a fungal toxin acting on a 14-3-3 regulatory complex. EMBO J. 22, 987-994 (2003).
    • (2003) EMBO J. , vol.22 , pp. 987-994
    • Wurtele, M.1    Jclich-Ottmann, C.2    Wittinghofer, A.3    Oecking, C.4
  • 41
    • 0029842109 scopus 로고    scopus 로고
    • Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP
    • Choi, J., Chen, J., Schreiber, S. L. & Clardy, J. Structure of the FKBP 12-rapamycin complex interacting with the binding domain of human FRAP. Science 273, 239-242 (1996).
    • (1996) Science , vol.273 , pp. 239-242
    • Choi, J.1    Chen, J.2    Schreiber, S.L.3    Clardy, J.4
  • 42
    • 0035798244 scopus 로고    scopus 로고
    • Structural mimicry of DH domains by Arfaptin suggests a model for the recognition of Rac-GDP by its guanine nucleotide exchange factors
    • Cherfils, J. Structural mimicry of DH domains by Arfaptin suggests a model for the recognition of Rac-GDP by its guanine nucleotide exchange factors. FEBS Lett. 507, 280-284 (2001).
    • (2001) FEBS Lett. , vol.507 , pp. 280-284
    • Cherfils, J.1
  • 43
    • 0038311995 scopus 로고    scopus 로고
    • Ras family signaling: Therapeutic targeting
    • Cox, A. D. & Der, C. J. Ras family signaling: therapeutic targeting. Cancer Biol. Ther. 1, 599-606 (2002).
    • (2002) Cancer Biol. Ther. , vol.1 , pp. 599-606
    • Cox, A.D.1    Der, C.J.2
  • 44
    • 0037139607 scopus 로고    scopus 로고
    • The role of Rho GTPases in disease development
    • Boettner, B. & Van Aelst, L. The role of Rho GTPases in disease development. Gene 286, 155-174 (2002).
    • (2002) Gene , vol.286 , pp. 155-174
    • Boettner, B.1    Van Aelst, L.2
  • 45
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.