메뉴 건너뛰기




Volumn 392, Issue 6671, 1998, Pages 101-105

Structure of the Sec 7 domain of the Arf exchange factor ARNO

Author keywords

[No Author keywords available]

Indexed keywords

CYTOHESIN 1; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; UNCLASSIFIED DRUG; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 1; CYTOHESIN 2; CYTOHESIN-2; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; PROTEIN; RECOMBINANT PROTEIN; SEC7 GUANINE NUCLEOTIDE EXCHANGE FACTORS;

EID: 0032485074     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/32210     Document Type: Article
Times cited : (154)

References (30)
  • 1
    • 0029294676 scopus 로고
    • Guanine nucleotide exchange factors: Activators of the Ras superfamily of proteins
    • Quilliam, L. A., Khosravi-Far, R., Huff, S. Y., Solski, P. A. & Der, C. J. Guanine nucleotide exchange factors: activators of the Ras superfamily of proteins. Bioessays 17, 395-404 (1995).
    • (1995) Bioessays , vol.17 , pp. 395-404
    • Quilliam, L.A.1    Khosravi-Far, R.2    Huff, S.Y.3    Solski, P.A.4    Der, C.J.5
  • 2
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Scheckman, R. & Orci, L. Coat proteins and vesicle budding. Sciece 271, 1526-1533 (1996).
    • (1996) Sciece , vol.271 , pp. 1526-1533
    • Scheckman, R.1    Orci, L.2
  • 3
    • 0029844904 scopus 로고    scopus 로고
    • A human exchange factor for ARF contains Scc7- And pleckstrin-homology domains
    • Chardin, P. et al. A human exchange factor for ARF contains Scc7- and pleckstrin-homology domains. Nature 384, 481-484 (1996).
    • (1996) Nature , vol.384 , pp. 481-484
    • Chardin, P.1
  • 4
    • 0031041536 scopus 로고    scopus 로고
    • Cytuhesin-1, a cytosolic guanine nucleotide-exchange protein for ADP-ribosyiation factor
    • Meacci, E., Tsai, S. C., Adamik, R., Moss, J. & Vaughan, M. Cytuhesin-1, a cytosolic guanine nucleotide-exchange protein for ADP-ribosyiation factor. Proc. Natl Acad. Sci. 94, 1745-1748 (1997).
    • (1997) Proc. Natl Acad. Sci. , vol.94 , pp. 1745-1748
    • Meacci, E.1    Tsai, S.C.2    Adamik, R.3    Moss, J.4    Vaughan, M.5
  • 5
    • 0030975196 scopus 로고    scopus 로고
    • Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 liomology domains
    • Klarlund, J. K. et al. Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 liomology domains. Science 275, 1927-1930 (1997).
    • (1997) Science , vol.275 , pp. 1927-1930
    • Klarlund, J.K.1
  • 6
    • 0019424489 scopus 로고
    • Orders of events in the yeast secretory pathway
    • Novick, P., Ferro, S. & Schekman, R. Orders of events in the yeast secretory pathway. Cell 25, 461-469 (1981).
    • (1981) Cell , vol.25 , pp. 461-469
    • Novick, P.1    Ferro, S.2    Schekman, R.3
  • 7
    • 0029851773 scopus 로고    scopus 로고
    • Nucleotide exchange on ARF mediated by yeast Geal protein
    • Peyroche, A., Paris, S. & Jackson, C. L. Nucleotide exchange on ARF mediated by yeast Geal protein. Nature 384, 479-481 (1996).
    • (1996) Nature , vol.384 , pp. 479-481
    • Peyroche, A.1    Paris, S.2    Jackson, C.L.3
  • 8
    • 0028322046 scopus 로고
    • EMB30 is essential for normal cell division, cell expansion, and cell adhesion in Arabidopsis and encodes a protein that has similarity to Sec7
    • Shevell, D. E. et al. EMB30 is essential for normal cell division, cell expansion, and cell adhesion in Arabidopsis and encodes a protein that has similarity to Sec7. Cell77, 1051-1062 (1994).
    • (1994) Cell , vol.77 , pp. 1051-1062
    • Shevell, D.E.1
  • 9
    • 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, 12926-12931 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12926-12931
    • Morinaga, N.1    Moss, J.2    Vaughan, M.3
  • 10
    • 0030800831 scopus 로고    scopus 로고
    • Three-dimensional structure of the Armadillo repeat of β-catenin
    • Huber, A. H., Nelson, J. & Wies, W. I. Three-dimensional structure of the Armadillo repeat of β-catenin. Cell 90, 871-882 (1997).
    • (1997) Cell , vol.90 , pp. 871-882
    • Huber, A.H.1    Nelson, J.2    Wies, W.I.3
  • 11
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 Å resolution
    • Kawashima, T., Berthet-Colominas, C., Wulff, M., Cusack, S. & Leberman, R. The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 Å resolution. Nature 379, 511-518 (1996).
    • (1996) Nature , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet-Colominas, C.2    Wulff, M.3    Cusack, S.4    Leberman, R.5
  • 13
    • 0029099915 scopus 로고
    • Structure of guanine-nucleotidc-exchange factor human Mss4 and identification of its Rab-interacting surface
    • Yu, H. & Schreiber, S. L. Structure of guanine-nucleotidc-exchange factor human Mss4 and identification of its Rab-interacting surface, Nature 376, 788-791 (1995).
    • (1995) Nature , vol.376 , pp. 788-791
    • Yu, H.1    Schreiber, S.L.2
  • 14
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison, C. J., Hayer-Hartl, M., Di Liberto, M., Hartl, F. U. & Kuriyan, J. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276, 431-435 (1997).
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.U.4    Kuriyan, J.5
  • 15
    • 0032485075 scopus 로고    scopus 로고
    • The 1.7 Å crystal structure of the regulator of chromosome condonation (RCC1) reveals a seven-bladed propeller
    • Renault, L. et al. The 1.7 Å crystal structure of the regulator of chromosome condonation (RCC1) reveals a seven-bladed propeller. Nature 392, 97-101 (1998).
    • (1998) Nature , vol.392 , pp. 97-101
    • Renault, L.1
  • 16
    • 0030772378 scopus 로고    scopus 로고
    • The ras-rasGAP complex: Structural basis for GTPase activation and its loss in oncogenic mutants
    • Scheffzek, K. et al. The ras-rasGAP complex: structural basis for GTPase activation and its loss in oncogenic mutants, Science 277, 333-338 (1997).
    • (1997) Science , vol.277 , pp. 333-338
    • Scheffzek, K.1
  • 17
    • 0030716497 scopus 로고    scopus 로고
    • Structure at 1.65 Å of RhoA and its GTPasep-activating protein in complex with a transition-state analog
    • Rittinger, K., Walker, P. A., Eccleston, J. F., Smerdon, S. J. & Gunblin, S. J. Structure at 1.65 Å of RhoA and its GTPasep-activating protein in complex with a transition-state analog. Nature 389, 758-762 (1997).
    • (1997) Nature , vol.389 , pp. 758-762
    • Rittinger, K.1    Walker, P.A.2    Eccleston, J.F.3    Smerdon, S.J.4    Gunblin, S.J.5
  • 18
    • 1842416568 scopus 로고    scopus 로고
    • Role of protein-phospholipid interactions in the activation of ARF1 by the guanine nucleotide exchange factor Arno
    • Paris, S. et al. Role of protein-phospholipid interactions in the activation of ARF1 by the guanine nucleotide exchange factor Arno. J. Biol Chem, 272, 22221-22226 (1997).
    • (1997) J. Biol Chem , vol.272 , pp. 22221-22226
    • Paris, S.1
  • 19
    • 0028980920 scopus 로고
    • Characterization of a mammalian C-CDC25Mm exchange factor and kinetic properties of the exchange reaction intermediate p21.C-CDC25Mra
    • Jacquet, E., Baouz, S. & Parmeggiani, A. Characterization of a mammalian C-CDC25Mm exchange factor and kinetic properties of the exchange reaction intermediate p21.C-CDC25Mra. Biochemisrry 34, 12347-12354 (1995).
    • (1995) Biochemisrry , vol.34 , pp. 12347-12354
    • Jacquet, E.1    Baouz, S.2    Parmeggiani, A.3
  • 20
    • 0026628881 scopus 로고
    • RAS residues that are distant form the GDP binding site play a critical role in dissociation factor-stimulated release of GDP
    • Verroti, A. C. et al. RAS residues that are distant form the GDP binding site play a critical role in dissociation factor-stimulated release of GDP. EMBO J, 11, 2855-2862 (1992).
    • (1992) EMBO J , vol.11 , pp. 2855-2862
    • Verroti, A.C.1
  • 21
    • 0027175224 scopus 로고
    • Residues crucial for Ras interaction with GDP-GTPexchangers
    • Segal, M., Willumsen, B. & Levitzk, A. Residues crucial for Ras interaction with GDP-GTPexchangers. Proc. Natl Acad. Sci. USA 90, 5564-5568 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5564-5568
    • Segal, M.1    Willumsen, B.2    Levitzk, A.3
  • 22
    • 0030891289 scopus 로고    scopus 로고
    • N-terminal hydrophobic residues of the G- Protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTF exchange
    • Antonny, B., Béraud-Dufour, S., Chardin, P. & Chabre, M. N-terminal hydrophobic residues of the G- protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTF exchange. Biochemistry 36, 4675-4684 (1997).
    • (1997) Biochemistry , vol.36 , pp. 4675-4684
    • Antonny, B.1    Béraud-Dufour, S.2    Chardin, P.3    Chabre, M.4
  • 24
    • 0028556994 scopus 로고
    • Structure of the human ADP-ribosylation factor 1 complexed with GDP
    • Amor, J. C., Harrison, D, H., Kahn, R. A. & Ringe, D, Structure of the human ADP-ribosylation factor 1 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
  • 26
    • 0029944499 scopus 로고    scopus 로고
    • Structure and mutational analysis of Rab GDP-dissociation inhibitor
    • Schalk, I. et al. Structure and mutational analysis of Rab GDP-dissociation inhibitor. Nature. 381, 42-48 (1996).
    • (1996) Nature , vol.381 , pp. 42-48
    • Schalk, I.1
  • 27
    • 0031570337 scopus 로고    scopus 로고
    • A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm
    • Keep, N. H. et al. A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm. Structure 5, 623-633 (1997).
    • (1997) Structure , vol.5 , pp. 623-633
    • Keep, N.H.1
  • 28
    • 0030602819 scopus 로고    scopus 로고
    • αLβ2 integrin/LFA-1 binding to ICAM-1 induced by cytohain-1, a cytoplasmic regulatory molecule
    • Kolanus, W. et al. αLβ2 integrin/LFA-1 binding to ICAM-1 induced by cytohain-1, a cytoplasmic regulatory molecule. Cell 86, 233-242 (1996).
    • (1996) Cell , vol.86 , pp. 233-242
    • Kolanus, W.1
  • 29
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No. 4
    • Collaborative Computational Project No. 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 30
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likeliwood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • De la Fortelle, E. & Bricogne, G. Maximum-likeliwood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol 276, 472-494 (1997).
    • (1997) Methods Enzymol , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.