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Volumn 288, Issue 7, 2013, Pages 4659-4672

Kinetics of interaction between ADP-ribosylation factor-1 (Arf1) and the Sec7 domain of arno guanine nucleotide exchange factor, modulation by allosteric factors, and the uncompetitive inhibitor brefeldin A

Author keywords

[No Author keywords available]

Indexed keywords

ADP-RIBOSYLATION; BREFELDIN A; DISSOCIATION RATES; DOMAIN COMPLEXES; GUANINE NUCLEOTIDE EXCHANGE FACTORS; INHIBITORY MECHANISM; INTERACTING SPECIES;

EID: 84874098165     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.391748     Document Type: Article
Times cited : (9)

References (53)
  • 1
    • 84859967413 scopus 로고    scopus 로고
    • The ras protein superfamily. Evolutionary tree and role of conserved amino acids
    • Rojas, A. M., Fuentes, G., Rausell, A., and Valencia, A. (2012) The Ras protein superfamily. Evolutionary tree and role of conserved amino acids. J. Cell Biol. 196, 189-201
    • (2012) J. Cell Biol. , vol.196 , pp. 189-201
    • Rojas, A.M.1    Fuentes, G.2    Rausell, A.3    Valencia, A.4
  • 2
  • 3
    • 79952092131 scopus 로고    scopus 로고
    • Multiple roles for RhoA during T cell transendothelial migration
    • Heasman, S.J., and Ridley, A.J. (2010) Multiple roles for RhoA during T cell transendothelial migration. Small GTPases 1, 174-179
    • (2010) Small GTPases , vol.1 , pp. 174-179
    • Heasman, S.J.1    Ridley, A.J.2
  • 4
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian rho GTPases. New insights into their functions from in vivo studies
    • Heasman, S. J., and Ridley, A. J. (2008) Mammalian Rho GTPases. New insights into their functions from in vivo studies. Nat Rev. Mol. Cell Biol. 9, 690-701
    • (2008) Nat Rev. Mol. Cell Biol. , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 5
    • 78649487698 scopus 로고    scopus 로고
    • Ras superfamily GEFs and GAPs. Validated and tractable targets for cancer therapy?
    • Vigil, D., Cherfils, J., Rossman, K. L., and Der, C. J. (2010) Ras superfamily GEFs and GAPs. Validated and tractable targets for cancer therapy? Nat. Rev. Cancer 10, 842-857
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 842-857
    • Vigil, D.1    Cherfils, J.2    Rossman, K.L.3    Der, C.J.4
  • 6
    • 13444252631 scopus 로고    scopus 로고
    • GEF means go. Turning on RHO GTPases with guanine nucleotide-exchange factors
    • Rossman, K. L., and Der., C. J., and Sondek, J. (2005) GEF means go. Turning on RHO GTPases with guanine nucleotide-exchange factors. Nat. Rev. Mol. Cell Biol. 6, 167-180
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 167-180
    • Rossman, K.L.1    Der, C.J.2    Sondek, J.3
  • 7
    • 0028801195 scopus 로고
    • The kinetic mechanism of ran-nucleotide exchange catalyzed by RCC1
    • Klebe, C., Prinz, H., Wittinghofer, A., and Goody, R. S. (1995) The kinetic mechanism of Ran-nucleotide exchange catalyzed by RCC1. Biochemistry 34, 12543-12552
    • (1995) Biochemistry , vol.34 , pp. 12543-12552
    • Klebe, C.1    Prinz, H.2    Wittinghofer, A.3    Goody, R.S.4
  • 8
    • 28244456271 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors operate by a simple allosteric competitive mechanism
    • Guo, Z., and Ahmadian., M. R., and Goody, R. S. (2005) Guanine nucleotide exchange factors operate by a simple allosteric competitive mechanism. Biochemistry 44, 15423-15429
    • (2005) Biochemistry , vol.44 , pp. 15423-15429
    • Guo, Z.1    Ahmadian, M.R.2    Goody, R.S.3
  • 9
    • 0036656168 scopus 로고    scopus 로고
    • Exchange factors, effectors, GAPs and motor proteins. Common thermodynamic and kinetic principles for different functions
    • Goody, R. S., and Hofmann-Goody, W. (2002) Exchange factors, effectors, GAPs and motor proteins. Common thermodynamic and kinetic principles for different functions. Eur. Biophys. J. 31, 268-274
    • (2002) Eur. Biophys. J. , vol.31 , pp. 268-274
    • Goody, R.S.1    Hofmann-Goody, W.2
  • 12
    • 0034682668 scopus 로고    scopus 로고
    • 2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of rho family GTP-binding proteins
    • 2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins. J. Biol. Chem. 275, 25299-25307
    • (2000) J. Biol. Chem. , vol.275 , pp. 25299-25307
    • Zhang, B.1    Zhang, Y.2    Wang, Z.3    Zheng, Y.4
  • 15
    • 35348884249 scopus 로고    scopus 로고
    • Regulation of arf activation. The sec7 family of guanine nucleotide exchange factors
    • Casanova, J. E. (2007) Regulation of Arf activation. The Sec7 family of guanine nucleotide exchange factors. Traffic 8, 1476-1485
    • (2007) Traffic , vol.8 , pp. 1476-1485
    • Casanova, J.E.1
  • 16
    • 79957473559 scopus 로고    scopus 로고
    • ARF family G proteins and their regulators. Roles in membrane transport, development and disease
    • Donaldson, J. G., and Jackson, C. L. (2011) ARF family G proteins and their regulators. Roles in membrane transport, development and disease. Nat. Rev. Mol. Cell Biol. 12, 362-375
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 362-375
    • Donaldson, J.G.1    Jackson, C.L.2
  • 17
    • 80052545798 scopus 로고    scopus 로고
    • ARF1 controls proliferation of breast cancer cells by regulating the retinoblastoma protein
    • Boulay, P. L., Schlienger, S., Lewis-Saravalli, S., Vitale, N, Ferbeyre, G., and Claing, A. (2011) ARF1 controls proliferation of breast cancer cells by regulating the retinoblastoma protein. Oncogene 30, 3846-3861
    • (2011) Oncogene , vol.30 , pp. 3846-3861
    • Boulay, P.L.1    Schlienger, S.2    Lewis-Saravalli, S.3    Vitale, N.4    Ferbeyre, G.5    Claing, A.6
  • 18
    • 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
  • 20
    • 34447335816 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors of the cytohesin family and their roles in signal transduction
    • Kolanus, W. (2007) Guanine nucleotide exchange factors of the cytohesin family and their roles in signal transduction. Immunol. Rev. 218, 102-113
    • (2007) Immunol. Rev. , vol.218 , pp. 102-113
    • Kolanus, W.1
  • 21
    • 0028556994 scopus 로고
    • Structure of the human ADP-ribosylation factor 1 complexed with GDP
    • Amor, J. C, Harrison, D.H., Kahn, R. A., and Ringe, D. (1994) Structure of the human ADP-ribosylation factor 1 complexed with GDP. Nature 372, 704-708
    • (1994) Nature , vol.372 , pp. 704-708
    • Amor, J.C.1    Harrison, D.H.2    Kahn, R.A.3    Ringe, D.4
  • 22
    • 0029113233 scopus 로고
    • The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms
    • Greasley, S. E., Jhoti, H, Teahan, C, Solari, R., Fensome, A., Thomas, G. M., Cockcroft, S., and Bax, B. (1995) The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms. Nat Struct. Biol. 2, 797-806
    • (1995) Nat Struct. Biol. , vol.2 , pp. 797-806
    • Greasley, S.E.1    Jhoti, H.2    Teahan, C.3    Solari, R.4    Fensome, A.5    Thomas, G.M.6    Cockcroft, S.7    Bax, B.8
  • 25
    • 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
  • 26
    • 0346243924 scopus 로고    scopus 로고
    • Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor
    • Renault, L., Guibert, B., and Cherfils, J. (2003) Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor. Nature 426, 525-530
    • (2003) Nature , vol.426 , pp. 525-530
    • Renault, L.1    Guibert, B.2    Cherfils, J.3
  • 27
    • 14644420930 scopus 로고    scopus 로고
    • Interfacial inhibition of macromolecular interactions. Nature's paradigm for drug discovery
    • Pommier, Y., and Cherfils, J. (2005) Interfacial inhibition of macromolecular interactions. Nature's paradigm for drug discovery. Trends Pharmacol. Sci. 26, 138-145
    • (2005) Trends Pharmacol. Sci. , vol.26 , pp. 138-145
    • Pommier, Y.1    Cherfils, J.2
  • 28
    • 2342434546 scopus 로고    scopus 로고
    • Conformational states of the small G protein arf-1 in complex with the guanine nucleotide exchange factor ARNO-sec7
    • Kremer, W., Steiner, G., Béraud-Dufour, S., and Kalbitzer, H. R. (2004) Conformational states of the small G protein Arf-1 in complex with the guanine nucleotide exchange factor ARNO-Sec7. J. Biol. Chem. 279, 17004-17012
    • (2004) J. Biol. Chem. , vol.279 , pp. 17004-17012
    • Kremer, W.1    Steiner, G.2    Béraud-Dufour, S.3    Kalbitzer, H.R.4
  • 30
    • 0032520638 scopus 로고    scopus 로고
    • A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in escherichia coli
    • Smith, P. A., Tripp, B. C, DiBlasio-Smith, E. A., Lu, Z., LaVallie, E. R., and McCoy, J. M. (1998) A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in Escherichia coli. Nucleic Acids Res. 26, 1414-1420
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1414-1420
    • Smith, P.A.1    Tripp, B.C.2    DiBlasio-Smith, E.A.3    Lu, Z.4    LaVallie, E.R.5    McCoy, J.M.6
  • 31
    • 0032924825 scopus 로고    scopus 로고
    • BirA enzyme. Production and application in the study of membrane receptor-ligand interactions by site-specific biotinylation
    • O'callaghan C. A., Byford, M. F., Wyer, J. R., Willcox, B. E., Jakobsen, B. K., McMichael, A. J., and Bell, J. I. (1999) BirA enzyme. Production and application in the study of membrane receptor-ligand interactions by site-specific biotinylation. Anal. Biochem. 266, 9-15
    • (1999) Anal. Biochem. , vol.266 , pp. 9-15
    • O'callaghan, C.A.1    Byford, M.F.2    Wyer, J.R.3    Willcox, B.E.4    Jakobsen, B.K.5    McMichael, A.J.6    Bell, J.I.7
  • 32
    • 33744964615 scopus 로고    scopus 로고
    • Dual specificity of the interfacial inhibitor brefeldin A for arf proteins and sec7 domains
    • Zeeh, J. C, Zeghouf, M., Grauffel, C, Guibert, B., Martin, E., Dejaegere, A., and Cherfils, J. (2006) Dual specificity of the interfacial inhibitor brefeldin A for arf proteins and sec7 domains. J. Biol. Chem. 281, 11805-11814
    • (2006) J. Biol. Chem. , vol.281 , pp. 11805-11814
    • Zeeh, J.C.1    Zeghouf, M.2    Grauffel, C.3    Guibert, B.4    Martin, E.5    Dejaegere, A.6    Cherfils, J.7
  • 33
    • 39049110605 scopus 로고    scopus 로고
    • Expression and characterization of recombinant C-terminal biotinylated extracellular domain of human receptor for advanced glycation end products (hsRAGE) in escherichia coli
    • Kumano-Kuramochi, M., Xie, Q., Sakakibara, Y., Niimi, S., Sekizawa, K., Komba, S., and Machida, S. (2008) Expression and characterization of recombinant C-terminal biotinylated extracellular domain of human receptor for advanced glycation end products (hsRAGE) in Escherichia coli. J. Biochem. 143, 229-236
    • (2008) J. Biochem. , vol.143 , pp. 229-236
    • Kumano-Kuramochi, M.1    Xie, Q.2    Sakakibara, Y.3    Niimi, S.4    Sekizawa, K.5    Komba, S.6    Machida, S.7
  • 34
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • Beckett, D., Kovaleva, E., and Schatz, P. J. (1999) A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Sci. 8, 921-929
    • (1999) Protein Sci. , vol.8 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 37
    • 14044276363 scopus 로고    scopus 로고
    • Mechanism of the guanine nucleotide exchange reaction of ras GTPase. Evidence for a GTP/ GDP displacement model
    • Zhang, B., Zhang, Y., Shacter, E., and Zheng, Y. (2005) Mechanism of the guanine nucleotide exchange reaction of Ras GTPase. Evidence for a GTP/ GDP displacement model. Biochemistry 44, 2566-2576
    • (2005) Biochemistry , vol.44 , pp. 2566-2576
    • Zhang, B.1    Zhang, Y.2    Shacter, E.3    Zheng, Y.4
  • 38
    • 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. U. S.A. 97, 9913-9918
    • (2000) Proc. Natl. Acad. Sci. U. S.A. , vol.97 , pp. 9913-9918
    • Robineau, S.1    Chabre, M.2    Antonny, B.3
  • 39
    • 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
  • 40
    • 77953356593 scopus 로고    scopus 로고
    • Exploring minimal biotinylation conditions for biosensor analysis using capture chips
    • Papalia, G, and Myszka, D. (2010) Exploring minimal biotinylation conditions for biosensor analysis using capture chips. Anal. Biochem. 403, 30-35
    • (2010) Anal. Biochem. , vol.403 , pp. 30-35
    • Papalia, G.1    Myszka, D.2
  • 41
    • 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
  • 42
    • 0348047597 scopus 로고    scopus 로고
    • *Sec7 complexed with brefeldin A and its implications for the guanine nucleotide exchange mechanism
    • *Sec7 complexed with Brefeldin A and its implications for the guanine nucleotide exchange mechanism. Mol. Cell 12, 1403-1411
    • (2003) Mol. Cell , vol.12 , pp. 1403-1411
    • Mossessova, E.1    Corpina, R.A.2    Goldberg, J.3
  • 43
    • 1842416568 scopus 로고    scopus 로고
    • Role of protein-phospholipid interactions in the activation of ARF1 by the guanine nucleotide exchange factor arno
    • Paris, S., Béraud-Dufour, S., Robineau, S., Bigay, J., Antonny, B., Chabre, M., and Chardin, P. (1997) Role of protein-phospholipid interactions in the activation of ARF1 by the guanine nucleotide exchange factor Arno. J. Biol. Chem. 272, 22221-22226
    • (1997) J. Biol. Chem. , vol.272 , pp. 22221-22226
    • Paris, S.1    Béraud-Dufour, S.2    Robineau, S.3    Bigay, J.4    Antonny, B.5    Chabre, M.6    Chardin, P.7
  • 44
    • 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, and Cool., R. H., Prinz, H., Kuhlmann, J., and Wittinghofer, A. (1998) 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) Biochemistry , vol.37 , pp. 7420-7430
    • Lenzen, C.1    Cool, R.H.2    Prinz, H.3    Kuhlmann, J.4    Wittinghofer, A.5
  • 46
    • 79960194927 scopus 로고    scopus 로고
    • Interconversion of two GDP-bound conformations and their selection in an arf-family small G protein
    • Okamura, H., Nishikiori, M., Xiang, H, Ishikawa, M., and Katoh, E. (2011) Interconversion of two GDP-bound conformations and their selection in an Arf-family small G protein. Structure 19, 988-998
    • (2011) Structure , vol.19 , pp. 988-998
    • Okamura, H.1    Nishikiori, M.2    Xiang, H.3    Ishikawa, M.4    Katoh, E.5
  • 47
    • 84863793694 scopus 로고    scopus 로고
    • The pleckstrin homology (PH) domain of the arf exchange factor brag2 is an allos-teric binding site
    • Jian, X., and Gruschus., J. M., Sztul, E., and Randazzo, P. A. (2012) The pleckstrin homology (PH) domain of the Arf exchange factor Brag2 is an allos-teric binding site. J. Biol. Chem. 287, 24273-24283
    • (2012) J. Biol. Chem. , vol.287 , pp. 24273-24283
    • Jian, X.1    Gruschus, J.M.2    Sztul, E.3    Randazzo, P.A.4
  • 48
    • 0020709919 scopus 로고
    • Kinetic studies of adenosine kinase from L1210 cells. A model enzyme with a two-site ping-pong mechanism
    • Chang, C. H, Cha, S., Brockman, R. W., and Bennett, L. L., Jr. (1983) Kinetic studies of adenosine kinase from L1210 cells. A model enzyme with a two-site ping-pong mechanism. Biochemistry 22, 600-611
    • (1983) Biochemistry , vol.22 , pp. 600-611
    • Chang, C.H.1    Cha, S.2    Brockman, R.W.3    Bennett Jr., L.L.4
  • 49
    • 79952781379 scopus 로고    scopus 로고
    • Kinetic studies of the arf activator arno on model membranes in the presence of arf effectors suggest control by a positive feedback loop
    • Stalder, D., Barelli, H., Gautier, R., Macia, E., and Jackson., C. L., and Antonny, B. (2011) Kinetic studies of the Arf activator Arno on model membranes in the presence of Arf effectors suggest control by a positive feedback loop. J. Biol. Chem. 286, 3873-3883
    • (2011) J. Biol. Chem. , vol.286 , pp. 3873-3883
    • Stalder, D.1    Barelli, H.2    Gautier, R.3    Macia, E.4    Jackson, C.L.5    Antonny, B.6
  • 53


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