The assembly of a GTPase–kinase signalling complex by a bacterial catalytic scaffold (original) (raw)

• Scott, J. D. & Pawson, T. Cell signaling in space and time: where proteins come together and when they’re apart. Science 326, 1220–1224 (2009)
  Article ADS CAS Google Scholar
• Lim, W. A. Designing customized cell signalling circuits. Nature Rev. Mol. Cell Biol. 11, 393–403 (2010)
  Article CAS Google Scholar
• Duesbery, N. S. et al. Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor. Science 280, 734–737 (1998)
  Article ADS CAS Google Scholar
• Yarbrough, M. L. et al. AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science 323, 269–272 (2009)
  Article CAS Google Scholar
• Schmidt, G. et al. Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1. Nature 387, 725–729 (1997)
  Article ADS CAS Google Scholar
• Li, H. et al. The phosphothreonine lyase activity of a bacterial type III effector family. Science 315, 1000–1003 (2007)
  Article ADS CAS Google Scholar
• Alto, N. M. et al. The type III effector EspF coordinates membrane trafficking by the spatiotemporal activation of two eukaryotic signaling pathways. J. Cell Biol. 178, 1265–1278 (2007)
  Article CAS Google Scholar
• Vingadassalom, D. et al. Insulin receptor tyrosine kinase substrate links the E. coli O157:H7 actin assembly effectors Tir and EspFU during pedestal formation. Proc. Natl Acad. Sci. USA 106, 6754–6759 (2009)
  Article ADS CAS Google Scholar
• Rivera, V. M. et al. Regulation of protein secretion through controlled aggregation in the endoplasmic reticulum. Science 287, 826–830 (2000)
  Article ADS CAS Google Scholar
• Winnen, B. et al. Hierarchical effector protein transport by the Salmonella Typhimurium SPI-1 type III secretion system. PLoS ONE 3, e2178 (2008)
  Article ADS Google Scholar
• Shaw, R. K. et al. Enteropathogenic Escherichia coli type III effectors EspG and EspG2 disrupt the microtubule network of intestinal epithelial cells. Infect. Immun. 73, 4385–4390 (2005)
  Article CAS Google Scholar
• Tomson, F. L. et al. Enteropathogenic Escherichia coli EspG disrupts microtubules and in conjunction with Orf3 enhances perturbation of the tight junction barrier. Mol. Microbiol. 56, 447–464 (2005)
  Article CAS Google Scholar
• Yoshida, S. et al. Microtubule-severing activity of Shigella is pivotal for intercellular spreading. Science 314, 985–989 (2006)
  Article ADS CAS Google Scholar
• Germane, K. L., Ohi, R., Goldberg, M. B. & Spiller, B. W. Structural and functional studies indicate that Shigella VirA is not a protease and does not directly destabilize microtubules. Biochemistry 47, 10241–10243 (2008)
  Article CAS Google Scholar
• Davis, J. et al. Novel fold of VirA, a type III secretion system effector protein from Shigella flexneri . Protein Sci. 17, 2167–2173 (2008)
  Article CAS Google Scholar
• Kahn, R. A. Toward a model for Arf GTPases as regulators of traffic at the Golgi. FEBS Lett. 583, 3872–3879 (2009)
  Article CAS Google Scholar
• D’Souza-Schorey, C. & Chavrier, P. ARF proteins: roles in membrane traffic and beyond. Nature Rev. Mol. Cell Biol. 7, 347–358 (2006)
  Article Google Scholar
• Bokoch, G. M. Biology of the p21-activated kinases. Annu. Rev. Biochem. 72, 743–781 (2003)
  Article CAS Google Scholar
• Borthakur, A. et al. Enteropathogenic Escherichia coli inhibits butyrate uptake in Caco-2 cells by altering the apical membrane MCT1 level. Am. J. Physiol. Gastrointest. Liver Physiol. 290, G30–G35 (2006)
  Article CAS Google Scholar
• Guttman, J. A. et al. Aquaporins contribute to diarrhoea caused by attaching and effacing bacterial pathogens. Cell. Microbiol. 9, 131–141 (2007)
  Article CAS Google Scholar
• Pasqualato, S., Menetrey, J., Franco, M. & Cherfils, J. The structural GDP/GTP cycle of human Arf6. EMBO Rep. 2, 234–238 (2001)
  Article CAS Google Scholar
• Hanzal-Bayer, M., Renault, L., Roversi, P., Wittinghofer, A. & Hillig, R. C. The complex of Arl2-GTP and PDE delta: from structure to function. EMBO J. 21, 2095–2106 (2002)
  Article CAS Google Scholar
• Isabet, T. et al. The structural basis of Arf effector specificity: the crystal structure of ARF6 in a complex with JIP4. EMBO J. 28, 2835–2845 (2009)
  Article CAS Google Scholar
• O’Neal, C. J., Jobling, M. G., Holmes, R. K. & Hol, W. G. Structural basis for the activation of cholera toxin by human ARF6-GTP. Science 309, 1093–1096 (2005)
  Article ADS Google Scholar
• Shiba, T. et al. Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport. Nature Struct. Biol. 10, 386–393 (2003)
  Article CAS Google Scholar
• Zhao, L. et al. Direct and GTP-dependent interaction of ADP ribosylation factor 1 with coatomer subunit beta. Proc. Natl Acad. Sci. USA 94, 4418–4423 (1997)
  Article ADS CAS Google Scholar
• Chardin, P. & McCormick, F. Brefeldin A: the advantage of being uncompetitive. Cell 97, 153–155 (1999)
  Article CAS Google Scholar
• Lei, M. et al. Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. Cell 102, 387–397 (2000)
  Article CAS Google Scholar
• Bremser, M. et al. Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors. Cell 96, 495–506 (1999)
  Article CAS Google Scholar
• Goldberg, J. Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Cell 96, 893–902 (1999)
  Article CAS Google Scholar
• Minor, W., Cymborowski, M., Otwinowski, Z. & Chruszcz, M. HKL-3000: the integration of data reduction and structure solution–from diffraction images to an initial model in minutes. Acta Crystallogr. D 62, 859–866 (2006)
  Article Google Scholar
• Schneider, T. R. & Sheldrick, G. M. Substructure solution with SHELXD. Acta Crystallogr. D 58, 1772–1779 (2002)
  Article Google Scholar
• Cowtan, K. & Main, P. Miscellaneous algorithms for density modification. Acta Crystallogr. D 54, 487–493 (1998)
  Article CAS Google Scholar
• Terwilliger, T. SOLVE and RESOLVE: automated structure solution, density modification and model building. J. Synchrotron Radiat. 11, 49–52 (2004)
  Article CAS Google Scholar
• Cowtan, K. The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr. D 62, 1002–1011 (2006)
  Article Google Scholar
• McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658–674 (2007)
  Article CAS Google Scholar
• 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)
• Adams, P. D. et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D 58, 1948–1954 (2002)
  Article Google Scholar
• Davis, I. W. et al. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35, W375–W383 (2007)
  Article ADS Google Scholar