Structure of the Human Receptor Tyrosine Kinase Met in Complex with the Listeria Invasion Protein InlB

Cell

Volumn 130, Issue 2, 2007, Pages 235-246

  Niemann, Hartmut H ^a   Jäger, Volker ^a   Butler, P Jonathan G ^b   van den Heuvel, Joop ^a   Schmidt, Sabine ^a   Ferraris, Davide ^a   Gherardi, Ermanno ^b   Heinz, Dirk W ^a  

^a HELMHOLTZ CENTRE FOR INFECTION RESEARCH   (Germany)

^b MEDICAL RESEARCH COUNCIL   (United Kingdom)

Author keywords

CELLBIO; HUMDISEASE; SIGNALING

Indexed keywords

BACTERIAL PROTEIN; HEPARIN; LEUCINE; MEMBRANE PROTEIN; PROTEIN INIB; PROTEIN TYROSINE KINASE; SCATTER FACTOR; SCATTER FACTOR RECEPTOR; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL VIRULENCE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CELL FUNCTION; CELL INVASION; CELL MIGRATION; CELL SURVIVAL; COMPLEX FORMATION; CRYSTAL STRUCTURE; DIMERIZATION; HOST CELL; HUMAN; LISTERIA MONOCYTOGENES; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTO ONCOGENE; SIGNAL TRANSDUCTION;

LISTERIA; LISTERIA MONOCYTOGENES;

EID: 34447548559     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2007.05.037     Document Type: Article

References (51)

1. Adams P.D., Gopal K., Grosse-Kunstleve R.W., Hung L.W., Ioerger T.R., McCoy A.J., Moriarty N.W., Pai R.K., Read R.J., Romo T.D., et al. Recent developments in the PHENIX software for automated crystallographic structure determination. J. Synchrotron Radiat. 11 (2004) 53-55
2. Baker N.A., Sept D., Joseph S., Holst M.J., and McCammon J.A. Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl. Acad. Sci. USA 98 (2001) 10037-10041
3. Banerjee M., Copp J., Vuga D., Marino M., Chapman T., van der Geer P., and Ghosh P. GW domains of the Listeria monocytogenes invasion protein InlB are required for potentiation of Met activation. Mol. Microbiol. 52 (2004) 257-271
4. Bierne H., and Cossart P. InlB, a surface protein of Listeria monocytogenes that behaves as an invasin and a growth factor. J. Cell Sci. 115 (2002) 3357-3367
5. Birchmeier C., Birchmeier W., Gherardi E., and Vande Woude G.F. Met, metastasis, motility and more. Nat. Rev. Mol. Cell Biol. 4 (2003) 915-925
6. Braun L., Dramsi S., Dehoux P., Bierne H., Lindahl G., and Cossart P. InlB: an invasion protein of Listeria monocytogenes with a novel type of surface association. Mol. Microbiol. 25 (1997) 285-294
7. Braun L., Ohayon H., and Cossart P. The InIB protein of Listeria monocytogenes is sufficient to promote entry into mammalian cells. Mol. Microbiol. 27 (1998) 1077-1087
8. Braun L., Nato F., Payrastre B., Mazie J.C., and Cossart P. The 213-amino-acid leucine-rich repeat region of the Listeria monocytogenes InlB protein is sufficient for entry into mammalian cells, stimulation of PI 3-kinase and membrane ruffling. Mol. Microbiol. 34 (1999) 10-23
9. Braun L., Ghebrehiwet B., and Cossart P. gC1q-R/p32, a C1q-binding protein, is a receptor for the InlB invasion protein of Listeria monocytogenes. EMBO J. 19 (2000) 1458-1466
10. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S., et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54 (1998) 905-921
11. DeLano W.L. The PyMOL Molecular Graphics System. DeLano Scientific LLC. http://www.pymol.org
12. Dramsi S., Biswas I., Maguin E., Braun L., Mastroeni P., and Cossart P. Entry of Listeria monocytogenes into hepatocytes requires expression of inIB, a surface protein of the internalin multigene family. Mol. Microbiol. 16 (1995) 251-261
13. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 2126-2132
14. Gaillard J.L., Berche P., Frehel C., Gouin E., and Cossart P. Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from gram-positive cocci. Cell 65 (1991) 1127-1141
15. Galan J.E. Alternative strategies for becoming an insider: lessons from the bacterial world. Cell 103 (2000) 363-366
16. Gherardi E., Youles M.E., Miguel R.N., Blundell T.L., Iamele L., Gough J., Bandyopadhyay A., Hartmann G., and Butler P.J. Functional map and domain structure of MET, the product of the c-met protooncogene and receptor for hepatocyte growth factor/scatter factor. Proc. Natl. Acad. Sci. USA 100 (2003) 12039-12044
17. Gherardi E., Sandin S., Petoukhov M.V., Finch J., Youles M.E., Ofverstedt L.G., Miguel R.N., Blundell T.L., Vande Woude G.F., Skoglund U., et al. Structural basis of hepatocyte growth factor/scatter factor and MET signalling. Proc. Natl. Acad. Sci. USA 103 (2006) 4046-4051
18. Hamon M., Bierne H., and Cossart P. Listeria monocytogenes: a multifaceted model. Nat. Rev. Microbiol. 4 (2006) 423-434
19. Hayes D.B., Laue T., and Philo J. RASMB software archive (2006). http://www.rasmb.bbri.org/rasmb/windows/sednterp-philo/sdtr0601.exe
20. Hayward S., and Berendsen H.J. Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme. Proteins 30 (1998) 144-154
21. Holmes O., Pillozzi S., Deakin J.A., Carafoli F., Kemp L., Butler P.J., Lyon M., and Gherardi E. Insights into the Structure/Function of Hepatocyte Growth Factor/Scatter Factor from Studies with Individual Domains. J. Mol. Biol. 367 (2007) 395-408
22. Hubbard S.R., and Till J.H. Protein tyrosine kinase structure and function. Annu. Rev. Biochem. 69 (2000) 373-398
23. Ireton K., Payrastre B., and Cossart P. The Listeria monocytogenes protein InlB is an agonist of mammalian phosphoinositide 3-kinase. J. Biol. Chem. 274 (1999) 17025-17032
24. Jonquieres R., Bierne H., Fiedler F., Gounon P., and Cossart P. Interaction between the protein InlB of Listeria monocytogenes and lipoteichoic acid: a novel mechanism of protein association at the surface of gram-positive bacteria. Mol. Microbiol. 34 (1999) 902-914
25. Jonquieres R., Pizarro-Cerda J., and Cossart P. Synergy between the N- and C-terminal domains of InlB for efficient invasion of non-phagocytic cells by Listeria monocytogenes. Mol. Microbiol. 42 (2001) 955-965
26. Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26 (1993) 795-800
27. Kong-Beltran M., Stamos J., and Wickramasinghe D. The Sema domain of Met is necessary for receptor dimerization and activation. Cancer Cell 6 (2004) 75-84
28. Krissinel E., and Henrick K. Detection of protein assemblies in crystals. In: Berthold M.R. (Ed). CompLife (2005), Springer-Verlag, Berlin Heidelberg 163-174
29. Laue T.M., Shah B.D., Ridgeway T.M., and Pelletier S.L. Computer-aided interpretation of analytical sedimentation data for proteins. In: Harding S.E., Rowe A.J., and Horton J.C. (Eds). Analytical Ultracentrifugation in Biochemistry and Polymer Science (1992), Royal Society of Chemistry, Cambridge, UK 90-125
30. Lecuit M., Vandormael-Pournin S., Lefort J., Huerre M., Gounon P., Dupuy C., Babinet C., and Cossart P. A transgenic model for listeriosis: role of internalin in crossing the intestinal barrier. Science 292 (2001) 1722-1725
31. Machner M.P., Frese S., Schubert W.D., Orian-Rousseau V., Gherardi E., Wehland J., Niemann H.H., and Heinz D.W. Aromatic amino acids at the surface of InlB are essential for host cell invasion by Listeria monocytogenes. Mol. Microbiol. 48 (2003) 1525-1536
32. Majeed S., Ofek G., Belachew A., Huang C.C., Zhou T., and Kwong P.D. Enhancing protein crystallization through precipitant synergy. Structure 11 (2003) 1061-1070
33. Marino M., Braun L., Cossart P., and Ghosh P. Structure of the lnlB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen L. monocytogenes. Mol. Cell 4 (1999) 1063-1072
34. Marino M., Banerjee M., Jonquieres R., Cossart P., and Ghosh P. GW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands. EMBO J. 21 (2002) 5623-5634
35. McCoy A.J., Grosse-Kunstleve R.W., Storoni L.C., and Read R.J. Likelihood-enhanced fast translation functions. Acta Crystallogr. D Biol. Crystallogr. 61 (2005) 458-464
36. Mengaud J., Ohayon H., Gounon P., Mege R.M., and Cossart P. E-cadherin is the receptor for internalin, a surface protein required for entry of L. monocytogenes into epithelial cells. Cell 84 (1996) 923-932
37. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53 (1997) 240-255
38. Parida S.K., Domann E., Rohde M., Muller S., Darji A., Hain T., Wehland J., and Chakraborty T. Internalin B is essential for adhesion and mediates the invasion of Listeria monocytogenes into human endothelial cells. Mol. Microbiol. 28 (1998) 81-93
39. Pentecost M., Otto G., Theriot J.A., and Amieva M.R. Listeria monocytogenes invades the epithelial junctions at sites of cell extrusion. PLoS Pathog. 2 (2006) e3 10.1371/journal.ppat.0020003
40. Philo J.S. Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques. Anal. Biochem. 354 (2006) 238-246
41. Prat M., Crepaldi T., Pennacchietti S., Bussolino F., and Comoglio P.M. Agonistic monoclonal antibodies against the Met receptor dissect the biological responses to HGF. J. Cell Sci. 111 (1998) 237-247
42. Rubin J.S., Day R.M., Breckenridge D., Atabey N., Taylor W.G., Stahl S.J., Wingfield P.T., Kaufman J.D., Schwall R., and Bottaro D.P. Dissociation of heparan sulfate and receptor binding domains of hepatocyte growth factor reveals that heparan sulfate-c-met interaction facilitates signaling. J. Biol. Chem. 276 (2001) 32977-32983
43. Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 103 (2000) 211-225
44. Schubert W.D., and Heinz D.W. Structural aspects of adhesion to and invasion of host cells by the human pathogen Listeria monocytogenes. ChemBioChem 4 (2003) 1285-1291
45. Schubert W.D., Gobel G., Diepholz M., Darji A., Kloer D., Hain T., Chakraborty T., Wehland J., Domann E., and Heinz D.W. Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain. J. Mol. Biol. 312 (2001) 783-794
46. Schubert W.D., Urbanke C., Ziehm T., Beier V., Machner M.P., Domann E., Wehland J., Chakraborty T., and Heinz D.W. Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin. Cell 111 (2002) 825-836
47. Shen Y., Naujokas M., Park M., and Ireton K. InIB-dependent internalization of Listeria is mediated by the Met receptor tyrosine kinase. Cell 103 (2000) 501-510
48. Stamos J., Lazarus R.A., Yao X., Kirchhofer D., and Wiesmann C. Crystal structure of the HGF beta chain in complex with the Sema domain of the Met receptor. EMBO J. 23 (2004) 2325-2335
49. Stanley P. Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycoproteins with minimal carbohydrate heterogeneity. Mol. Cell. Biol. 9 (1989) 377-383
50. Stebbins C.E., and Galan J.E. Structural mimicry in bacterial virulence. Nature 412 (2001) 701-705
51. Stoker M., Gherardi E., Perryman M., and Gray J. Scatter factor is a fibroblast-derived modulator of epithelial cell mobility. Nature 327 (1987) 239-242