GTP-Ras Disrupts the Intramolecular Complex of C1 and RA Domains of Nore1

Structure

Volumn 14, Issue 5, 2006, Pages 881-888

  Harjes, Elena ^a,b   Harjes, Stefan ^a,b   Wohlgemuth, Sabine ^a   Müller, Karl Heinz ^a,b   Krieger, Elmar ^d   Herrmann, Christian ^c   Bayer, Peter ^a,b  

^a MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

^b Interdisciplinary Center of Magnetic Resonance (IZMR)   (Germany)

^c RUHR UNIVERSITY BOCHUM   (Germany)

^d RADBOUD UNIVERSITY NIJMEGEN   (Netherlands)

Author keywords

CELLCYCLE; SIGNALING

Indexed keywords

GUANOSINE TRIPHOSPHATE; LIPID BINDING PROTEIN; MIDOSTAURIN; PHOSPHATIDYLINOSITOL 3 PHOSPHATE; PROTEIN; PROTEIN NORE1; RAP1 PROTEIN; RAS PROTEIN; UNCLASSIFIED DRUG;

APOPTOSIS; ARTICLE; ATOM; BINDING AFFINITY; CALORIMETRY; COMPLEX FORMATION; EVIDENCE BASED PRACTICE; ISOTHERM; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SEQUENCE HOMOLOGY; SOLUTION AND SOLUBILITY;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID SEQUENCE; ANIMALS; LIPIDS; MICE; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHATIDYLINOSITOL PHOSPHATES; PROTEIN CONFORMATION; PROTEIN INTERACTION MAPPING; PROTEIN STRUCTURE, TERTIARY; RAP1 GTP-BINDING PROTEINS; RAS PROTEINS;

EID: 33646363331     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2006.03.008     Document Type: Article

References (38)

1. Aoyama Y., Avruch J., and Zhang X. Nore1 inhibits tumor cell growth independent of Ras or the MST1/2 kinases. Oncogene 23 (2004) 3426-3433
2. Bateman A., Coin L., Durbin R., Finn R., Hollich V., Griffiths-Jones S., Khanna A., Marshall M., Moxon S., Sonnhammer E., et al. The pfam protein families database. Nucleic Acids Res. 32 (2004) D138-D141
3. Brunger A. X-PLOR version 3.1: a system for X-ray crystallography and NMR (1992), Yale University Press, New Haven, CT
4. 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
5. Chen H., Legault P., Glushka J., Omichinski G., and Scott R. Structure of a Cys3His zinc ribbon, a ubiquitous motif in archaeal and eucaryal transription. Protein Sci. 9 (2000) 1743-1752
6. Cox A., and Der C. The dark side of Ras: regulation of apoptosis. Oncogene 22 (2003) 8999-9006
7. Cutler Jr. R., Stephens R., Saracino M., and Morrision D. Autoregulation of the Raf-1 serine/threonine kinase. Proc. Natl. Acad. Sci. USA 95 (1998) 9214-9219
8. Dumas J., Merithew E., Sudharshan E., Rajamani D., Hayes S., Lawe D., Corvera S., and Lambright D. Multivalent endosome targeting by homodimeric EEA1. Mol. Cell 8 (2001) 947-958
9. Essman U., Perera L., Berkowitz M., Darden T., Lee H., and Pedersen L. A smooth particle mesh ewald method. J. Chem. Phys. 103 (1995) 8577-8593
10. Feig L., and Buchsbaum R. Cell signaling: life or death decisions of Ras proteins. Curr. Biol. 12 (2002) R259-R261
11. Gillooly D., Morrow I., Lindsay M., Gould R., Bryant N., Gaullier J.-M., Parton R., and Stenmark H. Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells. EMBO J. 19 (2000) 4577-4588
12. Gronwald W., Huber F., Grünewald P., Spörner M., Wohlgemuth S., Herrmann C., and Kalbitzer H. Solution structure of the Ras binding domain of the protein kinase Byr2 from Schizosaccharomyces pombe. Structure 9 (2001) 1029-1041
13. Guex N., and Peitsch M. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
14. Herrmann C., Horn G., Spaargaren M., and Wittinghofer A. Differential interaction of the Ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Ras kinase and Ral-guanine nucleotide exchange factor. J. Biol. Chem. 271 (1996) 6794-6800
15. Holm L., and Sander C. Protein structure comparison by alignment of distance matices. J. Mol. Biol. 233 (1993) 123-138
16. Hu C.-D., Kariya K.-I., Tamada M., Akasaka K., Shirouzu M., Yokoyama S., and Kataoka T. Cysteine-rich region of Raf-1 interacts with activator domain of posttranslationnally modified Ha-Ras. J. Biol. Chem. 270 (1995) 30274-30277
17. Hurley J., and Misra S. Signaling and subcellular targeting by membrane-binding domain. Annu. Rev. Biophys. Biomol. Struct. 29 (2000) 50-79
18. Jung J., and Lee B. Protein structure alignment using environmental profiles. Protein Eng. 13 (2000) 535-543
19. 15N inverse detected heteronuclear NMR spectroscopy: application to staphyloccal nuclase. Biochemistry 28 (1989) 8972-8979
20. Khokhlatchev A., Rabizadeh S., Xavier R., Nedwidek M., Chen T., Zhang X., Seed B., and Avruch J. Identification of a novel Ras-regulated proapoptotic pathway. Curr. Biol. 12 (2002) 253-265
21. Koradi R., Billeter M., and Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55
22. Krieger, E. (2003). YASARA (www.yasara.org/sd).
23. Krieger E., Koraimann G., and Vriend G. Increasing the precision of comparative models with YASARA NOVA -a self-parameterizing force field. Proteins 47 (2002) 393-402
24. Krieger E., Darden T., Nabuurs S., Finkelstein A., and Vriend G. Making optimal use of empirical energy functions: force field parameterization in crystal space. Proteins 57 (2004) 678-683
25. Kuszewski J., and Clore G. Source of and solutions to problems in the refinement of protein NMR structures against torsion angle potentials of mean force. J. Magn. Reson. 146 (2000) 249-254
26. Laskowski R., MacArthur M., and Thornton D.M.J. Procheck: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26 (1993) 283-291
27. Lenzen C., Cool R., and Wittinghofer A. Analysis of intrinsic and CDC25-stimulated guanine nucleotide exchange of p21ras-nucleotide complex by fluorescence measurements. Methods Enzymol. 255 (1995) 95-105
28. Medkova M., and Cho W. Interplay of C1 and C2 domains of protein kinase C-α in its membrane binding and activation. J. Biol. Chem. 274 (1999) 19852-19861
29. Misra S., and Hurley J. Crystal structure of a phosphatidylinositol 3-phosphatespecific membrane-targeting motif, the FYVE domain of Vsp27p. Cell 97 (1999) 657-666
30. Mott H., Carpenter J., Zhong S., Ghosh S., Bell M., and Campbell S. The solution structure of the Raf-1 cysteine-rich domain: a novel Ras and phospholipid binding site. Proc. Natl. Acad. Sci. USA 93 (1996) 8312-8317
31. Ortiz-Vega S., Khokhlatchev A., Nedwidek M., Zhang X., Dammann R., Pfeifer G., and Avruch J. The putative tumor supressor RASSF1A homodimerizes and heterodimerizes with the Ras-GTP binding protein Nore1. Oncogene 21 (2002) 1381-1390
32. Praskova M., Khoklatchev A., Ortiz-Vega S., and Avruch J. Regulation of the MST1 kinase by autophosphorylation, by the inhibitory proteins, RASSF1 and NORE1, and by ras. Biochem. J. 381 (2004) 453-462
33. Radziwill G., Erdmann R.A., Margelisch U., and Moelling K. The Bcr kinase downregulates Ras signaling by phosphorylating AF-6 and binding to its PDZ domain. Mol. Cell. Biol. 23 (2003) 4663-4672
34. Shields J., Pruitt K., McFall A., Shaub A., and Der C. Understanding Ras: 'it ain't over 'til it's over.'. Trends Cell Biol. 10 (2000) 147-154
35. Vavvas D., Li X., Avruch J., and Zhang X. Identification of Nore1 as a potential Ras effector. J. Biol. Chem. 273 (1998) 5439-5442
36. Xu R., Pawelczyk T., Xia T.-H., and Brown S. NMR structure of a protein kinase c-phorbol-binding domain and study of protein-lipid micelle interactions. Biochemistry 36 (1997) 10709-10717
37. Yau W.-M., Wimley W., Gawrisch K., and White S. The preference of tryptophan for membrane interfaces. Biochemistry 37 (1998) 14713-14718
38. Zhang G., Kayanietz M., Blumberg P., and Hurley J. Crystal structure of the Cys2 activator-binding domain of protein kinase Cδ in complex with phorbol ester. Cell 81 (1995) 917-924