Changes in structural dynamics of the Grb2 adaptor protein upon binding of phosphotyrosine ligand to its SH2 domain

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1700, Issue 1, 2004, Pages 53-64

  De Mol, Nico J ^a   Catalina, M Isabel ^b   Fischer, Marcel J E ^a   Broutin, Isabelle ^c   Maier, Claudia S ^b   Heck, Albert J R ^b  

^a UTRECHT UNIVERSITY   (Netherlands)

^b UTRECHT UNIVERSITY   (Netherlands)

^c UNIVERSITÉ PARIS DESCARTES   (France)

Author keywords

Binding kinetics; electrospray ionization mass spectrometry; ESI MS; Grb2; growth factor receptor bound protein 2 (Q13588); H D mass spectrometry; m z; mass to charge ratio; Protein structural dynamics; SH2; SPR; Surface plasmon resonance

Indexed keywords

ADAPTOR PROTEIN; DEUTERIUM; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; HYDROGEN; PHOSPHOPEPTIDE; PHOSPHOTYROSINE; PROTEIN SH2; PROTEIN SHC;

AMINO ACID SEQUENCE; ARTICLE; ELECTROSPRAY MASS SPECTROMETRY; KINETICS; MEASUREMENT; MOLECULAR DYNAMICS; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN ISOLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SURFACE PLASMON RESONANCE;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ADAPTOR PROTEINS, VESICULAR TRANSPORT; AMINO ACID SEQUENCE; ANIMALS; DEUTERIUM EXCHANGE MEASUREMENT; GRB2 ADAPTOR PROTEIN; KINETICS; LIGANDS; MICE; PEPTIDE FRAGMENTS; PHOSPHOTYROSINE; PROTEIN BINDING; PROTEINS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SRC HOMOLOGY DOMAINS; SURFACE PLASMON RESONANCE;

EID: 2942733237     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2004.03.016     Document Type: Article

References (40)

1. Lim W.A. The modular logic of signaling proteins: building allosteric switches from simple binding domains. Curr. Opin. Struct. Biol. 12:2002;61-68
2. Songyang Z., Shoelson S.E., McGlade J., Olivier P., Pawson T., Bustelo X.R., Barbacid M., Sabe H., Hanafusa H., Yi T., et al. Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav. Mol. Cell Biol. 14:1994;2777-2785
3. Garbay C., Liu W.Q., Vidal M., Roques B.P. Inhibitors of Ras signal transduction as antitumor agents. Biochem. Pharmacol. 60:2000;1165-1169
4. Koretzky G.A. The Role of Grb2-Associated Proteins in T-Cell activation. Immunol. Today. 18:1997;401-406
5. Turner H., Reif K., Rivera J., Cantrell D.A. Regulation of the adapter molecule Grb2 by the Fc-Epsilon-R1 in the Mast-Cell Line Rbl2H3. J. Biol. Chem. 270:1995;9500-9506
6. Vihinen M., Smith C.I.E. Structural aspects of signal-transduction in B-Cells. Crit. Rev. Immunol. 16:1996;251-275
7. Schlaepfer D.D., Hanks S.K., Hunter T., van der Geer P. Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature. 372:1994;786-791
8. Buday L. Membrane-targeting of signalling molecules by SH2/SH3 domain containing adaptor proteins. Biochim. Biophys. Acta. 1422:1999;187-204
9. Jordan M.S., Singer A.L., Koretzky G.A. Adaptors as central mediators of signal transduction in immune cells. Nat. Immunol. 4:2003;110-116
10. Yuzawa S., Yokochi M., Hatanaka H., Ogura K., Kataoka M., Miura K., Mandiyan V., Schlessinger J., Inagaki F. Solution structure of Grb2 reveals extensive flexibility necessary for target recognition. J. Mol. Biol. 306:2001;527-537
11. Maignan S., Guilloteau J.P., Fromage N., Arnoux B., Becquart J., Ducruix A. Crystal structure of the mammalian Grb2 adaptor. Science. 268:1995;291-293
12. Nioche P., Liu W.Q., Broutin I., Charbonnier F., Latreille M.T., Vidal M., Roques B., Garbay C., Ducruix A. Crystal structures of the SH2 domain of Grb2: highlight on the binding of a new high-affinity inhibitor. J. Mol. Biol. 315:2002;1167-1177
13. Morton T.A., Myszka D.G. Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors. Methods Enzymol. 295:1998;268-294
14. Myszka D.G., Morton T.A. Clamp(C) - A biosensor kinetic data-analysis program. Trends Biochem. Sci. 23:1998;149-150
15. de Mol N.J., Plomp E., Fischer M.J.E., Ruijtenbeek R. Kinetic analysis of the mass transport limited interaction between the tyrosine kinase lck SH2 domain and a phosphorylated peptide studied by a new cuvette-based surface plasmon resonance instrument. Anal. Biochem. 279:2000;61-70
16. Felder S., Zhou M., Hu P., Urena J., Ullrich A., Chaudhuri M., White M., Shoelson S.E., Schlessinger J. SH2 domains exhibit high-affinity binding to tyrosinephosphorylated peptides yet also exhibit rapid dissociation and exchange. Mol. Cell Biol. 13:1993;1449-1455
17. Schuck P. Kinetics of ligand-binding to receptor immobilized in a polymer matrix, as detected with an evanescent-wave biosensor. 1. A computer-simulation of the influence of mass-transport. Biophys. J. 70:1996;1230-1249
18. Schiering N., Casale E., Caccia P., Giordano P., Battistini C. Dimer formation through domain swapping in the crystal structure of the Grb2-SH2-Ac-pYVNV complex. Biochemistry. 39:2000;13376-13382
19. Catalina M.I., de Mol N.J., Fischer M.J.E., Heck A.J.R. Probing factors affecting the gas phase stabilities of noncovalent complexes formed by peptides bound to the Grb2 SH2 domain protein. Phys. Chem. Chem. Phys. 6:2004;2572-2579
20. Anderegg R., Wagner D. Mass spectrometric characterization of protein-ligand interaction. J. Am. Chem. Soc. 117:1995;1374-1377
21. van den Bremer E.T.J., Jiskoot W., James R., Moore G.R., Kleanthous C., Heck A.J.R., Maier C.S. Probing metal ion binding and conformational properties of the colicin E9 endonuclease by electrospray ionization time-of-flight mass spectrometry. Protein Sci. 11:2002;1738-1752
22. Miranker A., Robinson C.V., Radford S.E., Aplin R.T., Dobson C.M. Detection of transient protein folding populations by mass spectrometry. Science. 262:1993;896-900
23. Wagner M.L., Yan D.S., Erickson B.W., Anderegg R.J. Deuterium exchange of alphahelices and beta-sheets as monitored by electrospray ionization mass spectrometry. Protein Sci. 3:1994;1305-1314
24. Mohimen A., Dobo A., Hoerner J.K., Kaltashov I.A. A chemometric approach to detection and characterization of multiple protein conformers in solution using electrospray ionization mass spectrometry. Anal. Chem. 75:2003;4139-4147
25. Konermann L., Douglas D.J. Equilibrium unfolding of proteins monitored by electrospray ionization mass spectrometry: distinguishing two-state from multi-state transitions. Rapid Commun. Mass Spectrom. 12:1998;435-442
26. Yan X., Watson J., Ho P., Deinzer M. Mass spectrometric approaches using electrospray ionization charge States and hydrogen-deuterium exchange for determining protein structures and their conformational changes. Mol. Cell Proteomics. 3:2004;10-23
27. Engen G.W. Jr., Smithgall T.E., Smith D.L. Hydrogen exchange shows peptide binding stabilizes motions in Hck SH2. Biochemistry. 38:1999;8926-8935
28. Farrow N.A., Muhandiram R., Singer A.U., Pascal S.M., Kay C.M., Gish G., Shoelson S.E., Pawson T., Forman-Kay J.D., Kay L.E. Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation. Biochemistry. 33:1994;5984-6003
29. Shoelson S.E., Sivaraja M., Williams K.P., Hu P., Schlessinger J., Weiss M.A. Specific phosphopeptide binding regulates a conformational change in the PI 3-kinase SH2 domain associated with enzyme activation. EMBO J. 12:1993;795-802
30. Breeze A.L., Kara B.V., Barratt D.G., Anderson M., Smith J.C., Luke R.W., Best J.R., Cartlidge S.A. Structure of a specific peptide complex of the carboxy-terminal Sh2 domain from the P85-alpha subunit of phosphatidylinositol 3-kinase. EMBO J. 15:1996;3579-3589
31. de Mol N.J., Fischer M.J.E. Applications of surface plasmon resonance (SPR). Ligand-Receptor Binding Studies: Affinity, Kinetics and Thermodynamics. vol. 3:2003;Transworld Research Network, Trivandrum, India
32. Waksman G., Shoelson S.E., Pant N., Cowburn D., Kuriyan J. Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell. 72:1993;779-790
33. Rahuel J., Gay B., Erdmann D., Strauss A., Garciaecheverria C., Furet P., Caravatti G., Fretz H., Schoepfer J., Grutter M.G. Structural basis for specificity of Grb2-Sh2 revealed by a novel ligand-binding mode. Nat. Struct. Biol. 3:1996;586-589
34. Cussac D., Frech M., Chardin P. Binding of the Grb2 SH2 domain to phosphotyrosine motifs does not change the affinity of its SH3 domains for Sos proline-rich motifs. EMBO J. 13:1994;4011-4021
35. Lemmon M.A., Ladbury J.E., Mandiyan V., Zhou M., Schlessinger J. Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2. J. Biol. Chem. 269:1994;31653-31658
36. Cussac D., Vidal M., Leprince C., Liu W.Q., Cornille F., Tiraboschi G., Roques B.P., Garbay C. A Sos-derived peptidimer blocks the Ras signaling pathway by binding both Grb2 SH3 domains and displays antiproliferative activity. FASEB J. 13:1999;31-38
37. Chook Y.M., Gish G.D., Kay C.M., Pai E.F., Pawson T. The Grb2-mSos1 complex binds phosphopeptides with higher affinity than Grb2. J. Biol. Chem. 271:1996;30472-30478
38. Guan K.L., Dixon J.E. Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal. Biochem. 192:1991;262-267
39. Guilloteau J.P., Fromage N., Rieskautt M., Reboul S., Bocquet D., Dubois H., Faucher D., Colonna C., Ducruix A., Becquart J. Purification, stabilization, and crystallization of a modular protein: Grb2. Proteins: Struct. Funct. Genet. 25:1996;112-119
40. Lauffenburger D.A., Linderman J.J. Receptors: Models for Binding, Trafficking, and Signalling. 1993;Oxford Univ. Press, Oxford