Protein-protein interaction affinity plays a crucial role in controlling the Sho1p-mediated signal transduction pathway in yeast

Molecular Cell

Volumn 14, Issue 6, 2004, Pages 813-823

  Marles, Jennifer A ^a   Dahesh, Samira ^a   Haynes, Jennifer ^a   Andrews, Brenda J ^a   Davidson, Alan R ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCEROL; MITOGEN ACTIVATED PROTEIN KINASE KINASE; MUTANT PROTEIN; PHEROMONE; PROTEIN; PROTEIN SHO1P; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING KINETICS; ENERGY; NONHUMAN; OSMOLARITY; PROTEIN DOMAIN; PROTEIN ENGINEERING; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; BINDING SITES; CONSERVED SEQUENCE; MAP KINASE SIGNALING SYSTEM; MEMBRANE PROTEINS; MITOGEN-ACTIVATED PROTEIN KINASES; MOLECULAR SEQUENCE DATA; MUTATION; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SRC HOMOLOGY DOMAINS;

EID: 2942648435     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.05.024     Document Type: Article

References (44)

1. Block C., Janknecht R., Herrmann C., Nassar N., Wittinghofer A. Quantitative structure-activity analysis correlating Ras/Raf interaction in vitro to Raf activation in vivo. Nat. Struct. Biol. 3:1996;244-251
2. Brewster J.L., de Valoir T., Dwyer N.D., Winter E., Gustin M.C. An osmosensing signal transduction pathway in yeast. Science. 259:1993;1760-1763
3. Chan B., Lanyi A., Song H.K., Griesbach J., Simarro-Grande M., Poy F., Howie D., Sumegi J., Terhorst C., Eck M.J. SAP couples Fyn to SLAM immune receptors. Nat. Cell Biol. 5:2003;155-160
4. Cullen P.J., Schultz J., Horecka J., Stevenson B.J., Jigami Y., Sprague G.F. Jr. Defects in protein glycosylation cause SHO1-dependent activation of a STE12 signaling pathway in yeast. Genetics. 155:2000;1005-1018
5. Dalgarno D.C., Botfield M.C., Rickles R.J. SH3 domains and drug design. ligands, structure, and biological function Biopolymers. 43:1997;383-400
6. Douangamath A., Filipp F.V., Klein A.T., Barnett P., Zou P., Voorn-Brouwer T., Vega M.C., Mayans O.M., Sattler M., Distel B., et al. Topography for independent binding of alpha-helical and PPII-helical ligands to a peroxisomal SH3 domain. Mol. Cell. 10:2002;1007-1017
7. Evans S.V. Setor. hardware-lighted three-dimensional solid model representations of macromolecules J. Mol. Graph. 11:1993;134-138
8. Feng S., Chen J.K., Yu H., Simon J.A., Schreiber S.L. Two binding orientations for peptides to the Src SH3 domain. development of a general model for SH3-ligand interactions Science. 266:1994;1241-1247
9. Gavin A.C., Bosche M., Krause R., Grandi P., Marzioch M., Bauer A., Schultz J., Rick J.M., Michon A.M., Cruciat C.M., et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature. 415:2002;141-147
10. Giot L., Bader J.S., Brouwer C., Chaudhuri A., Kuang B., Li Y., Hao Y.L., Ooi C.E., Godwin B., Vitols E., et al. A protein interaction map of Drosophila melanogaster. Science. 302:2003;1727-1736
11. Harris K., Lamson R.E., Nelson B., Hughes T.R., Marton M.J., Roberts C.J., Boone C., Pryciak P.M. Role of scaffolds in MAP kinase pathway specificity revealed by custom design of pathway-dedicated signaling proteins. Curr. Biol. 11:2001;1815-1824
12. Ho Y., Gruhler A., Heilbut A., Bader G.D., Moore L., Adams S.L., Millar A., Taylor P., Bennett K., Boutilier K., et al. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature. 415:2002;180-183
13. Ito T., Chiba T., Ozawa R., Yoshida M., Hattori M., Sakaki Y. A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc. Natl. Acad. Sci. USA. 98:2001;4569-4574
14. Larson S.M., Davidson A.R. The identification of conserved interactions within the SH3 domain by alignment of sequences and structures. Protein Sci. 9:2000;2170-2180
15. Lim W.A., Richards F.M., Fox R.O. Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature. 372:1994;375-379
16. Maeda T., Wurgler-Murphy S.M., Saito H. A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature. 369:1994;242-245
17. Maeda T., Takekawa M., Saito H. Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor. Science. 269:1995;554-558
18. Maxwell K.L., Davidson A.R. Mutagenesis of a buried polar interaction in an SH3 domain. sequence conservation provides the best prediction of stability effects Biochemistry. 37:1998;16172-16182
19. Mayer B.J., Eck M.J. SH3 domains. Minding your p's and q's. Curr. Biol. 5:1995;364-367
20. Musacchio A., Saraste M., Wilmanns M. High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides. Nat. Struct. Biol. 1:1994;546-551
21. Nishida M., Nagata K., Hachimori Y., Horiuchi M., Ogura K., Mandiyan V., Schlessinger J., Inagaki F. Novel recognition mode between Vav and Grb2 SH3 domains. EMBO J. 20:2001;2995-3007
22. O'Rourke S.M., Herskowitz I. The Hog1 MAPK prevents cross talk between the HOG and pheromone response MAPK pathways in Saccharomyces cerevisiae. Genes Dev. 12:1998;2874-2886
23. O'Rourke S.M., Herskowitz I. A third osmosensing branch in Saccharomyces cerevisiae requires the Msb2 protein and functions in parallel with the Sho1 branch. Mol. Cell. Biol. 22:2002;4739-4749
24. O'Rourke S.M., Herskowitz I., O'Shea E.K. Yeast go the whole HOG for the hyperosmotic response. Trends Genet. 18:2002;405-412
25. Ota I.M., Varshavsky A. A yeast protein similar to bacterial two-component regulators. Science. 262:1993;566-569
26. Pace C.N., Vajdos F., Fee L., Grimsley G., Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4:1995;2411-2423
27. Pawson T., Scott J.D. Signaling through scaffold, anchoring, and adaptor proteins. Science. 278:1997;2075-2080
28. Pearce K.H. Jr., Cunningham B.C., Fuh G., Teeri T., Wells J.A. Growth hormone binding affinity for its receptor surpasses the requirements for cellular activity. Biochemistry. 38:1999;81-89
29. Piehler J., Roisman L.C., Schreiber G. New structural and functional aspects of the type I interferon-receptor interaction revealed by comprehensive mutational analysis of the binding interface. J. Biol. Chem. 275:2000;40425-40433
30. Posas F., Saito H. Osmotic activation of the HOG MAPK pathway via Ste11p MAPKKK. scaffold role of Pbs2p MAPKK Science. 276:1997;1702-1705
31. Posas F., Witten E.A., Saito H. Requirement of STE50 for osmostress-induced activation of the STE11 mitogen-activated protein kinase kinase kinase in the high-osmolarity glycerol response pathway. Mol. Cell. Biol. 18:1998;5788-5796
32. Raitt D.C., Posas F., Saito H. Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent activation of the Hog1 MAPK pathway. EMBO J. 19:2000;4623-4631
33. Reiser V., Salah S.M., Ammerer G. Polarized localization of yeast Pbs2 depends on osmostress, the membrane protein Sho1 and Cdc42. Nat. Cell Biol. 2:2000;620-627
34. Rickles R.J., Botfield M.C., Zhou X.M., Henry P.A., Brugge J.S., Zoller M.J. Phage display selection of ligand residues important for Src homology 3 domain binding specificity. Proc. Natl. Acad. Sci. USA. 92:1995;10909-10913
35. Roberts C.J., Nelson B., Marton M.J., Stoughton R., Meyer M.R., Bennett H.A., He Y.D., Dai H., Walker W.L., Hughes T.R., et al. Signaling and circuitry of multiple MAPK pathways revealed by a matrix of global gene expression profiles. Science. 287:2000;873-880
36. Sikorski R.S., Hieter P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:1989;19-27
37. Tong A.H., Drees B., Nardelli G., Bader G.D., Brannetti B., Castagnoli L., Evangelista M., Ferracuti S., Nelson B., Paoluzi S., et al. A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules. Science. 295:2002;321-324
38. Toone W.M., Jones N. Stress-activated signalling pathways in yeast. Genes Cells. 3:1998;485-498
39. Uetz P., Giot L., Cagney G., Mansfield T.A., Judson R.S., Knight J.R., Lockshon D., Narayan V., Srinivasan M., Pochart P., et al. A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature. 403:2000;623-627
40. Warner F.J., Miller R.C., Burcher E. Structure-activity relationship of neurokinin A(4-10) at the human tachykinin NK(2) receptor. the effect of amino acid substitutions on receptor affinity and function Biochem. Pharmacol. 63:2002;2181-2186
41. Waskiewicz A.J., Cooper J.A. Mitogen and stress response pathways. MAP kinase cascades and phosphatase regulation in mammals and yeast Curr. Opin. Cell Biol. 7:1995;798-805
42. Wu X., Knudsen B., Feller S.M., Zheng J., Sali A., Cowburn D., Hanafusa H., Kuriyan J. Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk. Structure. 3:1995;215-226
43. Zarrinpar A., Park S.H., Lim W.A. Optimization of specificity in a cellular protein interaction network by negative selection. Nature. 426:2003;676-680
44. Zhu Z., Hattori K., Zhang H., Jimenez X., Ludwig D.L., Dias S., Kussie P., Koo H., Kim H.J., Lu D., et al. Inhibition of human leukemia in an animal model with human antibodies directed against vascular endothelial growth factor receptor 2. Correlation between antibody affinity and biological activity. Leukemia. 17:2003;604-611