Molecular basis of the complex formation between the two calcium-binding proteins S100A8 (MRP8) and S100A9 (MRP14)

Biological Chemistry

Volumn 386, Issue 5, 2005, Pages 429-434

  Leukert, Nadja ^a   Sorg, Clemens ^a   Roth, Johannes ^a  

^a UNIVERSITY OF MÜNSTER   (Germany)

Author keywords

Heterodimerization; Homodimerization; Myeloid related proteins (MRP); S100 proteins; Site directed mutagenesis; Yeast two hybrid

Indexed keywords

CALCIUM BINDING PROTEIN; MYELOID RELATED PROTEIN 14; MYELOID RELATED PROTEIN 8; PROTEIN S100A8; PROTEIN S100A9; UNCLASSIFIED DRUG;

ARTICLE; COMPLEX FORMATION; DIMERIZATION; HUMAN; HYDROPHOBICITY; IN VIVO STUDY; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN LOCALIZATION; SIGNAL TRANSDUCTION; TWO HYBRID SYSTEM; YEAST;

CALGRANULIN A; CALGRANULIN B; DIMERIZATION; HUMANS; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; TWO-HYBRID SYSTEM TECHNIQUES;

EID: 26844553337     PISSN: 14316730     EISSN: 14316730     Source Type: Journal    
DOI: 10.1515/BC.2005.051     Document Type: Article

References (33)

1. Brodersen, D.E., Etzerodt, M., Madsen, P., Celis, J.E., Thogersen, H.C., Nyborg, J., and Kjeldgaard, M. (1998). EF-hands at atomic resolution: the structure of human psoriasin (S100A7) solved by MAD phasing. Structure 6, 477-489.
2. Cornish, C.J., Devery, J.M., Poronnik, P., Lackmann, M., Cook, D.I., and Geczy, C.L. (1996). S100 protein CP-10 stimulates myeloid cell chemotaxis without activation. J. Cell Physiol. 166, 427-437.
3. Deloulme, J.C., Assard, N., Mbele, G.O., Mangin, C., Kuwano, R., and Baudier, J. (2000). S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo. J. Biol. Chem. 275, 35302-35310.
4. Donato, R. (2001). S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles. Int. J. Biochem. Cell Biol. 33, 637-668.
5. Drohat, A.C., Baldisseri, D.M., Rustandi, R.R., and Weber, D.J. (1998). Solution structure of calcium-bound rat S100B(ββ) as determined by nuclear magnetic resonance spectroscopy. Biochemistry 37, 2729-2740.
6. Foell, D., Frosch, M., Sorg, C., and Roth, J. (2004). Phagocytespecific calcium-binding S100 proteins as clinical laboratory markers of inflammation. Clin. Chim. Acta 344, 37-51.
7. Fritz, G., Mittl, P.R., Vasak, M., Grutter, M.G., and Heizmann, C.W. (2002). The crystal structure of metal-free human EFhand protein S100A3 at 1.7-Å resolution. J. Biol. Chem. 277, 33092-33098.
8. Gietz, D., St Jean, A., Woods, R.A., and Schiestl, R.H. (1992). Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20, 1425.
9. Heizmann, C.W., Fritz, G., and Schafer, B.W. (2002). S100 proteins: structure, functions and pathology. Front. Biosci. 7, d1356-d1368.
10. Hunter, M.J. and Chazin, W.J. (1998). High level expression and dimer characterization of the S100 EF-hand proteins, migration inhibitory factor-related proteins 8 and 14. J. Biol. Chem. 273, 12427-12435.
11. Ishikawa, K., Nakagawa, A., Tanaka, I., Suzuki, M., and Nishihira, J. (2000). The structure of human MRP8, a member of the S100 calcium-binding protein family, by MAD phasing at 1.9 Å resolution. Acta Crystallogr. D Biol. Crystallogr. 56, 559-566.
12. 2+-dependent regulator protein in inflammatory process. J. Mol. Biol. 316, 265-276.
13. Kilby, P.M., Van Eldik, L.J., and Roberts, G.C. (1996). The solution structure of the bovine S100B protein dimer in the calcium-free state. Structure 4, 1041-1052.
14. Koltzscher, M. and Gerke, V. (2000). Identification of hydrophobic amino acid residues involved in the formation of S100P homodimers in vivo. Biochemistry 39, 9533-9539.
15. Lackmann, M., Cornish, C.J., Simpson, R.J., Moritz, R.L., and Geczy, C.L. (1992). Purification and structural analysis of a murine chemotactic cytokine (CP-10) with sequence homology to S100 proteins. J. Biol. Chem. 267, 7499-7504.
16. Lackmann, M., Rajasekariah, P., Iismaa, S.E., Jones, G., Cornish, C.J., Hu, S., Simpson, R.J., Moritz, R.L., and Geczy, C.L. (1993). Identification of a chemotactic domain of the pro-inflammatory S100 protein CP-10. J. Immunol. 150, 2981-2991.
17. Matsumura, H., Shiba, T., Inoue, T., Harada, S., and Kai, Y. (1998). A novel mode of target recognition suggested by the Å structure of holo S100B from bovine brain. Structure 6, 233-241.
18. Moroz, O.V., Antson, A.A., Murshudov, G.N., Maitland, N.J., Dodson, G.G., Wilson, K.S., Skibshoj, I., Lukanidin, E.M., and Bronstein, I.B. (2001). The three-dimensional structure of human S100A12. Acta Crystallogr. D Biol. Crystallogr. 57, 20-29.
19. Newton, R.A. and Hogg, N. (1998). The human S100 protein MRP-14 is a novel activator of the β2 integrin Mac-1 on neutrophils. J. Immunol. 160, 1427-1435.
20. Odink, K., Cerletti, N., Bruggen, J., Clerc, R.G., Tarcsay, L., Zwadlo, G., Gerhards, G., Schlegel, R., and Sorg, C. (1987). Two calcium-binding proteins in infiltrate macrophages of rheumatoid arthritis. Nature 330, 80-82.
21. 2+-bound states: the calcium sensor mechanism of S100 proteins revealed at atomic resolution. Structure 10, 557-567.
22. 2+binding proteins. Nat. Struct. Biol. 2, 790-796.
23. 1H NMR assignments of apo calcyclin and comparative structural analysis with calbindin D9k and S100β. Protein Sci. 5, 2162-2174.
24. Pröpper, C., Huang, X., Roth, J., Sorg, C., and Nacken, W. (1999). Analysis of the MRP8-MRP14 protein-protein interaction by the two-hybrid system suggests a prominent role of the C-terminal domain of S100 proteins in dimer formation. J. Biol. Chem. 274, 183-188.
25. Roth, J., Vogl, T., Sorg, C., and Sunderkotter, C. (2003). Phagocyte-specific S100 proteins: a novel group of proinflammatory molecules. Trends Immunol. 24, 155-158.
26. Rustandi, R.R., Baldisseri, D.M., Inman, K.G., Nizner, P., Hamilton, S.M., Landar, A., Landar, A., Zimmer, D.B., and Weber, D.J. (2002). Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR. Biochemistry 41, 788-796.
27. Tarabykina, S., Kriajevska, M., Scott, D.J., Hill, T.J., Lafitte, D., Derrick, P.J., Dodson, G.G., Lukanidin, E., and Bronstein, I. (2000). Heterocomplex formation between metastasis-related protein S100A4 (Mts1) and S100A1 as revealed by the yeast two-hybrid system. FEBS Lett. 475, 187-191.
28. Tarabykina, S., Scott, D.J., Herzyk, P., Hill, T.J., Tame, J.R., Kriajevska, M., Lafitte, D., Derrick, P.J., Dodson, G.G., Maitland, N.J., Lukanidin, E.M., and Bronstein, I.B. (2001). The dimerization interface of the metastasis-associated protein S100A4 (Mts1): in vivo and in vitro studies. J. Biol. Chem. 276, 24212-24222.
29. Vallely, K.M., Rustandi, R.R., Ellis, K.C., Varlamova, O., Bresnick, A.R., and Weber, D.J. (2002). Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy. Biochemistry 41, 12670-12680.
30. Vogl, T., Roth, J., Sorg, C., Hillenkamp, F., and Strupat, K. (1999). Calcium-induced noncovalently linked tetramers of MRP8 and MRP14 detected by ultraviolet matrix-assisted laser desorption/ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 10, 1124-1130.
31. Vogl, T., Ludwig, S., Goebeler, M., Strey, A., Thorey, I.S., Reichelt, R., Foell, D., Gerke, V., Manitz, M.P., Nacken, W., Werner, S., Sorg, C., and Roth, J. (2004). MRP8 and MRP14 control microtubule reorganization during transendothelial migration of phagocytes. Blood 104, 4260-4268.
32. Wang, G., Rudland, P.S., White, M.R., and Barraclough, R. (2000). Interaction in vivo and in vitro of the metastasisinducing S100 protein, S100A4 (p9Ka) with S100A1. J. Biol. Chem. 275, 11141-11146.
33. 2+-binding protein S100P. J. Mol. Biol. 325, 785-794.