PI 3-kinase: Structural and functional analysis of intersubunit interactions

EMBO Journal

Volumn 13, Issue 3, 1994, Pages 511-521

  Dhand, Ritu ^a   Hara, Kenta ^b   Hiles, Ian ^a,c   Bax, Ben ^d   Gout, Ivan ^a   Panayotou, George ^a   Fry, Michael J ^a,e   Yonezawa, Kazuyoshi ^b   Kasuga, Masato ^b   Waterfield, Michael D ^a,f  

^a LUDWIG INSTITUTE FOR CANCER RESEARCH   (United Kingdom)

^b KOBE UNIVERSITY   (Japan)

^c WELLCOME RESEARCH LABORATORIES   (United Kingdom)

^d UNIVERSITY OF LONDON   (United Kingdom)

^e INSTITUTE OF CANCER RESEARCH   (United Kingdom)

^f UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

PI 3 kinase; Protein structure; SH2 domains

Indexed keywords

GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; PHOSPHATIDYLINOSITOL KINASE; PROTEIN SUBUNIT; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BINDING SITE; COMPLEX FORMATION; CONTROLLED STUDY; DELETION MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; STRUCTURE ACTIVITY RELATION;

ANIMALIA;

EID: 0028157767     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1994.tb06289.x     Document Type: Article

References (47)

1. Backer, J.M. et al. (1992) EMBO J., 11, 3469-3479.
2. Bernstein, F.C., Koetzle, T.F., Williams, G.J.B., Meyer, E.F. Jr, Brice, M.D., Rodgers, J.R., Kennard, O., Shimanouchi, T. and Tasumi, M. (1977) J. Mol. Biol., 112, 535-542.
3. Blundell, T.L., Barlow, D., Borkakoti, N. and Thorton, J. (1983) Nature, 306, 281-283.
4. Booker, G.W., Breeze, A.L., Downing, A.K., Panayotou, G., Gout, I., Waterfield, M.D. and Campbell, I.D. (1992) Nature, 358, 684-687.
5. Carpenter, C.L., Duckworth, B.C., Auger, K.R., Cohen, B., Schaffhausen, B.S. and Cantley, L.C. (1990) J. Biol. Chem., 265, 19704-19711.
6. Carpenter, C.L., Auger, K.R., Chanudhuri, M., Yoakim, M., Schaffhausen, B., Shoelson, S. and Cantley, L.C. (1993) J. Biol. Chem., 268, 9478-9483.
7. Conway, J.F. and Parry, D.A.D. (1990) Int. J. Biol. Macromol., 12, 328-334.
8. Cooper, J.A. and Kashishian, A. (1993) Mol. Cell. Biol., 13, 1737-1745.
9. Crick, F.H.C. (1953) Acta Crystallogr., 6, 689-697.
10. Eliopoulos, E.G. (1989) Documentation for Leeds Prediction Programs. Department of Biophysics, University of Leeds.
11. End, P., Gout, I., Fry, M.J., Panayotou, G., Dhand, R., Yonezawa, K., Kasuga, M. and Waterfield, M.D. (1993) J. Biol. Chem., 268, 10066-10075.
12. Fantl, W.J., Escobedo, J.A., Martin, G.A., Turck, C.W., Delrosario, M., McCormick, F. and Williams, L.T. (1992) Cell, 69, 413-423.
13. Fry, M.J. (1992) Curr. Biol., 2, 78-80.
14. Fry, M.J., Panayotou, G., Dhand, R., Ruiz-Larrea, F., Gout, I., Nguyen, O., Courtneidge, S.A. and Waterfield, M.D. (1992) Biochem. J., 288, 383-393.
15. Giorgetti, S., Ballotti, R., Kowalskichauvel, A., Tartare, S. and Van Obberghen, E. (1993) J. Biol. Chem., 268, 7358-7364.
16. Gout, I., Dhand, R., Panayotou, G., Fry, M.J., Hues, I., Otsu, M. and Waterfield, M.D. (1992) Biochem. J., 288, 395-405.
17. Hawkins, P.T., Jackson, T.R. and Stephens, L.R. (1992) Nature, 358, 157-159.
18. Herman, P.K. and Emr, S.D. (1990) Mol. Cell. Biol., 10, 6742-6754.
19. Hiles, I.D. et al. (1992) Cell, 70, 419-429.
20. Hodges, R.S., Sodek, J., Smillie, L.B. and Jurasek, L. (1972) Cold Spring Harbor Symp. Quant. Biol., 37, 299-310.
21. Jamney, P.A., Lamb, J., Allen, P.G. and Matsudaira, P.T. (1992) J. Biol. Chem., 267, 11818-11823.
22. Kunz, J., Henriquez, R., Schneider, U., Deuterreinhard, M., Movva, N.R. and Hall, M.N. (1993) Cell, 73, 585-596.
23. Ling, L.E., Druker, B.J., Cantley, L.C. and Roberts, T.M. (1992) J. Virol., 66, 1702-1708.
24. Mclachlan, A.D. and Stewart, M. (1975) J. Mol. Biol., 98, 293-304.
25. Morgan, S.J., Smith, A.D. and Parker, P.J. (1990) Eur. J. Biochem., 191, 761-767.
26. Otsu, M. et al. (1991) Cell, 65, 91-104.
27. Parry, D.A.D. (1975) J. Mol. Biol., 98, 519-535.
28. Panayotou, G. and Waterfield, M.D. (1992) Trends Cell Biol., 2, 358-360.
29. Panayotou, G., Bax, B., Gout, I., Federwisch, M., Wroblowski, B., Dhand, R., Fry, M.J., Blundell, T.L., Wollmer, A. and Waterfield, M.D. (1992) EMBO J., 11, 4261-4272.
30. Parker, P. and Waterfield, M.D. (1992) Cell Growth Differ., 3, 747-752.
31. Pawson, T. and Gish, G.D. (1992) Cell, 71, 359-362.
32. Pawson, T. and Schlessinger, J. (1993) Curr. Biol., 3, 434-442.
33. Philips, G.N., Jr, Lattman, E.E., Cummins, P., Lee, K.Y. and Cohen, C. (1979) Nature, 278, 413-417.
34. Philips, G.N., Jr, Fillers, J.P. and Cohen, C. (1986) J. Mol. Biol., 192, 111-131.
35. Reif, K., Gout, I., Waterfield, M.D. and Cantrell, D.A. (1993) J. Biol. Chem., 268, 10780-10788.
36. Ruiz-Larrea, F. et al. (1993) Biochem. J., 290, 609-616.
37. Schu, P.V., Takegawa, K., Fry, M.J., Stack, J.H., Waterfield, M.D. and Emr, S.D. (1993) Science, 260, 88-91.
38. Shibasaki, F., Homma, Y. and Takenawa, T. (1991) J. Biol. Chem., 266, 8108-8114.
39. Shoelson, S.E., Sivaraja, M., Williams, K.P., Hu, P., Schlessinger, J. and Weiss, M.A. (1993) EMBO J., 12, 795-802.
40. Smith, D.B. and Johnson, K.S. (1988) Gene, 67, 31-40.
41. Stephens, L.R., Hughes, K.T. and Irvine, R.F. (1991) Nature, 351, 33-39.
42. Summers, M.D. and Smith, G.E. (1987) Tex. Exp. Stat. Bull., 1555, 1-56.
43. Takebe, Y., Seiki, M., Fujisawa, J., Hoy, P., Yokota, K., Arai, K., Yoshida, M. and Arai, N. (1988) Mol. Cell. Biol., 8, 466-472.
44. Valius, M. and Kazlauskas, A. (1993) Cell, 73, 321-334.
45. Volinia, S., Patracchini, P., Otsu, M., Hiles, I., Gout, I., Calzolari, E., Bernardi, F., Rooke, L. and Waterfield, M.D. (1992) Oncogene, 7, 789-793.
46. Yonezawa, K. et al. (1992) J. Biol. Chem., 267, 25958-25965.
47. Yu, F.X., Sun, H.-Q., Janmey, P.A. and Yin, H.L. (1992) J. Biol. Chem. 267, 14616-14621.