Structural insights into enzyme regulation for inositol 1,4,5-trisphosphate 3-kinase B

Biochemistry

Volumn 44, Issue 44, 2005, Pages 14486-14493

  Chamberlain, Philip P ^a   Sandberg, Mark L ^a   Sauer, Karsten ^a   Cooke, Michael P ^a   Lesley, Scott A ^a   Spraggon, Glen ^a  

^a GENOMICS INSTITUTE OF THE NOVARTIS RESEARCH FOUNDATION   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CELLS; CRYSTAL STRUCTURE; IMMUNOLOGY; MUTAGENESIS;

CATALYTIC DOMAIN; ENZYME ACTIVATION; ENZYME REGULATION; METAZOAN CELLULAR SIGNALING;

ENZYMES;

ADENOSINE TRIPHOSPHATE; CALCIUM ION; CALMODULIN; INDOLE; INOSITOL 1,4,5 TRISPHOSPHATE 3 KINASE B; INOSITOL TRISPHOSPHATE 3 KINASE; MAGNESIUM ION; TRYPTOPHAN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CATALYSIS; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME REGULATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; STRUCTURE ANALYSIS; T LYMPHOCYTE;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; HUMANS; MAGNESIUM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PHOSPHOTRANSFERASES (ALCOHOL GROUP ACCEPTOR); PROTEIN CONFORMATION; PROTEIN ISOFORMS; SEQUENCE ALIGNMENT;

METAZOA;

EID: 27644434704     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051256q     Document Type: Article

References (42)

1. Irvine, R. F., and Schell, M. J. (2001) Back in the water: The return of the inositol phosphates, Nat. Rev. Mol. Cell Biol. 2, 327-38.
2. 4 run a protection racket? Curr. Biol. 11, R172-4.
3. Wen, B. G., Pletcher, M. T., Warashina, M., Choe, S. H., Ziaee, N., Wiltshire, T., Sauer, K., and Cooke, M. P. (2004) Inositol 1,4,5-trisphosphate 3 kinase B controls positive selection of T cells and modulates Erk activity, Proc. Natl. Acad. Sci. U.S.A. 101, 5604-9.
4. Wen, B. G., Miller, A. T., Huang, Y. H., Pletcher, M. T., Warashina, M., Choe, S. H., Ziaee, N., Wiltshire, T., Cooke, M. P., and Sauer, K. (2004) Ms. T-less, an ENU-Induced Mouse Mutant Linking Impaired Expression of Ins(1,4,5)P3 3-kinase B (Itpkb) to Defective Erk Activation and Blocked Positive Selection, Immunology 2004, pp 85-90, Medimont S.r.1., Bologna, Italy.
5. Cullen, P. J., Hsuan, J. J., Truong, O., Letcher, A. J., Jackson, T. R., Dawson, A. P., and Irvine, R. F. (1995) Identification of a specific Ins(1,3,4,5)P4-binding protein as a member of the GAP1 family, Nature 376, 527-30.
6. Pattni, K., and Banting, G. (2004) Ins(1,4,5)P3 metabolism and the family of IP3-3 Kinases, Cell Signalling 16, 643-54.
7. Takazawa, K., Perret, J., Dumont, J. E., and Erneux, C. (1991) Molecular cloning and expression of a new putative inositol 1,4,5-trisphosphate 3-kinase isoenzyme, Biochem. J. 278 (Part 3), 883-6.
8. Choi, K. Y., Kim, H. K., Lee, S. Y., Moon, K. H., Sim, S. S., Kim, J. W., Chung, H. K., and Rhee, S. G. (1990) Molecular cloning and expression of a complementary DNA for inositol 1,4,5-trisphosphate 3-kinase, Science 248, 64-6.
9. Dewaste, V., Pouillon, V., Moreau, C., Shears, S., Takazawa, K., and Erneux, C. (2000) Cloning and expression of a cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase C, Biochem. J. 352 (Part 2), 343-51.
10. Jun, K., Choi, G., Yang, S. G., Choi, K. Y., Kim, H., Chan, G. C., Storm, D. R., Albert, C., Mayr, G. W., Lee, C. J., and Shin, H. S. (1998) Enhanced hippocampal CA1 LTP but normal spatial learning in inositol 1,4,5-trisphosphate 3-kinase(A)-deficient mice, Learn. Mem. 5, 317-30.
11. Mailleux, P., Takazawa, K., Erneux, C., and Vanderhaeghen, J. J. (1991) Inositol 1,4,5-trisphosphate 3-kinase distribution in the rat brain. High levels in the hippocampal CA1 pyramidal and cerebellar Purkinje cells suggest its involvement in some memory processes, Brain Res. 539, 203-10.
12. Nalaskowski, M. M., Bertsch, U., Fanick, W., Stockebrand, M. C., Schmale, H., and Mayr, G. W. (2003) Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol trisphosphate phosphorylation and shuttles actively between nucleus and cytoplasm, J. Biol. Chem. 278, 19765-76.
13. Vanweyenberg, V., Communi, D., D'Santos, C. S., and Erneux, C. (1995) Tissue- and cell-specific expression of Ins(1,4,5)P3 3-kinase isoenzymes, Biochem. J. 306 (Part 2), 429-35.
14. 2+ homoeostasis, Biochem. J. 324 (Part 2), 579-89.
15. 2+ responses on transfection in COS-7 cells, Biochem. J. 374, 41-9.
16. Pouillon, V., Hascakova-Bartova, R., Pajak, B., Adam, E., Bex, F., Dewaste, V., Van Lint, C., Leo, O., Erneux, C., and Schurmans, S. (2003) Inositol 1,3,4,5-tetrakisphosphate is essential for T lymphocyte development, Nat. Immunol. 4, 1136-43.
17. Dewaste, V., Roymans, D., Moreau, C., and Erneux, C. (2002) Cloning and expression of a full-length cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase B, Biochem. Biophys. Res. Commun. 291, 400-5.
18. Pattni, K., Millard, T. H., and Banting, G. (2003) Calpain cleavage of the B isoform of Ins(1,4,5)P3 3-kinase separates the catalytic domain from the membrane anchoring domain, Biochem. J. 375, 643-51.
19. Woodring, P. J., and Garrison, J. C. (1997) Expression, purification, and regulation of two isoforms of the inositol 1,4,5-trisphosphate 3-kinase, J. Biol. Chem. 272, 30447-54.
20. Takazawa, K., and Erneux, C. (1991) Identification of residues essential for catalysis and binding of calmodulin in rat brain inositol 1,4,5-trisphosphate 3-kinase, Biochem. J. 280 (Part 1), 125-9.
21. Erneux, C., Moreau, C., Vandermeers, A., and Takazawa, K. (1993) Interaction of calmodulin with a putative calmodulin-binding domain of inositol 1,4,5-triphosphate 3-kinase. Effects of synthetic peptides and site-directed mutagenesis of Trp165, Eur. J. Biochem. 214, 497-501.
22. Sim, S. S., Kim, J. W., and Rhee, S. G. (1990) Regulation of D-myo-inositol 1,4,5-trisphosphate 3-kinase by cAMP-dependent protein kinase and protein kinase C, J. Biol. Chem. 265, 10367-72.
23. Communi, D., Vanweyenberg, V., and Erneux, C. (1997) D-myoinositol 1,4,5-trisphosphate 3-kinase A is activated by receptor activation through a calcium:calmodulin-dependent protein kinase II phosphorylation mechanism, EMBO J. 16, 1943-52.
24. Rogers, S., Wells, R., and Rechsteiner, M. (1986) Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis, Science 234, 364-8.
25. Molinari, M., Anagli, J., and Carafoli, E. (1995) Purification of μ-calpain by a novel affinity chromatography approach. New insights into the mechanism of the interaction of the protease with targets, J. Biol. Chem. 270, 2032-5.
26. Gonzalez, B., Schell, M. J., Letcher, A. J., Veprintsev, D. B., Irvine, R. F., and Williams, R. L. (2004) Structure of a human inositol 1,4,5-trisphosphate 3-kinase: Substrate binding reveals why it is not a phosphoinositide 3-kinase, Mol. Cell 75, 689-701.
27. Miller, G. J., and Hurley, J. H. (2004) Crystal structure of the catalytic core of inositol 1,4,5-trisphosphate 3-kinase, Mol. Cell 15, 703-11.
28. Soderling, T. R., and Stall, J. T. (2001) Structure and regulation of calcium/calmodulin-dependent protein kinases, Chem. Rev. 101, 2341-52.
29. Otwinowski, Z., and Minor, W. (1997) Processing of X-ray Diffraction Data Collected in Oscillation Mode, Methods Enzymol. 276, 307-26.
30. Collaborative Computational Project, No. 4 (1994) The CCP4 suite: Programs for protein crystallography, version 3.1, Acta Crystallogr. D50, 760-3.
31. Stroroni, L. C., McCoy, A. J., and Read, R. J. (2004) Likelihood enhanced fast rotation functions, Acta Crystallogr. D60, 432-8.
32. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-9.
33. Emsley, P., and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics, Acta Crystallogr. D60, 2126-32.
34. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method, Acta Crystallogr. D53, 240-55.
35. Perrakis, A., Harkiolaki, M., Wilson, K. S., and Lamzin, V. S. (2001) ARP/wARP and molecular replacement, Acta Crystallogr. D57, 1445-50.
36. Yap, K. L., Kim, J., Truong, K., Sherman, M., Yuan, T., and Ikura, M. (2000) Calmodulin target database, J. Struct. Fund Genomics 1, 8-14.
37. Rhoads, A. R., and Friedberg, F. (1997) Sequence motifs for calmodulin recognition, FASEB J. 11, 331-40.
38. Porumb, T., Crivici, A., Blackshear, P. J., and Ikura, M. (1997) Calcium binding and conformational properties of calmodulin complexed with peptides derived from myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein (MRP), Eur. Biophys. J. 25, 239-47.
39. 2+-calmodulin-dependent kinase kinase, Nat. Struct. Biol. 6, 819-24.
40. Takazawa, K., Passareiro, H., Dumont, J. E., and Erneux, C. (1989) Purification of bovine brain inositol 1,4,5-trisphosphate 3-kinase. Identification of the enzyme by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, Biochem. J. 261, 483-8.
41. Johanson, R. A., Hansen, C. A., and Williamson, J. R. (1988) Purification of D-myo-inositol 1,4,5-trisphosphate 3-kinase from rat brain, J. Biol. Chem. 263, 7465-71.
42. 2+ releasing second messenger Ins(1,4,5)-P3, Curr. Mol. Med. 4, 277-90.