IRBIT Suppresses IP 3 Receptor Activity by Competing with IP 3 for the Common Binding Site on the IP 3 Receptor

Molecular Cell

Volumn 22, Issue 6, 2006, Pages 795-806

  Ando, Hideaki ^a   Mizutani, Akihiro ^b   Kiefer, Hélène ^b   Tsuzurugi, Dai ^b   Michikawa, Takayuki ^a,b,c   Mikoshiba, Katsuhiko ^a,b,c  

^a RIKEN BRAIN SCIENCE INSTITUTE   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

MOLNEURO; SIGNALING

Indexed keywords

AMINO ACID; BINDING PROTEIN; CALCIUM; IP3 RECEPTOR; IRBIT PROTEIN; LIGAND; PROTEIN; UNCLASSIFIED DRUG; ADENOSYLHOMOCYSTEINASE; CALCIUM CHANNEL; CELL RECEPTOR; DCAL 1 PROTEIN, HUMAN; DCAL-1 PROTEIN, HUMAN; INOSITOL 1,4,5 TRISPHOSPHATE; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; ITPR1 PROTEIN, HUMAN; LECTIN; MEMBRANE PROTEIN; SERINE;

ANIMAL CELL; ARTICLE; BINDING SITE; CALCIUM TRANSPORT; CONTROLLED STUDY; HUMAN; HUMAN CELL; IN VITRO STUDY; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN BINDING; PROTEIN PHOSPHORYLATION; ANIMAL; BINDING COMPETITION; CALCIUM SIGNALING; CELL STRAIN COS1; CERCOPITHECUS; DRUG EFFECT; DRUG POTENTIATION; FLUORESCENCE MICROSCOPY; HELA CELL; METABOLISM; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN PROCESSING;

ADENOSYLHOMOCYSTEINASE; ANIMALS; BINDING, COMPETITIVE; CALCIUM; CALCIUM CHANNELS; CALCIUM SIGNALING; CERCOPITHECUS AETHIOPS; COS CELLS; HELA CELLS; HUMANS; INOSITOL 1,4,5-TRISPHOSPHATE; INOSITOL 1,4,5-TRISPHOSPHATE RECEPTORS; LECTINS, C-TYPE; LIGANDS; MEMBRANE PROTEINS; MICROSCOPY, FLUORESCENCE; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECEPTORS, CYTOPLASMIC AND NUCLEAR; SERINE;

EID: 33745206890     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2006.05.017     Document Type: Article

References (28)

1. 3 binding to the receptor. J. Biol. Chem. 278 (2003) 10602-10612
2. Berridge M.J. Inositol trisphosphate and calcium signalling. Nature 361 (1993) 315-325
3. Berridge M.J., Lipp P., and Bootman M.D. The versatility and universality of calcium signalling. Nat. Rev. Mol. Cell Biol. 1 (2000) 11-21
4. Berridge M.J., Bootman M.D., and Roderick H.L. Calcium signalling: dynamics, homeostasis and remodelling. Nat. Rev. Mol. Cell Biol. 4 (2003) 517-529
5. 2+ signals. J. Cell Sci. 114 (2001) 2213-2222
6. Bosanac I., Alattia J.R., Mal T.K., Chan J., Talarico S., Tong F.K., Tong K.I., Yoshikawa F., Furuichi T., Iwai M., et al. Structure of the inositol 1,4,5-trisphosphate receptor binding core in the complex with its ligand. Nature 420 (2002) 696-700
7. 3 receptor. Biochim. Biophys. Acta 1742 (2004) 89-102
8. Bosanac I., Yamazaki H., Matsu-ura T., Michikawa T., Mikoshiba K., and Ikura M. Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor. Mol. Cell 17 (2005) 193-203
9. 3 receptor activity is differentially regulated in endoplasmic reticulum subdomains during oocyte maturation. Curr. Biol. 15 (2005) 765-770
10. Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., and Grant S.G.N. Proteomic analysis of in vivo phosphorylated synaptic proteins. J. Biol. Chem. 280 (2005) 5972-5982
11. Dekker J.W., Budhia S., Angel N.Z., Cooper B.J., Clark G.J., Hart D.N.J., and Kato M. Identification of an S-adenosylhomocysteine hydrolase-like transcript induced during dendritic cell differentiation. Immunogenetics 53 (2002) 993-1001
12. Flotow H., Graves P.R., Wang A., Fiol C.J., Roeske R.W., and Roach P.J. Phosphate groups as substrate determinants for casein kinase I action. J. Biol. Chem. 265 (1990) 14264-14269
13. 2+ signaling in the brain. J. Neurochem. 64 (1995) 953-960
14. Hanks S.K. Genomic analysis of the eukaryotic protein kinase superfamily: a perspective. Genome Biol. 4 (2003) 111
15. 2+ signaling. J. Biol. Chem. 279 (2004) 11967-11975
16. 2+ signaling by diacylglycerol-mediated inositol 1,4,5-trisphosphate production. J. Biol. Chem. 280 (2005) 11723-11730
17. Michikawa T., Hirota J., Kawano S., Hiraoka M., Yamada M., Furuichi T., and Mikoshiba K. Calmodulin mediates calcium-dependent inactivation of cerebellar type 1 inositol 1,4,5-trisphosphate receptor. Neuron 23 (1999) 799-808
18. Nissen P., Kjeldgaard M., and Nyborg J. Macromolecular mimicry. EMBO J. 19 (2000) 489-495
19. Patel S., Joseph S.K., and Thomas A.P. Molecular properties of inositol 1,4,5-trisphosphate receptors. Cell Calcium 25 (1999) 247-264
20. Patterson R.L., Boehning D., and Snyder S.H. Inositol 1,4,5-trisphosphate receptors as signal integrators. Annu. Rev. Biochem. 73 (2004) 437-465
21. Rena G., Bain J., Elliott M., and Cohen P. D4476, a cell-permeant inhibitor of CKI, suppresses the site-specific phosphorylation and nuclear exclusion of FOXO1a. EMBO Rep. 5 (2004) 60-65
22. Scherer L.J., and Rossi J.J. Approaches for the sequence-specific knockdown of mRNA. Nat. Biotechnol. 21 (2003) 1457-1465
23. Turner M.A., Yuan C.S., Borchardt R.T., Hershfield M.S., Smith G.D., and Howell P.L. Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength. Nat. Struct. Biol. 5 (1998) 369-376
24. 3-mediated calcium signaling. J. Biol. Chem. 277 (2002) 8106-8113
25. 3R. Nat. Cell Biol. 7 (2005) 1021-1028
26. Wittig R., Nessling M., Will R.D., Mollenhauer J., Salowsky R., Munstermann E., Schick M., Helmbach H., Gschwendt B., Korn B., et al. Candidate genes for cross-resistance against DNA-damaging drugs. Cancer Res. 62 (2002) 6698-6705
27. 2+ release channels. Proc. Natl. Acad. Sci. USA 99 (2002) 7711-7716
28. Yoshikawa F., Morita M., Monkawa T., Michikawa T., Furuichi T., and Mikoshiba K. Mutational analysis of the ligand binding site of the inositol 1,4,5-trisphosphate receptor. J. Biol. Chem. 271 (1996) 18277-18284