Characterization of a central Ca2+/calmodulin-dependent protein kinase IIα/β binding domain in densin that selectively modulates glutamate receptor subunit phosphorylation

Journal of Biological Chemistry

Volumn 286, Issue 28, 2011, Pages 24806-24818

  Jiao, Yuxia ^a,c   Jalan Sakrikar, Nidhi ^a   Robison, A J ^a,d   Baucum II, Anthony J ^a   Bass, Martha A ^a   Colbran, Roger J ^a,b  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b VANDERBILT UNIVERSITY MEDICAL CENTER   (United States)

^c Chinese Academy of Sciences and China National Center for Bioinformation   (China)

^d MOUNT SINAI SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; AMPA-RECEPTOR; AUTOPHOSPHORYLATION; BINDING DOMAIN; C-TERMINAL DOMAINS; CATALYTIC DOMAINS; DOWNSTREAM TARGET; GLUTAMATE RECEPTOR; HEK293 CELLS; IN-VITRO; INHIBITOR PROTEINS; INTACT CELLS; ISOFORMS; MODEL PEPTIDES; NMDA RECEPTOR; PROTEIN KINASE;

AMINO ACIDS; CALCIUM; ENZYMES; PEPTIDES; PHOSPHORYLATION;

CALMODULIN;

AMPA RECEPTOR; BRAIN EXTRACT; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II ALPHA; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II BETA; DENSIN; ENZYME INHIBITOR; GLUTAMATE RECEPTOR; ISOENZYME; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PEPTIDE; PROTEIN; RECEPTOR SUBUNIT; SERINE; SYNTIDE 2; THREONINE; UNCLASSIFIED DRUG; CALCIUM; CALMODULIN; GLUTAMATE RECEPTOR IONOTROPIC, AMPA 1; LRRC7 PROTEIN, HUMAN; LRRC7 PROTEIN, MOUSE; LRRC7 PROTEIN, RAT; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 2B; SIALOGLYCOPROTEIN; XENOPUS PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; AUTOPHOSPHORYLATION; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CELL STRAIN HEK293; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME INHIBITION; ENZYME PHOSPHORYLATION; ENZYME SUBSTRATE; GENE MUTATION; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; IN VITRO STUDY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; ANIMAL; GENETICS; METABOLISM; MOUSE; MUTATION; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; RAT; SWINE; XENOPUS LAEVIS;

ANIMALS; CALCIUM; CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE TYPE 2; CALMODULIN; HUMANS; ISOENZYMES; MICE; MUTATION; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; RATS; RECEPTORS, AMPA; RECEPTORS, N-METHYL-D-ASPARTATE; SIALOGLYCOPROTEINS; SWINE; XENOPUS LAEVIS; XENOPUS PROTEINS;

EID: 79960146846     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.216010     Document Type: Article

References (46)

1. Colbran, R. J. (2004) Biochem. J. 378, 1-16
2. Schulman, H. (2004) J. Neurosci. 24, 8399-8403
3. Barria, A., and Malinow, R. (2005) Neuron 48, 289-301
4. Zhou, Y., Takahashi, E., Li, W., Halt, A., Wiltgen, B., Ehninger, D., Li, G. D., Hell, J. W., Kennedy, M. B., and Silva, A. J. (2007) J. Neurosci. 27, 13843-13853
5. Apperson, M. L., Moon, I. S., and Kennedy, M. B. (1996) J. Neurosci. 16, 6839-6852
6. Strack, S., Robison, A. J., Bass, M. A., and Colbran, R. J. (2000) J. Biol. Chem. 275, 25061-25064
7. Walikonis, R. S., Oguni, A., Khorosheva, E. M., Jeng, C. J., Asuncion, F. J., and Kennedy, M. B. (2001) J. Neurosci. 21, 423-433
8. Izawa, I., Nishizawa, M., Ohtakara, K., and Inagaki, M. (2002) J. Biol. Chem. 277, 5345-5350
9. Jiao, Y., Robison, A. J., Bass, M. A., and Colbran, R. J. (2008) J. Neurochem. 105, 1746-1760
10. Thalhammer, A., Trinidad, J. C., Burlingame, A. L., and Schoepfer, R. (2009) J. Neurochem. 109, 297-302
11. Robison, A. J., Bass, M. A., Jiao, Y., MacMillan, L. B., Carmody, L. C., Bartlett, R. K., and Colbran, R. J. (2005) J. Biol. Chem. 280, 35329-35336
12. Jenkins, M. A., Christel, C. J., Jiao, Y., Abiria, S., Kim, K. Y., Usachev, Y. M., Obermair, G. J., Colbran, R. J., and Lee, A. (2010) J. Neurosci. 30, 5125-5135
13. Quitsch, A., Berhörster, K., Liew, C. W., Richter, D., and Kreienkamp, H. J. (2005) J. Neurosci. 25, 479-487
14. Tobimatsu, T., and Fujisawa, H. (1989) J. Biol. Chem. 264, 17907-17912
15. Brocke, L., Chiang, L. W., Wagner, P. D., and Schulman, H. (1999) J. Biol. Chem. 274, 22713-22722
16. Brocke, L., Srinivasan, M., and Schulman, H. (1995) J. Neurosci. 15, 6797-6808
17. Shen, K., Teruel, M. N., Subramanian, K., and Meyer, T. (1998) Neuron 21, 593-606
18. Srinivasan, M., Edman, C. F., and Schulman, H. (1994) J. Cell Biol. 126, 839-852
19. Strack, S., McNeill, R. B., and Colbran, R. J. (2000) J. Biol. Chem. 275, 23798-23806
20. Barria, A., Derkach, V., and Soderling, T. (1997) J. Biol. Chem. 272, 32727-32730
21. Lin, Y. C., and Redmond, L. (2008) Proc. Natl. Acad. Sci. U.S.A. 105, 15791-15796
22. Robison, A. J., Bartlett, R. K., Bass, M. A., and Colbran, R. J. (2005) J. Biol. Chem. 280, 39316-39323
23. Bayer, K. U., LeBel, E., McDonald, G. L., O'Leary, H., Schulman, H., and De Koninck, P. (2006) J. Neurosci. 26, 1164-1174
24. Bayer, K. U., De Koninck, P., Leonard, A. S., Hell, J. W., and Schulman, H. (2001) Nature 411, 801-805
25. Strack, S., and Colbran, R. J. (1998) J. Biol. Chem. 273, 20689-20692
26. Chang, B. H., Mukherji, S., and Soderling, T. R. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 10890-10895
27. Vest, R. S., Davies, K. D., O'Leary, H., Port, J. D., and Bayer, K. U. (2007) Mol. Biol. Cell 18, 5024-5033
28. Yang, E., and Schulman, H. (1999) J. Biol. Chem. 274, 26199-26208
29. Omkumar, R. V., Kiely, M. J., Rosenstein, A. J., Min, K. T., and Kennedy, M. B. (1996) J. Biol. Chem. 271, 31670-31678
30. Pawson, C. T., and Scott, J. D. (2010) Nat. Struct. Mol. Biol. 17, 653-658
31. Wong, W., and Scott, J. D. (2004) Nat. Rev. Mol. Cell Biol. 5, 959-970
32. Bollen, M., Peti, W., Ragusa, M. J., and Beullens, M. (2010) Trends Biochem. Sci. 35, 450-458
33. Grueter, C. E., Abiria, S. A., Dzhura, I., Wu, Y., Ham, A. J., Mohler, P. J., Anderson, M. E., and Colbran, R. J. (2006) Mol. Cell 23, 641-650
34. Grueter, C. E., Abiria, S. A., Wu, Y., Anderson, M. E., and Colbran, R. J. (2008) Biochemistry 47, 1760-1767
35. Nikandrova, Y. A., Jiao, Y., Baucum, A. J., Tavalin, S. J., and Colbran, R. J. (2010) J. Biol. Chem. 285, 923-934
36. Bingol, B., Wang, C. F., Arnott, D., Cheng, D., Peng, J., and Sheng, M. (2010) Cell 140, 567-578
37. Pi, H. J., Otmakhov, N., El Gaamouch, F., Lemelin, D., De Koninck, P., and Lisman, J. (2010) Proc. Natl. Acad. Sci. U.S.A. 107, 14437-14442
38. Hojjati, M. R., van Woerden, G. M., Tyler, W. J., Giese, K. P., Silva, A. J., Pozzo-Miller, L., and Elgersma, Y. (2007) Nat. Neurosci. 10, 1125-1127
39. Thiagarajan, T. C., Piedras-Renteria, E. S., and Tsien, R. W. (2002) Neuron 36, 1103-1114
40. Aakalu, G., Smith, W. B., Nguyen, N., Jiang, C., and Schuman, E. M. (2001) Neuron 30, 489-502
41. Ouyang, Y., Rosenstein, A., Kreiman, G., Schuman, E. M., and Kennedy, M. B. (1999) J. Neurosci. 19, 7823-7833
42. McGuinness, T. L., Lai, Y., and Greengard, P. (1985) J. Biol. Chem. 260, 1696-1704
43. Miller, S. G., and Kennedy, M. B. (1985) J. Biol. Chem. 260, 9039-9046
44. Chao, L. H., Pellicena, P., Deindl, S., Barclay, L. A., Schulman, H., and Kuriyan, J. (2010) Nat. Struct. Mol. Biol. 17, 264-272
45. Rellos, P., Pike, A. C., Niesen, F. H., Salah, E., Lee, W. H., von Delft, F., and Knapp, S. (2010) PLoS Biol. 8, e1000426
46. Rosenberg, O. S., Deindl, S., Sung, R. J., Nairn, A. C., and Kuriyan, J. (2005) Cell 123, 849-860