14-3-3 proteins in pineal photoneuroendocrine transduction: How many roles?

Journal of Neuroendocrinology

Volumn 15, Issue 4, 2003, Pages 370-377

  Klein, David C ^a   Ganguly, S ^a   Coon, S L ^a   Shi, Q ^a   Gaildrat, P ^a   Morin, F ^a   Weller, J L ^a   Obsil, T ^b   Hickman, A ^b   Dyda, F ^b  

^a EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

14 3 3; Melatonin; N acetyltransferase; Pineal; Serotonin; Signal transduction

Indexed keywords

ARALKYLAMINE ACETYLTRANSFERASE; MELATONIN; PROTEIN 14 3 3; TRYPTOPHAN HYDROXYLASE;

HORMONE RELEASE; HORMONE SYNTHESIS; NEUROENDOCRINE SYSTEM; NEUROTRANSMISSION; PHOTORECEPTOR; PHYLOGENY; PINEAL BODY; PINEAL GLAND FUNCTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; REGULATORY MECHANISM; REVIEW; SIGNAL TRANSDUCTION; TRANSCRIPTION REGULATION;

14-3-3 PROTEINS; ANIMALS; ARYLAMINE N-ACETYLTRANSFERASE; LIGHT; MELATONIN; MODELS, MOLECULAR; NEUROSECRETORY SYSTEMS; NOREPINEPHRINE; PHOTOTRANSDUCTION; PINEAL GLAND; STRUCTURE-ACTIVITY RELATIONSHIP; TYROSINE 3-MONOOXYGENASE;

EID: 0037382527     PISSN: 09538194     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2826.2003.01000.x     Document Type: Review

References (54)

1. Aitken A. 14-3-3 and its possible role in co-ordinating multiple signaling pathways. Trends Cell Biol 1996; 6: 341-347.
2. Fu H, Subramanian RR, Masters SC. 14-3-3 proteins. structure, function, and regulation. Annu Rev Pharmacol Toxicol 2000; 40: 619.
3. Aitken A, Baxter H, Dubois T, Clokie S, Mackie S, Mitchell K, Peden A, Zemlickova E. Specificity of 14-3-3 isoform dimer interactions and phosphorylation. Biochem Soc Trans 2002; 30: 351-360.
4. Yaffe MB. How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis. FEBS Lett 2000; 513: 53-57.
5. Roseboom PH, Weller JL, Babila T, Aitken A, Sellers LA, Moffett JR, Namboodiri MA, Klein DC. Cloning and characterization of the epsilon and zeta isoforms of the 14-3-3 proteins. DNA Cell Biol 1994; 13: 629-640.
6. Moore BE, Perez VJ. Specific acidic protein of the nervous system. In: Carlson FD, ed. Physiological and Biochemical Aspects of Nervous Integration. Englewood Cliffs, NJ: Prentice Hall, 1967: 343-359.
7. 2+, calmodulin-dependent protein kinase II. FEBS Lett 1987; 219: 79-82.
8. Liu D, Bienkowska J, Petosa C, Collier RJ, Fu H, Liddington R. Crystal structure of the zeta isoform of the 14-3-3 protein. Nature 1995; 376: 191-194.
9. Xiao B, Smerdon SJ, Jones DH, Dodson GG, Soneji Y, Aitken A, Gamblin SJ. Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways. Nature 1995; 376: 188-191.
10. Yaffe MB, Rittinger K, Volinia S, Caron PR, Aitken A, Leffers H, Gamblin SJ, Smerdon SJ, Cantley LC. The structural basis for 14-3-3: phosphopeptide binding specificity. Cell 1997; 91: 961-971.
11. Petosa C, Masters SC, Bankston LA, Pohl J, Wang B, Fu H, Liddington RC. 14-3-3 zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove. J Biol Chem 1998; 273: 16305.
12. Rittinger K, Budman J, Xu J, Volinia S, Cantley LC, Smerdon SJ, Gamblin SJ, Yaffe MB. Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding. Mol Cell 1999; 4: 153-166.
13. Masters SC, Pederson KJ, Zhang L, Barbieri JT, Fu H. Interaction of 14-3-3 with a nonphosphorylated protein ligand, exoenzyme S of Pseudomonas aeruginosa. Biochemistry 1999; 38: 5216.
14. Wang BC, Yang HZ, Liu YC, Jelinek T, Zhang LX, Ruoslahti E, Fu H. Isolation of high affinity peptide antagonists for 14-3-3 proteins by phage display. Biochemistry 1999; 38: 12499-12504.
15. Klein DC, Baler R, Roseboom PH, Weller JL, Bernard M, Gastel JA, Zatz M, Iuvone PM, Begay V, Falcon J, Cahill G, Cassone VM, Coon SL. The molecular basis of the pineal melatonin rhythm: regulation of serotonin N-acetylation. In: Lydic R, Baghdoyan H, eds. Handbook of Behavioral State Control. Boca Raton, FL: CRC Press, 1998: 45-59.
16. Schulz R. The pharmacology of phosducin. Phamacol Res 2001; 43: 1-10.
17. 2+/calmodulin-dependent protein kinase II phosphorylation and 14-3-3 protein binding. J Biol Chem 2001; 276: 23805-23815.
18. Nakano K, Chen J, Tarr GE, Yoshida T, Flynn JM, Bitensky MW. Rethinking the role of phosducin: Light-regulated binding of phosducin to 14-3-3 in rod inner segments. Proc Natl Acad Sci USA 2001; 98: 4693-4698.
19. 2+/calmodulin-dependent protein kinase II phosphorylation and 14-3-3 protein binding. J Biol Chem 2001; 276: 23805-23815.
20. Le Bourdelles B, Horellou P, Le Caer JP, Denefle P, Latta M, Haavik J, Guibert B, Mayaux JF, Mallet J. Phosphorylation of human recombinant tyrosine hydroxylase isoforms 1 and 2: an additional phosphorylated residue in isoform 2 generated through alternative splicing. J Biol Chem 1991; 266: 17124-17130.
21. Almas B, Le Bourdelles B, Flatmark T, Mallet J, Haavik J. Regulation of recombinant human tyrosine hydroxylase isozymes by catecholamine binding and phosphorylation. Structure/activity studies and mechanistic implications. Eur J Biochem 1992; 209: 249-255.
22. Kumer SC, Vrana KE. Intricate regulation of tyrosine hydroxylase activity and gene expression. J Neurochem 1996; 67: 443-462.
23. Yamauchi T, Fujisawa H. Activation of tryptophan 5-monooxygenase by calcium-dependent regulator protein. Biochem Biophys Res Commun 1979; 90: 28-35.
24. Vulliet PR, Woodgett JR, Cohen P. Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase. J Biol Chem 1984; 259: 13680-13683.
25. Campbell DG, Hardie DG, Vulliet PR. Identification of four phosphorylation sites in the N-terminal region of tyrosine hydroxylase. J Biol Chem 1986; 261: 10489-10492.
26. 2+/calmodulin-dependent protein kinase II: effect of an activator protein. J Neurochem 1987; 49: 1241-1249.
27. Itagaki C, Isobe T, Taoka M, Natsume T, Nomura N, Horigome T, Omata S, Ichinose H, Nagatsu T, Greene LA, Ichimura T. Stimulus-coupled interaction of tyrosine hydroxylase with 14-3-3 proteins. Biochemistry 1999; 38: 15673-15680.
28. Kleppe R, Toska K, Haavik J. Interaction of phosphorylated tyrosine hydroxylase with 14-3-3 proteins: evidence for a phosphoserine 40-dependent association. J Neurochem 2001; 77: 1097-1107.
29. Morgan A, Burgoyne RD. Exo1 and Exo2 proteins stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells. Nature 1992; 355: 833-836.
30. Burgoyne RD. Mechanisms of catecholamine secretion from adrenal chromaffin cells. J Physiol Pharmacol 1995; 46: 273-283.
31. Isobe T, Hiyane Y, Ichimura T, Okuyama T, Takahashi N, Nakajo S, Nakaya K. Activation of protein kinase C by the 14-3-3 proteins homologous with Exo1 protein that stimulates calcium-dependent exocytosis. FEBS Lett 1992; 308: 121-124.
32. Burgoyne RD, Morgan A, O'Sullivan AJ. A major role for protein kinase C in calcium-activated exocytosis in permeabilised adrenal chromaffin cells. FEBS Lett 1988; 238: 151-155.
33. Roth D, Burgoyne RD. Stimulation of catecholamine secretion from adrenal chromaffin cells by 14-3-3 proteins is due to reorganisation of the cortical actin network. FEBS Lett 1995; 374: 77-81.
34. Vitale ML, Seward EP, Trifaro JM. Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis. Neuron 1995; 14: 353-363.
35. Burgoyne RD, Morgan A, O'Sullivan AJ. The control of cytoskeletal actin and exocytosis in intact and permeabilized adrenal chromaffin cells: role of calcium and protein kinase C. Cell Signal 1989; 1: 323-334.
36. Rose SD, Lejen T, Zhang L, Trifaro JM. Chromaffin cell F-actin disassembly and potentiation of catecholamine release in response to protein kinase C activation by phorbol esters is mediated through myristoylated alanine-rich C kinase substrate phosphorylation. J Biol Chem 2001; 276: 36757-36763.
37. Reig JA, Yu L, Klein DC. Pineal transduction. Adrenergic-cyclic AMP-dependent phosphorylation of cytoplasmic 33-kDa protein (MEKA) which binds βγ-complex of transducin. J Biol Chem 1990; 265: 5816-5824.
38. Schaad N, Shinohara T, Abe T, Klein DC. Photoneural control of the synthesis and phosphorylation of pineal MEKA (phosducin). Endocrinology 1991; 129: 3289-3298.
39. +-enriched medium. J Neurochem 1979; 33: 1031-1042.
40. Boadle-Biber MC, Phan TH. AGN 2979 [3(3-methoxyphenyl)-3-(3-dimethylaminopropyl)-4,4-dimethylpiperidine-2,6-dione]. An inhibitor of the activation of tryptophan hydroxylase. Biochem Pharmacol 1986; 35: 1521-1526.
41. Cooper JR, Bloom FE, Roth RH. The Biochemical Basis of Neuropharmacology, 5th edn. New York: Oxford University Press, 1986: 203-339.
42. 2+, calmodulin-dependent protein kinase. Purification and characterization. J Biol Chem 1981; 256: 5404-5409.
43. Furukawa Y, Ikuta N, Omata S, Yamauchi T, Isobe T, Ichimura T. Demonstration of the phosphorylation-dependent interaction of tryptophan hydroxylase with the 14-3-3 protein. Biochem Biophys Res Commun 1993; 194: 144-149.
44. Ichimura T, Uchiyama J, Kunihiro O, Ito M, Horigome T, Omata S, Shinkai F, Kaji H, Isobe T. Identification of the site of interaction of the 14-3-3 protein with phosphorylated tryptophan hydroxylase. J Biol Chem 1995; 270: 28515-28518.
45. Banik U, Wang G, Wagner P, Kaufman S. Interaction of phosphorylated tryptophan hydroxylase with 14-3-3 proteins. J Biol Chem 1997; 272: 26219-26225.
46. Sugden D, Grady R Jr, Mefford IN. Measurement of tryptophan hydroxylase activity in rat pineal glands and pinealocytes using an HPLC assay with electrochemical detection. J Pineal Res 1989; 6: 285-292.
47. Thomas KB, Iuvone PM. Circadian rhythm of tryptophan hydroxylase activity in chicken retina. Cell Mol Neurobiol 1991; 11: 511-527.
48. Valenciano AI, Alonso-Gomez AL, Iuvone PM. Diurnal rhythms of tryptophan hydroxylase activity in Xenopus laevis retina: opposing phases in photoreceptors and inner retinal neurons. Neuroreport 1999; 10: 2131-2135.
49. Valenciano AI, Alonso-Gomez AL, Iuvone PM. Regulation of tryptophan hydroxylase activity in Xenopus laevis photoreceptor cells by cyclic AMP. J Neurochem 2000; 74: 1961-1967.
50. Ganguly S, Coon SL, Klein DC. Control of melatonin synthesis in the mammalian pineal gland: the critical role of serotonin acetylation. Cell Tissue Res 2002; 309: 127-137.
51. Ganguly S, Gastel JA, Weller JL, Schwartz C, Jaffe H, Namboodiri MAA, Coon SL, Hickman AB, Rollag M, Obsil T, Beauverger P, Ferry G, Boutin JA, Klein DC. Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-binding switch in melatonin synthesis. Proc Natl Acad Sci USA 2001; 98: 8083-8088.
52. Obsil T, Ghirlando R, Klein DC, Ganguly S, Dyda F. Crystal structure of the 14-3-3zeta: serotonin N-acetyltransferase complex: a role for scaffolding in enzyme regulation. Cell 2001; 105: 257-267.
53. Klein DC, Ganguly S, Coon SL, Weller JL, Obsil T, Hickman A, Dyda F. 14-3-3 proteins and photoneuroendocrine transduction: role in controlling the daily rhythm in melatonin. Biochem Soc Trans 2002; 30: 365-373.
54. Hickman AB, Namboodiri MAA, Klein DC, Dyda F. The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8Å resolution with a bisubstrate analog. Cell 1999; 91: 361-369.