The Roles of 14-3-3 Proteins in Signal Transduction

Vitamins and Hormones

Volumn 52, Issue C, 1996, Pages 149-175

  Reuther, Gary W ^a   Pendergast, Ann Marie ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; PROTEIN; PROTEIN 14 3 3; PROTEIN KINASE INHIBITOR; TYROSINE 3 MONOOXYGENASE;

AMINO ACID SEQUENCE; CELL FUNCTION; CHEMISTRY; HOMEOSTASIS; HUMAN; MOLECULAR GENETICS; PHYSIOLOGY; REVIEW; SIGNAL TRANSDUCTION;

14-3-3 PROTEINS; AMINO ACID SEQUENCE; CELL PHYSIOLOGY; ENZYME INHIBITORS; HOMEOSTASIS; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN KINASE INHIBITORS; PROTEINS; SIGNAL TRANSDUCTION; TYROSINE 3-MONOOXYGENASE;

EID: 0029681252     PISSN: 00836729     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0083-6729(08)60410-0     Document Type: Chapter

References (97)

1. Agard D.A. To fold or not to fold. Science 260 (1993) 1903-1904
2. Aitken A. 14-3-3 proteins on the map. Trends Biochem Sci. 20 (1995) 95-97
3. Aitken A., Ellis C.A., Harris A., Sellers L.A., and Toker A. Kinase and neurotransmitters. Nature (London) 344 (1990) 594
4. Aitken A., Collinge D.B., van Heusden B.P.H., Isobe T., Rosebloom P.H., Rosenfield G., and Soll J. 14-3-3 proteins: A highly conserved, widespread family of eukaryotic proteins. Trends Biochem. Sci. 17 (1992) 498-501
5. Aitken A., Howell S., Jones D., Madrazo J., and Patel Y. 14-3-3 α and δ are the phosphorylated forms of Raf-activating 14-3-3 β and. J. Biol. Chem. 270 (1995) 5706-5709
6. Aktories K. Clostridial ADP-ribosylating toxins: Effects on ATP and GTP-binding proteins. Mol. Cell. Biochem. 138 (1994) 167-176
7. Alam R., Hachiya N., Sakaguchi M., Kawabata S., Iwanaga S., Kitajima M., Mihara K., and Omura T. cDNA cloning and characterization of mitochondrial import stimulation factor (MSF) purified from rat liver cytosol. J. Biochem. 116 (1994) 416-425
8. Ali S.M., Geisow M.J., and Burgoyne R.D. A role for calpactin in calcium-dependent exocytosis in adrenal chromaffin cells. Nature (London) 340 (1989) 313-315
9. Baker P.F., and Knight D.E. Calcium control of exocytosis and endocytosis in bovine adrenal medullary cells. Philos. Trans. R. Soc. Lond. Ser. B 296 (1981) 83-103
10. Boston P.F., Jackson P., Kynoch P.A.M., and Thompson R.J. Purification, properties, and immunohistochemical localisation of human brain 14-3-3 protein. J. Neurochem. 38 (1982) 1466-1474
11. Boston P.F., Jackson P., and Thompson R.J. Human 14-3-3 protein: Radioimmunoassay, tissue distribution, and cerebrospinal fluid levels in patients with neurological disorders. J. Neurochem. 38 (1982) 1475-1482
12. Bourne H.R., Sanders D.A., and McCormick F. The GTPase superfamily: A conserved switch for diverse cell functions. Nature (London) 348 (1990) 125-132
13. Braselmann S., and McCormick F. BCR and RAF form a complex in vivo via 14-3-3 proteins. EMBO J. 14 (1995) 4839-4848
14. Burbelo P.D., and Hall A. 14-3-3 proteins: Hot numbers in signal transduction. Curr. Biol. 5 (1995) 95-96
15. Chen F., and Wagner P.D. 14-3-3 proteins bind to histone and affect both histone phosphorylation and dephosphorylation. FEBS Lett. 347 (1994) 128-132
16. Chen Z., Fu H., Liu D., Chang P.F., Narasimhan M., Ferl R., Hasegawa P.M., and Bressan R.A. A NaCl-regulated plant gene encoding a brain protein homology that activates ADP ribosyltransferase and inhibits protein kinase. C. Plant J. 6 (1994) 729-740
17. Coburn J., and Gill D.M. ADP-ribosylation of p21ras and related proteins by Pseudomonas aeruginosa exoenzyme S. Infect. Immun. 59 (1991) 4259-4262
18. Coburn J., Wyatt R.T., Iglewski B.H., and Gill D.M. Several GTP-binding proteins, including p21c-H-ras, are preferred substrates of Pseudomonas aeruginosa exoenzyme S. J. Biol Chem. 264 (1989) 9004-9008
19. Coleman T.R., and Dunphy W.G. Cdc2 regulatory factors. Curr. Opin. Cell Biol. 6 (1994) 877-882
20. Conklin D.S., Galaktionov K., and Beach D. 14-3-3 proteins associate with cdc25 phosphatases. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 7892-7896
21. Cooper J.R., Bloom F.E., and Roth R.H. "Biochemical Basis of Neuropharmacology," 5th ed. (1986), Oxford University Press, New York 203-339
22. Cortez D., Kadlec L., and Pendergast A.M. Structural and signaling requirements for BCR-ABL-mediated transformation and inhibition of apoptosis. Mol. Cell. Biol. 15 (1995) 5531-5541
23. Craig E.A. Chaperones: Helpers along the pathways to protein folding. Science 260 (1993) 1902-1903
24. Daum G., Eisenmann-Tappe I., Fries H.W., Troppmair J., and Rapp U. The ins and outs of Raf kinases. Trends Biochem. Sci. 19 (1994) 474-480
25. Dent P., Jelinek T., Morrison D.K., Weber M.J., and Sturgill T.W. Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases. Science 268 (1995) 1902-1906
26. Diekmann D., Brill S., Garrett M.D., Totty N., Hsuan J., Monfries C., Hall C., Lim L., and Hall A. Bcr encodes a GTPase-activating protein for p21rac. Nature (London) 351 (1991) 400-402
27. Diekmann D., Abo A., Johnston C., Segal A.W., and Hall A. Interaction of Rac with p67phox and regulation of phagocytic NADPH oxidase activity. Science 265 (1994) 531-533
28. Du X., Harris S.J., Tetaz T.J., Ginsberg M.H., and Berndt M.C. Association of a phospholipase A2 (14-3-3 protein) with the platelet glycoprotein Ib-IX complex. J. Biol. Chem. 269 (1994) 18287-18290
29. Fantl W.J., Muslin A.J., Kikuchi A., Martin J.A., MacNicol A.M., Gross R.W., and Williams L.T. Activation of Raf-1 by 14-3-3 proteins. Nature (London) 371 (1994) 612-614
30. Ford J.C., Al-Khodairy F., Fotou E., Sheldrick K.S., Griffiths D.J.F., and Carr A.M. 14-3-3 protein homologs required for the DNA damage checkpoint in fission yeast. Science 265 (1994) 533-537
31. Freed E., Symons M., Macdonald S.G., McCormick F., and Ruggieri R. Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation. Science 265 (1994) 1713-1715
32. Fu H., Coburn J., and Collier R.J. A eukaryotic host factor that activates exoenzyme S of Pseudomonas aeruginosa is a member of the 14-3-3 protein family. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 2320-2324
33. Fu H., Xia K., Pallas D., Cui C., Conroy K., Narsimhan R.P., Mamnon H., Collier R.J., and Roberts T.M. Interaction of the protein kinase Raf-1 with 14-3-3 proteins. Science 266 (1994) 126-129
34. Furukawa Y., Ikuta N., Omata S., Yamauchi T., Isobe T., and Ichimura T. Demonstration of the phosphorylation-dependent interaction of tryptophan hydroxylase with the 14-3-3 proteins. Biochim. Biophys. Act 194 (1993) 144-149
35. Galaktionov K., Jessus C., and Beach D. Raf1 interaction with Cdc25 phosphatase ties mitogenic signal transduction to cell cycle activation. Genes Dev. 9 (1995) 1046-1058
36. Gierschik P. ADP-ribosylation of signal-transducing guanine nucleotide-binding proteins by pertussis toxin. Curr. Top. Microbiol. Immunol. 175 (1992) 69-96
37. Gruenberg J., and Emans N. Annexins in membrane traffic. Trends Cell Biol. 3 (1993) 224-227
38. Ichimura T., Isobe T., Okuyama T., Yamauchi T., and Fujisawa H. Brain 14-3-3 protein is an activator protein that activates tryptophan 5-monooxygenase and tyrosine 3-monooxygenase in the presence of Ca2+, calmodulin-dependent protein kinase II. FEBS Lett. 219 (1987) 79-82
39. Ichimura T., Isobe T., Okuyama T., Takahashi N., Araki K., Kuwano R., and Takahashi Y. Molecular cloning of cDNA coding for brain-specific 14-3-3 protein, a protein kinase-dependent activator of tyrosine and tryptophan hydroxylases. Proc. Natl. Acad. Sci. U.S.A. 85 (1988) 7084-7088
40. Irie K., Gotoh Y., Yashar B.M., Errede B., Nishida E., and Matsumoto K. Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase. Science 265 (1994) 1716-1719
41. Isobe T., Ichimura T., Sunaya T., Okuyama T., Takahashi N., Kuwano R., and Takahashi Y. Distinct forms of the protein kinase-dependent activator of tyrosine and tryptophan hydroxylases. J. Mol. Biol. 217 (1991) 125-132
42. Isobe T., Hiyane Y., Ichimura T., Okuyama T., Takahashi N., Nakajo S., and Nakaya K. Activation of protein kinase C by the 14-3-3 proteins homologous with Exol protein that stimulates calcium-dependent exocytosis. FEBS Lett. 308 (1992) 121-124
43. Jones D.H., Ley S., and Aitken A. Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: Implications for function as adapter proteins. FEBS Lett. 368 (1995) 55-58
44. Jones D.H.A., Martin H., Madrazo J., Robinson K.A., Nielsen P., Roseboom P.H., Patel Y., Howell S.A., and Aitken A. Expression and structural analysis of 14-3-3 proteins. J. Mol. Biol. 245 (1995) 375-384
45. Kemp B.E., Parker M.W., Hu S., Tiganis T., and House C. Substrate and pseudosubstrate interactions with protein kinases: Determinants of specificity. Trends Biochem. Sci. 19 (1994) 440-444
46. Kurzrock R., Gutterman J., and Talpaz M. The molecular genetics of Philadelphia chromosome-positive leukemias. New Engl. J. Med. 319 (1988) 990-998
47. Li S., Janosch P., Tanji M., Rosenfeld G.C., Waymire J.C., Mischak H., Kolch W., and Sedivy J.M. Regulation of Raf-1 kinase activity by the 14-3-3 family of proteins. EMBO J. 14 (1995) 685-696
48. Liu D., Blenkowska J., Petosa C., Collier R.J., Fu H., and Liddington R. Crystal structure of the zeta isoform of the 14-3-3 protein. Nature (London) 376 (1995) 191-194
49. Lu G., de Vetten N.C., Sehnke P.C., Isobe T., Ichimura T., Fu H., van Heusden G.P., and Ferl R.J. A single Arabidopsis GF14 isoform possesses biochemical characteristics of diverse 14-3-3 homologues. Plant Mol. Biol. 25 (1994) 659-667
50. Luo Z.J., Zhang X.F., Rapp U., and Avuch J. Identification of the 14-3-3 domains important for self-association and Raf binding. J. Biol. Chem. 270 (1995) 23681-23687
51. Maehama T., Takahashi K., Ohoka Y., Ui M., and Katada T. Identification of a botulinum C3-like enzyme in bovine brain that catalyzes ADP-ribosylation of GTP-binding proteins. J. Biol. Chem. 266 (1991) 10062-10065
52. Marais R., Light Y., Paterson H.F., and Marshall C.J. Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation. EMBO J. 14 (1995) 3136-3145
53. Maru Y., and Witte O.N. The BCR gene encodes a novel serine/threonine kinase activity within a single exon. Cell 67 (1991) 459-468
54. McWhirter J.R., Galasso D.L., and Wang J.Y.J. A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins. Mol. Cell. Biol. 13 (1993) 7587-7595
55. Michaud N.R., Fabian J.R., Mathes K.D., and Morrison D.K. 14-3-3 is not essential for Raf-1 function: Identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent manner. Mol. Cell. Biol. 15 (1995) 3390-3397
56. Miyata Y., and Yahara I. The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. J. Biol. Chem. 267 (1992) 7042-7047
57. Mochly-Rosen D. Localization of protein kinases by anchoring proteins: A theme in signal transduction. Science 268 (1995) 247-251
58. Mochly-Rosen D., Khaner H., and Lopez J. Identification of intracellular receptor proteins for activated protein kinase C. Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 3997-4000
59. Mochly-Rosen D., Khaner H., Lopez J., and Smith B.L. Intracellular receptors for activated protein kinase C. J. Biol. Chem. 266 (1991) 14866-14868
60. Moore B.W., and Perez V.J. Specific acidic proteins of the nervous system. In: Carlson F.D. (Ed). "Physiological and Biochemical Aspects of Nervous Integration" (1967), Prentice-Hall, Englewood Cliffs, New Jersey 343-349
61. Morgan A., and Burgoyne R.D. Exol and Exo2 proteins stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells. Nature (London) 355 (1992) 833-836
62. Morgan A., and Burgoyne R.D. Interaction between protein kinase C and Exo1 (14-3-3 protein) and its relevance to exocytosis in permeabilized adrenal chromaffin cells. Biochem. J. 286 (1992) 807-811
63. Morrison D. 14-3-3: Modulators of signaling proteins?. Science 266 (1994) 56-57
64. Moss J., Tsai S.C., and Vaughan M. Activation of cholera toxin by ADP-ribosylation factors. Methods Enzymol. 235 (1994) 640-647
65. Muller A.J., Young J.C., Pendergast A.M., Pondel M., Landau N.R., Littman D.R., and Witte O.N. BCR first exon sequences specifically activate the BCR/ABL tyrosine kinase oncogene of Philadelphia chromosome-positive human leukemias. Mol. Cell. Biol. 11 (1991) 1785-1792
66. Pallas D.C., Fu H., Haehnel L.C., Weller W., Collier R.J., and Roberts T.M. Association of polyomavirus middle tumor antigen with 14-3-3 proteins. Science 165 (1994) 535-537
67. Parker P.J., Kour G., Marais R.M., Mitchell F., Pears C., Schaap D., Stabel S., and Webster C. Protein kinase C-a family affair. Mol. Cell. Endocrinol. 65 (1989) 1-11
68. Pendergast A.M., Muller A.J., Havlik M.H., Maru Y., and Witte O.N. BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner. Cell 66 (1991) 161-171
69. Pendergast A.M., Quilliam L.A., Cripe L.D., Bassing C.H., Dai Z., Li N., Batzer A., Rabun K.M., Der C.J., Schlessinger J., and Gishizky M.L. BCR-ABL-induced oncogenesis is mediated by direct interaction with the SH2 domain of the GRB-2 adaptor protein. Cell 75 (1993) 175-185
70. Prasad G.L., Valverius E.M., McDuffie E., and Cooper H.L. Complementary DNA cloning of a novel epithelial cell marker protein, HME1, that may be down-regulated in neoplastic mammary cells. Cell Growth Differ. 3 (1992) 507-513
71. Pratt W.B., and Welsh M.J. Chaperone functions of the heat shock proteins associated with steroid receptors. Semin. Cell Biol. 5 (1994) 83-93
72. Reuther G.W., Fu H., Cripe L.D., Collier R.J., and Pendergast A.M. Association of the protein kinases cBcr and Bcr-Abl with proteins of the 14-3-3 family. Science 266 (1994) 129-133
73. Ridley A.J., Self A.J., Kasmi F., Paterson H.F., Hall A., Marshall C.J., and Ellis C. Rho family GTPase activating proteins p 190, bcr, and rhoGAP show distinct specificites in vitro and in vivo. EMBO J. 12 (1993) 5151-5160
74. Robinson K., Jones D., Patel Y., Martin H., Madrazo J., Martin S., Howell S., Elmore M., Finnen M.J., and Aitken A. Mechanism of inhibition of protein kinase C by 14-3-3 isoforms. Biochem. J. 299 (1994) 853-861
75. Ron D., Zannini M., Levis M., Wickner R.B., Hunt L.T., Graziani G., Tronick S.R., Aaronson S.A., and Eva A. A region of proto-dbl essential for its transforming activity shows sequence similarity to a yeast cell cycle gene, CDC 24, and the human breakpoint cluster gene. bcr. New Biol. 3 (1991) 372-379
76. Roth D., Morgan A., and Burgoyne R.D. Identification of a key domain in annexin and 14-3-3 proteins that stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells. FEBS Lett. 320 (1993) 207-210
77. Roth D., Morgan A., Martin H., Jones D., Martens G.J.M., Aitken A., and Burgoyne R.D. Characterization of 14-3-3 proteins in adrenal chromaffin cells and demonstration of isoform-specific phospholipid binding. Biochem. J. 301 (1994) 305-310
78. Sakariassen K.S., Bolhuis P.A., and Sixma J.J. Human blood platelet adhesion to artery subendothelium. Nature (London) 279 (1979) 636-638
79. Sarafian T., Aunis D., and Bader M.F. Loss of proteins from digitonin-permeabilized adrenal chromaffin cells essential for exocytosis. J. Biol. Chem. 262 (1987) 16671-16676
80. Shimizu K., Kuroda S., Yamamori B., Matsuda S., Kaibuchi K., Yamauchi T., Isobe T., Irie K., Matsumoto K., and Takai Y. Synergistic activation by Ras and 14-3-3 protein of a mitogen-activated protein kinase kinase kinase named Ras-dependent extracellular signal-regulated kinase kinase stimulator. J. Biol. Chem. 269 (1994) 22917-22920
81. Stokoe D., Macdonald S.G., Cadwallader K., Symons M., and Hancock J.F. Activation of Raf as a result of recruitment to the plasma membrane. Science 264 (1994) 1463-1467
82. Sutherland C., Alterio J., Campbell D.G., Le Bourdelles B., Mallet J., Haavik J., and Cohen P. Phosphorylation and activation of human tyrosine hydroxylase in vitro by mitogen-activated protein (MAP) kinase and MAP-kinase activated kinases 1 and 2. Eur. J. Biochem. 217 (1993) 715-722
83. Swanson K.D., and Ganguly R. Characterization of a Drosophila melanogaster gene similar to the mammalian genes encoding the tyrosine/tryptophan hydroxylase activator and protein kinase C inhibitor proteins. Gene 113 (1992) 183-190
84. Szyszka R., Kramer G., and Hardesty B. The phosphorylation state of the reticulocyte 90-kDa heat shock protein affects its ability to increase phosphorylation of peptide initiation factor 2 α subunits by the heme-sensitive kinase. Biochemistry 28 (1989) 1435-1438
85. Tanji M., Horwitz R., Rosenfeld G., and Waymire J.C. Activation of protein kinase C by purified bovine brain 14-3-3: Comparison with tyrosine hydroxylase activation. J. Neurochem. 63 (1994) 1908-1916
86. Toker A., Ellis C.A., Sellers L.A., and Aitken A. Protein kinase C inhibitor proteins. Eur. J. Biochem. 191 (1990) 421-429
87. Toker A., Sellers L.A., Amess B., Patel Y., Harris A., and Aitken A. Multiple isoforms of a protein kinase C inhibitor (KCIP/14-3-3) from sheep brain. Eur. J. Biochem. 206 (1992) 453-461
88. van Heusden G.P.H., Wenzel T.J., Lagendijk E.L., de Steensma H.Y., and van den Berg J.A. Characterization of the yeast BMH1 gene encoding a putative protein homologous to mammalian protein kinase II activators and protein kinase C inhibitors. FEBS Lett. 302 (1992) 145-150
89. van Heusden G.P.H., Griffiths D.J.F., Ford J.C., Chin-A-Woeng T.F.C., Schrader P.A.T., Carr A.M., and de Steensma H.Y. The 14-3-3 proteins encoded by the BMH1 and BMH2 genes are essential in the yeast Saccharomyces cerevisiae and can be replaced by a plant homologue. Eur. J. Biochem. 229 (1995) 45-53
90. Voncken J.W., van Schaick H., Kaartinen V., Deemer K., Coates T., Landing B., Pattengale P., Dorseuil O., Bokoch G.M., Groffen J., and Heisterkamp N. Increased neutrophil respiratory burst in bcr-null mutants. Cell 80 (1995) 719-728
91. Wang W., and Shakes D.C. Isolation and sequence analysis of a Caenorhabditis elegans cDNA which encodes a 14-3-3 homologue. Gene 147 (1994) 215-218
92. Wartmann M., and Davis R.J. The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex. J. Biol. Chem. 269 (1994) 6695-6701
93. Wu Y.N., Vu N.D., and Wagner P.D. Anti-(14-3-3 protein) antibody inhibits stimulation of noradrenaline (norepinephrine) secretion by chromaffin-cell cytosolic proteins. Biochem. J. 285 (1992) 697-700
94. Xiao B., Smerdon S.J., Jones D.H., Dodson G.G., Soneji Y., Aitken A., and Gamblin S.J. Structure of a 14-3-3 protein and implications for coordination of multiple signaling pathways. Nature (London) 376 (1995) 188-191
95. Yamamori B., Kuroda S., Shimizu K., Fukui K., Ohtsuka T., and Takai Y. Purification of a Ras-dependent mitogen-activated protein kinase kinase kinase from bovine brain cytosol and its identification as a complex of B-Raf and 14-3-3 proteins. J. Biol. Chem. 270 (1995) 11723-11726
96. Yamauchi T., Nakata H., and Fujisawa H. A new activator protein that activates tryptophan 5-monooxygenase and tyrosine 3-monooxygenase in the presence of Ca2+-calmodulin-dependent protein kinase. J. Biol. Chem. 256 (1981) 5404-5409
97. Zupan L.A., Steffens D.L., Berry C.A., Landt M., and Gross R.W. Cloning and expression of a human 14-3-3 protein mediating phospholipolysis. J. Biol. Chem. 267 (1992) 8707-8710