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Mechanisms of Growth Factor-Mediated Signal Transduction in PC12 Cells

  • Chapter
Genetic Mechanisms in Multiple Endocrine Neoplasia Type 2

Part of the book series: Medical Intelligence Unit ((MIU.LANDES))

Abstract

One of the most important and pressing issues in developmental neurobiology is understanding how neurons are generated from uncommitted precursor populations and how they acquire the specific phenotypic characters which distinguish them as mature neurons. As described in chapter 5, there has been substantial progress in understanding the complex intercellular relationships and the role of neurotrophins and other growth factors during nervous system development. These studies have relied principally on the use of in vivo models and primary tissue culture systems. While illuminating, these studies are of limited utility in the investigation of the intracellular, biochemical mechanisms subserving the actions of growth factors that direct the differentiation of these precursor cells into neurons. These populations of precursor cells are reliant upon growth factors for their survival, and this dependency confounds the design of experiments to explore the mechanism of the growth factors actions. Moreover, the limited amount of material available for study and the absence of appropriate control populations of cells has impeded the progress in elucidating the cellular mechanisms responsible for the effects of growth factors.

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References

  1. Greene LA, Tischler AS. Establishment of a noradrenergic clonal cell line of rat phaeochromocytoma cells that respond to nerve growth factor. Proc Natl Acad Sci USA 1976; 73: 2424–28.

    Article  PubMed  CAS  Google Scholar 

  2. Burstein DE, Greene LA. Evidence for RNA synthesis-dependent, and-independent pathways in the stimulation of neurite outgrowth by nerve growth factor. J Cell Biol 1978; 75: 6059–63.

    CAS  Google Scholar 

  3. Greene L, Aletta J, Rukenstein A et al. PC12 pheochromocytoma cells: Culture, NGF treatment and experimental exploitation. Meth Enzymol 1987; 147: 207–16.

    Article  PubMed  CAS  Google Scholar 

  4. Mesner PW, Winters TR, Green SH. Nerve growth factor withdrawal-induced cell death in neuronal PC12 cells resembles that in sympathetic neurons. J Cell Biol 1992; 119: 1669–80.

    Article  PubMed  CAS  Google Scholar 

  5. Chao M. Growth factor signaling: where is the specificity? Cell 1992; 68: 995–1007.

    Article  PubMed  CAS  Google Scholar 

  6. Wood K, Roberts T. Oncogenes and protein kinases in neuronal growth factor action. Biochem Biophys Acta 1993; 1155: 133–50.

    PubMed  CAS  Google Scholar 

  7. Raffioni S, Bradshaw R, Buxser S. The receptors for nerve growth factor and other neurotrophins. Ann Rev Biochem 1993; 62: 823–50.

    Article  PubMed  CAS  Google Scholar 

  8. Bothwell M. Keeping track of neurotrophin receptors. Cell 1991; 65: 915–18.

    Article  PubMed  CAS  Google Scholar 

  9. Chao M. Neurotrophin receptors: A window into neuronal differentiation. Neuron 1992; 9: 583–93.

    Article  PubMed  CAS  Google Scholar 

  10. Johnson D, Lanahan A, Buck CR et al. Expression and structure of the human NGF receptor. Cell 1986; 47: 545–54.

    Article  PubMed  CAS  Google Scholar 

  11. Radeke M, Misco T, Hsu C et al. Gene transfer and molecular cloning of the rat nerve growth factor receptor. Nature 1987; 325: 593–97.

    Article  PubMed  CAS  Google Scholar 

  12. Rodriguez-Tebar A, Dechant G, Barde Y. Binding of brain-derived neurotrophic factor to the nerve growth factor receptor. Neuron 1990; 4: 487–92.

    Article  PubMed  CAS  Google Scholar 

  13. Rabizadeh S, Oh J, Zhong L et al. Induction of apoptosis by the low affinity NGF receptor. Science 1993; 261: 345–48.

    Article  PubMed  CAS  Google Scholar 

  14. Dobrowsky RT, Werner MH, Castillino AM et al. Activation of the sphingomyelin cycle through the low affinity neurotrophin receptor. Science 1994; 265: 1596–98.

    Article  PubMed  CAS  Google Scholar 

  15. Hempstead B, Martin-Zanca D, Kaplan D et al. High affinity NGF binding requires coexpression of the trk proto-oncogene and the low affinity NGF receptor. Nature 1991; 678–83.

    Google Scholar 

  16. Jing S, Tapley P, Barbacid M. Nerve growth factor mediates signal transduction through trk homodimer formation. Neuron 1992; 9: 1067–79.

    Article  PubMed  CAS  Google Scholar 

  17. Kaplan D, Hempstead B Martin-Zanca D et al. The trk proto-oncogene product: a signal transducing receptor for nerve growth factor. Science 1991; 252: 554–58.

    Article  PubMed  CAS  Google Scholar 

  18. Kaplan D, Martin-Zanca D, Parada L. Tyrosine phosphorylation and tyrosine kinase activity of the trk proto-oncogene product induced by NGF. Nature 1991; 350: 158–60.

    Article  PubMed  CAS  Google Scholar 

  19. Klein R, Jing S, Nanduri V et al. The trk proto-oncogene encodes a receptor for NGF. Cell 1991; 65: 189–97.

    Article  PubMed  CAS  Google Scholar 

  20. Nebreda AR, Martin-Zanca D, Kaplan DR et al. Induction by NGF of meiotic maturation of Xenopus oocytes expressing the trk proto-oncogene product. Science 1991; 252: 558–61.

    Article  PubMed  CAS  Google Scholar 

  21. Barbacid M, Lamballe F, Pulido D et al. The trk family of tyrosine protein kinase receptors. Biochim Biophys Acta 1991; 1072: 115–27.

    PubMed  CAS  Google Scholar 

  22. Lee K, Li E, Huber J et al. Targeted mutation of the gene encoding the low affinity NGF receptor p75 leads to deficits in the peripheral sensory nervous system. Cell 1992; 69: 737–49.

    Article  PubMed  CAS  Google Scholar 

  23. Loeb DM, Maragos J, Martin-Zanca D et al. The trk proto-oncogene rescues NGF responsiveness in mutant NGF-nonresponsive PC12 cell lines. Cell 1991; 66: 961–66.

    Article  PubMed  CAS  Google Scholar 

  24. Klein R, Nanduri V, Jing S et al. The trkB tyrosine protein kinase is a receptor for brain derived neurotrophic factor and neurotrophin 3. Cell 1991; 66: 395–403.

    Article  PubMed  CAS  Google Scholar 

  25. Lamballe F, Klein R, Barbacid M. TrkC, a new member of the trk family of tyrosine protein kinases, is a receptor for neurotrophin 3. Cell 1991; 66: 967–79.

    Article  PubMed  CAS  Google Scholar 

  26. Berg MM, Sternberg DW, Hempsted BL et al. The low-affinity p75 nerve growth factor receptor mediates NGF-induced tyrosine phosphorylation. Proc Natl Acad Sci USA 1991; 88: 7106–10.

    Article  PubMed  CAS  Google Scholar 

  27. Barker PA, Shooter EM. Disruption of NGF binding to the low affinity neurotrophin receptor p75LNTR reduces NGF binding to trkA on PC12 cells. Neuron 1994; 18: 203–15.

    Article  Google Scholar 

  28. Hantzopoulos PA, Suri C, Glass DJ et al. The low affinity NGF receptor, p75, can collaborate with each of the trks to potentiate functional responses to the neurotrophins. Neuron 1994; 18: 187–201.

    Article  Google Scholar 

  29. Rovelli G, Heller RA, Canossa M et al. Chimeric tumor necrosis factor-TrkA receptors reveal that ligand-dependent activation of the trkA tyrosine kinase is sufficient for differentiation and survival of PC12 cells. Proc Natl Acad Sci USA 1993; 90: 8717–21.

    Article  PubMed  CAS  Google Scholar 

  30. Koch A, Anderson D, Moran M et al. SH2 and SH3 domains: Elements that control interactions of cytoplasmic signaling proteins. Science 1991; 252: 668–74.

    Article  PubMed  CAS  Google Scholar 

  31. Songyang Z, Shoelson S, Chaudhuri M et al. SH2 domains recognize specific phosphopeptide sequences. Cell 1993; 72: 767–78.

    Article  PubMed  CAS  Google Scholar 

  32. Pawson T. Protein modules and signalling networks. Nature 1995; 373: 573–80.

    Article  PubMed  CAS  Google Scholar 

  33. Soltoff S, Rabin S, Cantley L et al. Nerve growth factor promotes the activation of phosphatidylinositol 3-kinase and its association with the trk tyrosine kinase. J Biol Chem 1992; 267: 17472–77.

    PubMed  CAS  Google Scholar 

  34. Obermeier A, Halfter H, Wiesmuller K et al. Tyrosine 785 is a major determinant of Trk-substrate interaction. EMBO J 1993; 12: 933–41.

    PubMed  CAS  Google Scholar 

  35. Obermeier A, Lammers R, Wiesmuller K et al. Identification of trk binding sites for shc and phosphatidylinositol 3’-kinase and formation of a multimeric signaling complex. J Biol Chem 1993; 268: 22963–66.

    PubMed  CAS  Google Scholar 

  36. Vetter M, Martin-Zanca D, Parada L et al. NGF rapidly stimulates tyrosine phosphorylation of phospholipase C gamma by a kinase activity associated with the product of the trk protooncogene. Proc Natl Acad Sci USA 1991; 88: 5650–4.

    Article  PubMed  CAS  Google Scholar 

  37. Chung J, Grammer TC, Lemon KP et al. PDGF- and insulin-dependent pp70S6K activation mediated by phosphatidylinositol-3OH kinase. Nature 1994; 370: 71–75.

    Article  PubMed  CAS  Google Scholar 

  38. Chung J, Kuo C, Crabtree G et al. Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases. Cell 1992; 69: 1227–36.

    Article  PubMed  CAS  Google Scholar 

  39. Calvin J, Jonkyeong C, Fiorentino W et al. Rapamycin selectively inhibits interleukin-2 activation of p70 S6 kinase. Nature 1992; 358: 70–73.

    Article  Google Scholar 

  40. Basu T, Warne PH, Downward J. Role of Shc in the activation of Ras in response to epidermal growth factor and nerve growth factor. Oncogene 1994; 9: 3483–91.

    PubMed  CAS  Google Scholar 

  41. Ohmichi M, Matuoka K, Takenawa T et al. Growth factors differentially stimulate the phosphorylation of Shc proteins and their association with Grb2 in PC12 pheochromocytoma cells. J Biol Chem 1994; 269: 1143–48.

    PubMed  CAS  Google Scholar 

  42. Ravichandran KS, Lorenz U, Shoelson SE et al. Interaction of Shc with Grb2 regulates association of Grb2 with mSos. Mol Cell Biol 1995; 15: 593–600.

    PubMed  CAS  Google Scholar 

  43. Rozakis-Adcock M, McGlade J, Mbamalu G et al. Association of the shc and Grb2/Sem56 Sh2-containing proteins is implicated in activation of the ras pathway by tyrosine kinases. Nature 1992; 360: 689–91.

    Article  PubMed  CAS  Google Scholar 

  44. Skolnik EY, Lee CH, Batzer A et al. The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS 1 and Shc: implications for insulin control of ras signalling. EMBO J 1993; 12: 1929–36.

    PubMed  CAS  Google Scholar 

  45. Egan SE, Giddings BW, Brooks MW et al. Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation. Nature 1993; 363: 45–51.

    Article  PubMed  CAS  Google Scholar 

  46. Buday L, Downward J. Epidermal growth factor regulates p21 ras through the formation of a complex of receptor, grb2 adaptor protein and sos nucleotide exchange factor. Cell 1993; 73: 611–20.

    Article  PubMed  CAS  Google Scholar 

  47. Li N, Daly R, Yajnik V et al. Guanine nucleotide releasing factor hSosl binds to Grb2 and links receptor tyrosine kinases to Ras signalling. Nature 1993; 363: 85–87.

    Article  PubMed  CAS  Google Scholar 

  48. Chardin P, Camonis J, Gale N et al. Human Sosl: a guanine nucleotide exchange factor for ras that binds to grb2. Science 1993; 260: 1338–43.

    Article  PubMed  CAS  Google Scholar 

  49. Boguski M, McCormick F. Proteins regulating ras and its relatives. Nature 1993; 366: 643–54.

    Article  PubMed  CAS  Google Scholar 

  50. Bollag G, McCormick F. Regulators and effectors of ras proteins. Ann Rev Cell Biol 1991; 7: 601–32.

    Article  PubMed  CAS  Google Scholar 

  51. Obermeier A, Bradshaw RA, Seedorf K et al. Neuronal differentiation signals are controlled by nerve growth factor receptor/Trk binding sites for SHC and PLC-gamma. EMBO J 1994; 13: 1585–90.

    PubMed  CAS  Google Scholar 

  52. Blenis J. Signal transduction via the MAP kinases: proceed at your own RSK. Proc Natl Acad Sci USA 1993; 90: 5889–92.

    Article  PubMed  CAS  Google Scholar 

  53. de Vries-Smits AMM, Burgering BMT, Leevers SJ et al. Involvement of p2iras in activation of extracellular signal-regulated kinase 2. Nature 1992; 357: 602–4.

    Article  PubMed  Google Scholar 

  54. Alema S, Casalbore P, Agostini E et al. Differentiation of PC12 pheochromocytoma cells induced by v-src oncogene. Nature 1985; 316: 557–9.

    Article  PubMed  CAS  Google Scholar 

  55. Kremer N, D’Arcangelo G, Thomas S et al. Signal transduction by NGF and FGF in PC12 cells requires a sequence of src and ras actions. J Cell Biol 1991; 115: 809–19.

    Article  PubMed  CAS  Google Scholar 

  56. Feig LA, Cooper GM. Inhibition of NIH3T3 cell proliferation by a mutant ras protein with preferential affinity of GDP. Mol Cell Biol 1988; 8: 3235–43.

    PubMed  CAS  Google Scholar 

  57. Szeberenyi J, Cai H, Cooper G. Effect of a dominant inhibitory Ha-ras mutation on neuronal differentiation of PC12 cells. Mol Cell Biol 1990; 10: 5324–32.

    PubMed  CAS  Google Scholar 

  58. Bar-Sagi D, Feramisco JR. Microinjection of the ras oncogene protein into PC12 cells induces morphological differentiation. Cell 1985; 42: 841–48.

    Article  PubMed  CAS  Google Scholar 

  59. Thomas S, DeMarco M, D’Arcangelo G et al. Ras is essential for NGF- and phorbol ester-induced tyrosine phosphorylation of MAP kinases. Cell 1992; 68: 1031–40.

    Article  PubMed  CAS  Google Scholar 

  60. Wood K, Sarnecki C, Roberts T et al. Ras mediates NGF receptor modulation of three transducing protein kinases: MAP kinase, Raf1 and RSK. Cell 1992; 68: 1041–50.

    Article  PubMed  CAS  Google Scholar 

  61. D’Arcangelo G, Halegoua SAA. Branched signaling pathway for nerve growth factor is revealed by src, ras and raf-mediated gene inductions. Mol Cell Biol 1993; 13: 3146–55.

    PubMed  Google Scholar 

  62. Crews CM, Alessandrini A, Erikson R. ERKs: Their fifteen minutes has arrived. Cell Growth and Diff 1992; 3: 135–42.

    CAS  Google Scholar 

  63. Davis R. The mitogen activated protein kinase signal transduction pathway. J Biol Chem 1993; 268: 14553–56.

    PubMed  CAS  Google Scholar 

  64. Van Aelst L, Barr M, Marcus S et al. Complex formation between Ras and Raf and other protein kinases. Proc Natl Acad Sci USA 1993; 90: 6213–17.

    Article  PubMed  Google Scholar 

  65. Moodie S, Willumsen B, Weber M et al. Complexes of ras-GTP with raf-1 and mitogen activated protein kinase kinase. Science 1993; 260: 1658–61.

    Article  PubMed  CAS  Google Scholar 

  66. Vojtek A, Hollenberg S, Cooper J. Mammalian ras interacts directly with the serine/threonine kinase raf. Cell 1993; 74: 205–14.

    Article  PubMed  CAS  Google Scholar 

  67. Troppmair J, Bruder J, App H et al. Ras controls coupling of growth factor receptors and protein kinase C in the membrane to Raf-1 and B-raf protein serine kinases in the cytosol. Oncogene 1992; 7: 1867–73.

    PubMed  CAS  Google Scholar 

  68. Koide H, Satoh T, Nakafuku M et al. GTP-dependent association of Raf-1 with Ha-ras: Identification of Raf as a target downstream of Ras in mammalian cells. Proc Natl Acad Sci USA 1993; 90: 8683–86.

    Article  PubMed  CAS  Google Scholar 

  69. Jaiswal R, Moodie S, Wolfman A et al. The mitogen activated protein kinase cascade is activated by B-raf in NGF-treated PC12 cell through interaction with p2lras. Mol Cell Biol 1994; 14: 6944–53.

    PubMed  CAS  Google Scholar 

  70. Jelinek T, Catling AD, Reuter CW et al. Ras and Raf-1 form a signaling complex with Mek-1 but not Mek-2. Mol Cell Biol 1994; 14: 8212–18.

    PubMed  CAS  Google Scholar 

  71. Moodie SA, Paris MJ, Kolch W et al. Association of MEK1 with p21RAS-GMPPNP is dependent on B-Raf. Mol Cell Biol 1994; 14: 7153–62.

    PubMed  CAS  Google Scholar 

  72. Warne P, Viciana P, Downward J. Direct interaction of ras and the amino-terminal region of raf-1 in vitro. Nature 1993; 364: 352–55.

    Article  PubMed  CAS  Google Scholar 

  73. Leevers SJ, Paterson HF, Marshall CJ. Requirement for ras in the raf activation is overcome by targeting raf to the plasma membrane. Nature 1994; 369: 411–14.

    Article  PubMed  CAS  Google Scholar 

  74. Stokoe D, Macdonald SG, Cadwallader K et al. Activation of Raf as a result of recruitment to the plasma membrane. Science 1994; 264: 1413–14.

    Article  Google Scholar 

  75. Rapp U, Heidecker G, Huleihel M et al. Raf family serine/threonine protein kinases in mitogen signal transduction. Cold Spring Harbor Symp Quant Biol 1988; 53: 173–84.

    Article  PubMed  CAS  Google Scholar 

  76. Howe L, Leevers S, Gomez N et al. Activation of the MAP kinase pathway by the protein kinase raf. Cell 1992; 71: 335–42.

    Article  PubMed  CAS  Google Scholar 

  77. Kyriakis J, App H, Zhang XF et al. Raf-1 activates MAP kinase kinase. Nature 1992; 358: 417–21.

    Article  PubMed  CAS  Google Scholar 

  78. McDonald S, Crews C, Wu L et al. Reconstitution of the Raf-1MEK-ERK signal transduction pathway in vitro. Mol Cell Biol 1993; 13: 6615–20.

    Google Scholar 

  79. Vaillancourt RR, Gardner AM, Johnson GL. B-raf-dependent regulation of the MEK-1/mitogen-activated protein kinase pathway in PC12 cells and regulation by cyclic AMP. Mol Cell Biol 1994; 14: 6522–30.

    PubMed  CAS  Google Scholar 

  80. Huang W, Alessandrini A, Crews C et al. Raf-1 forms a stable complex with MEK1 and activates MEK1 by serine phosphorylation. Proc Natl Acad Sci USA 1993; 90: 10947–51.

    Article  PubMed  CAS  Google Scholar 

  81. Ahn N, Seger R, Krebs E. The mitogen activated protein kinase activator. Curr Opin Cell Biol 1992; 4: 992–9.

    Article  PubMed  CAS  Google Scholar 

  82. Blenis J, Chung J, Erikson E et al. Distinct mechanisms for the activation of the rsk kinases MAP2 kinase pp90rsk, and pp70s6k signaling systems are indicated by inhibition of protein synthesis. Cell Growth and Diff 1991; 2: 279–85.

    CAS  Google Scholar 

  83. Chung J, Pelech S, Blenis J. Mitogen-activated Swiss mouse 3T3 RSK kinases I and II are related to pp44mpk from sea star oocytes and participate in the regulation of pp90rsk activity. Proc Natl Acad Sci USA 1991; 88: 4981–5.

    Article  PubMed  CAS  Google Scholar 

  84. Grove JR, Price DJ, Banerjee P et al. Regulation of an EpitopeTagged Recombinant Rsk-1 S6 Kinase by Phorbol Ester and erk/MAP Kinase. Biochemistry 1993; 32: 7727–38.

    Article  PubMed  CAS  Google Scholar 

  85. Chen R, Sarnecki C, Blenis J. Nuclear localization and regulation of erk and rsk encoded protein kinases. Mol Cell Biol 1992; 12: 915–27.

    PubMed  CAS  Google Scholar 

  86. Lenormand P, Sardet C, Pages G et al. Growth factors induce nuclear translocation of MAP kinases but not of their activator Map kinase kinase in fibroblasts. J Cell Biol 1993; 122: 1079–88.

    Article  PubMed  CAS  Google Scholar 

  87. Seth A, Gonzales F, Gupta S et al. Signal transduction within the nucleus by mitogen actived protein kinase. J Biol Chem 1992; 267: 24796–806.

    PubMed  CAS  Google Scholar 

  88. Oshima M, Sithanandam G, Rapp UR et al. The phosphorylation and activation of B-raf in PC12 cells stimulated by nerve growth factor. J Biol Chem 1991; 266: 23753–60.

    PubMed  CAS  Google Scholar 

  89. Stephens RM, Sithanandam G, Copeland TD et al. 95-kilodalton B-Raf serine/threonine kinase: identification of the protein and its major autophosphorylation site. Mol Cell Biol 1992; 12: 3733–42.

    PubMed  CAS  Google Scholar 

  90. Wu J, Dent P, Jelinek T et al. Inhibition of the EGF-activated MAP kinase signaling pathway by adenosine 3’,5’-monophosphate. Science 1993; 262: 1065–8.

    Article  PubMed  CAS  Google Scholar 

  91. Cook SJ, McCormick F. Inhibition by cAMP of Ras-dependent activation of Raf. Science 1993; 262: 1069–72.

    Article  PubMed  CAS  Google Scholar 

  92. Wartmann M, Davis M. The native structure of the activated raf protein kinase is a membrane-bound multi-subunit complex. J Biol Chem 1994; 269: 6695–701.

    PubMed  CAS  Google Scholar 

  93. Peraldi P, Frodin M, Barnier JV et al. Regulation of the MAP kinase cascade in PC12 cells: B-Raf activates MEK-1 (MAP kinase or ERK kinase) and is inhibited by cAMP. FEBS Letters 1995; 357: 290–6.

    Article  PubMed  CAS  Google Scholar 

  94. Young SW, Dickens M, Tavare JM. Differentiation of PC12 cells in response to a cAMP analogue is accompanied by sustained activation of mitogen-activated protein kinase. FEBS Letters 1994; 338: 212–6.

    Article  PubMed  CAS  Google Scholar 

  95. Marshall CJ. Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation. Cell 1995; 80: 179–85.

    CAS  Google Scholar 

  96. Cowley S, Paterson H, Kemp P et al. Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH3T3 cells. Cell 1994; 77: 841–52.

    Article  PubMed  CAS  Google Scholar 

  97. Kyriakis JM, Banerjee P, Nikolakaki E et al. The stress-activated protein kinase subfamily of c-Jun kinases. Nature 1994; 369: 156–60.

    Article  PubMed  CAS  Google Scholar 

  98. Lange-Carter C, Pleiman C, Gardner A et al. A divergence in the MAP kinase regulatory network defined by MEK kinase and raf. Science 1993; 260: 315–9.

    Article  PubMed  CAS  Google Scholar 

  99. Yan M, Dai T, Deak JC et al. Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1. Nature 1994; 372: 798–800.

    PubMed  CAS  Google Scholar 

  100. Sanchez I, Hughes RT, Mayer BJ et al. Role of SAP/ERK kinase-1 in the stress-activated pathway regulating transcription factor c-Jun. Nature 1994; 372: 794–8.

    PubMed  CAS  Google Scholar 

  101. Lange-Carter CA, Johnson GL. Ras-dependent growth factor regulation of MEK kinase in PC12 cells. Science 1994; 265: 1458–61.

    Article  PubMed  CAS  Google Scholar 

  102. Rouse J, Cohen P, Trigon S et al. A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins. Cell 1994; 78: 1027–37.

    Article  PubMed  CAS  Google Scholar 

  103. Derijard B, Raingeaud J, Barrett T et al. Independent human MAP kinase signal transduction pathways defined by MEK and MKK isoforms. Science 1995; 267: 682–5.

    Article  PubMed  CAS  Google Scholar 

  104. Stokoe D, Campbell DG, Nakielny S et al. MAPKAP kinase-2; a novel protein kinase activated by mitogen-activated protein kinase. EMBO J 1992; 11: 3985–94.

    PubMed  CAS  Google Scholar 

  105. Shimizu K, Kuroda S, Yamamori B et al. Synergistic activation by RAS and 14–3–3 protein of a mitogen–activated protein kinase kinase kinase. J Biol Chem 1994; 269: 22917 – 20.

    PubMed  CAS  Google Scholar 

  106. Curran T, Morgan J. Superinduction of fos by NGF in the pres-ence of peripherally active benzodiazepines. Science 1985; 229: 1265–8.

    Article  PubMed  CAS  Google Scholar 

  107. Distel RJ, Speigelman BM. Proto-oncogene c-fos as a transcription factor. Advances in Cancer Research 1990; 55: 37–55.

    Article  PubMed  CAS  Google Scholar 

  108. Graham R, Gilman M. Distinct protein targets for signals acting at the c-Fos serum response element. Science 1991; 251: 189–92.

    Article  PubMed  CAS  Google Scholar 

  109. Gizang-Ginsberg E, Ziff E. Nerve growth factor regulates tyrosine hydroxylase gene transcription through a nucleoprotein complex that contains c-fos. Genes Dev 1990; 4: 477–91.

    Article  PubMed  CAS  Google Scholar 

  110. Lucibello FC, Neuberg M, Hunter JB et al. Transactivation of gene expression by fos protein: Involvement of a binding site for the transcription factor AP-1. Oncogene 1988; 3: 43–51.

    CAS  Google Scholar 

  111. Milbrandt J. Nerve growth factor rapidly induces c-fos in PC12 cells. Proc Natl Acad Sci USA 1986; 83: 4789–93.

    Article  PubMed  CAS  Google Scholar 

  112. Kruijer W, Schubert D, Verma IM. Induction of the proto-oncogene fos by nerve growth factor. Proc Nat Acad Sci. USA 1985; 82: 7330–4.

    Article  CAS  Google Scholar 

  113. Bartel D, Sheng M, Lau L et al. Growth factors and membrane depolarization activate distinct programs of early response gene expression: dissociation of fos and jun induction. Genes Dev 1989; 3: 304–13.

    Article  PubMed  CAS  Google Scholar 

  114. Curran T, Morgan J. Barium modulates c-fos expression and post-translational modification. Proc Natl Acad Sci USA 1986; 83: 8521–4.

    Article  PubMed  CAS  Google Scholar 

  115. Sheng M, Dougan ST, McFadden G et al. Calcium and growth factor pathways of c-fos transcriptional activation require distinct upstream regulatory sequences. Mol Cell Biol 1988; 8: 2787–96.

    PubMed  CAS  Google Scholar 

  116. Treisman R Transient accumulation of c-fos RNA following serum stimulation requires a conserved 5’ element and c-fos 3’ sequences. Cell 1985; 42: 889–902.

    Article  Google Scholar 

  117. Robertson LM, Kerppola TK, Vendril M et al. Regulation of c-fos expression in transgenic mice requires multiple interdependent transcription control elements. Neuron 1995; 14: 241–52.

    Article  PubMed  CAS  Google Scholar 

  118. Treisman R. Identification of a protein-binding site that mediates transcriptional response of the c-fos gene to serum factors. Cell 1986; 46: 567–74.

    Article  Google Scholar 

  119. Hill CS, Marais R, John S et al. Functional analysis of a growth factor-responsive transcription factor complex. Cell 1993; 73: 395–406.

    Article  PubMed  CAS  Google Scholar 

  120. Shaw PE, Schroter H, Nordheim A. The ability of a ternary complex to form over the serum response element correlates with serum inducibility of the human c-fos promoter. Cell 1989; 56: 563–72.

    Article  PubMed  CAS  Google Scholar 

  121. Hipskind R, Rao V, Mueller G et al. Ets-related protein Elk-1 is homologous to the c-Fos regulatory factor p62tcf. Nature 1991; 354: 531–4.

    Article  PubMed  CAS  Google Scholar 

  122. Rivera VM, Miranti CK, Misra RP et al. A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity. Mol Cell Biol 1993; 13: 6260–73.

    PubMed  CAS  Google Scholar 

  123. Marais R, Wynne J, Treisman R. The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain. Cell 1993; 73: 381–93.

    Article  PubMed  CAS  Google Scholar 

  124. Gille H, Sharrocks A, Shaw P. Phosphorylation of transcription factor p62tcf by MAP kinase stimulates ternary complex formation at the c-fos promoter. Nature 1992; 358: 414–7.

    Article  PubMed  CAS  Google Scholar 

  125. Misra V, Rivera V, Wang J et al. The serum response factor is extensively modified by phosphorylation following its synthesis in serum-stimulated fibroblasts. Mol Cell Biol 1991; 11: 4545–54.

    PubMed  CAS  Google Scholar 

  126. Ginty DD, Bonni A, Greenberg ME. Nerve growth factor activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB. Cell 1994; 77: 713–25.

    Article  PubMed  Google Scholar 

  127. Sheng M, McFadden G, Greenberg ME. Membrane depolarization and calcium induce c-fos transcription via phosphorylation of transcription factor CREB. Neuron 1990; 4: 571–82.

    Article  PubMed  CAS  Google Scholar 

  128. Gonzales GA, Montminy MR. Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133. Cell 1989; 59: 675–80.

    Article  Google Scholar 

  129. Kwok RS, Lundblad JR, Chrivia JC et al. Nuclear protein CBP is a coactivator for the transcription factor CREB. Nature 1994; 370: 223–6.

    Article  PubMed  CAS  Google Scholar 

  130. Chrivia JC, Kwok RP, Lamb N et al. Phosphorylated CREB binds specifically to the nuclear protein CBP. Nature 1993; 365: 855–9.

    Article  PubMed  CAS  Google Scholar 

  131. Arias J, Alberts AS, Brindle P et al. Activation of cAMP and mito-gen responsive genes relies on a common nuclear factor. Nature 1994; 370: 226–9.

    Article  PubMed  CAS  Google Scholar 

  132. Wagner BJ, Hayes TE, Hoban CJ et al. The SIF binding element confers sis/PDGF inducibility onto the c-fos promoter. EMBO J 1990; 9: 4477–84.

    PubMed  CAS  Google Scholar 

  133. Darnell JE, Kerr IM, Stark GR. Jak-STAT pathways and transcriptional regulation in response to IFNs and other extracellular signaling proteins. Science 1994; 264: 1415–21.

    Article  PubMed  CAS  Google Scholar 

  134. Ihle JN, Witthuhn BA, Quelle FW et al. Signaling by the cytokine receptor superfamily: JAKs and STATs. Trends Biol Sci 1994; 19: 222–7.

    Article  CAS  Google Scholar 

  135. Fu XY, Zhang JJ. Transcription factor p91 interacts with the epidermal growth factor receptor and mediates activation of the c-fos gene promoter. Cell 1993; 74: 1135–45.

    Article  PubMed  CAS  Google Scholar 

  136. Hill CS, Treisman R. Transcriptional regulation by extracellular signals: Mechanisms and specificity. Cell 1995; 80: 199–211.

    Article  PubMed  CAS  Google Scholar 

  137. Lucibello F, Lowag C, Neuberg M et al. Trans-repression of the mouse c-Fos promoter: A novel mechanism of Fos-mediated trans-regulation. Cell 1989; 59: 999–1007.

    Article  PubMed  CAS  Google Scholar 

  138. Sassone-Corsi P, Sisson J, Verma I. Transcriptional autoregulation of the proto-oncogene Fos. Nature 1988; 334: 314–9.

    Article  PubMed  CAS  Google Scholar 

  139. Wilson T and Treisman R. Fos C-terminal mutations block down-regulation of c-fos transcription following serum stimulation. EMBO J 1988; 7: 4193–4202.

    PubMed  CAS  Google Scholar 

  140. Ofir R, Dwarki V, Rashid D et al. Phosphorylation of the C terminus of Fos protein is required for transcriptional transrepression of the c-Fos promoter. Nature 1990; 348: 80–2.

    Article  PubMed  CAS  Google Scholar 

  141. Chen R, Abate C, Blenis J. Phosphorylation of the c-Fos transrepressive domain by mitogen activated protein kinase and 90 kDa ribosomal S6 kinase. Proc Natl Acad Sci USA 1993; 90: 10952–56.

    Article  PubMed  CAS  Google Scholar 

  142. Taylor LK, Marshak DR, Landreth GE. Identification of a nerve growth factor-and epidermial growth factor-regulated protein kinase that phosphorylates the protooncogene product c-fos. Proc Natl Acad Sci USA 1993; 90: 368–372.

    Article  PubMed  CAS  Google Scholar 

  143. Nel AE, Taylor LK, Kumar GP et al. Activation of a novel serine/ threonine kinase that phosphorylates c-fos upon stimulation of T and B lymphocytes via antigen and cytokine receptors. J Immunology 1993; 152: 4347–57.

    Google Scholar 

  144. Szeberenyi J, Eberhardt PE. Cellular components of nerve growth factor signaling. Biochim Biophys Acta 1994; 1222: 187–202.

    Article  PubMed  CAS  Google Scholar 

  145. Heasley LE, Johnson GL. The PDGF receptor induces neuronal differentiation of PC12 cells. Mol Biol Cell 1992; 3: 545–53.

    PubMed  CAS  Google Scholar 

  146. Huff K, End D, Guroff G. Nerve growth factor-induced alteration in the response of PC12 pheochromocytoma cells to epidermal growth factor. J Cell Biol 1981; 88: 189–98.

    Article  PubMed  CAS  Google Scholar 

  147. Countaway JL, McQuilkin P, Girones N et al. Multisite phosphorylation of the epidermal growth factor. J Biol Chem 1992; 265: 3407–16.

    Google Scholar 

  148. Qiu M, Green S. NGF and EGF rapidly activate p2lras in PC12 cells by distinct, convergent pathways involving tyrosine phosphorylation. Neuron 1991; 7: 937–46.

    Article  PubMed  CAS  Google Scholar 

  149. Nguyen TT, Scimeca JC, Filloux C et al. Co-regulation of the mitogen-activated protein kinase, extracellular signal-regulated kinase 1, and the 90-kDa S6 kinase in PC12 cells. J Biol Chem 1993; 268: 9803–10.

    PubMed  CAS  Google Scholar 

  150. Traverse S, Gomez N, Paterson H et al. Sustained activation of the mitogen-activated protein (MAP) kinase cascade may be required for differentiation of PC12 cells. Biochem J 1992; 288: 351–5.

    PubMed  CAS  Google Scholar 

  151. Dikic I, Schlessinger J, Lax I. PC12 cells overexpressing the insulin receptor undergo insulin-dependent neuronal differentiation. Curr Biol 1994; 4: 702–8.

    Article  PubMed  CAS  Google Scholar 

  152. Traverse S, Seedorf K, Paterson H et al. EGF triggers the neuronal differentiation of PC12 cells that overexpress the EGF receptor. Curr Biol 1994; 4: 694–701.

    Article  PubMed  CAS  Google Scholar 

  153. Wu CF, Zhang M, Howard BD. K252a potentiates epidermal growth factor-induced differentiation of PC12 cells. J Neurosci 1993; 36: 539–50.

    CAS  Google Scholar 

  154. Gonzalez FA, Seth A, Raden DL et al. Serum-induced translocation of mitogen-activated protein kinase to the cell surface ruffling membrane and the nucleus. J Cell Biol 1993; 122: 1089–101.

    Article  PubMed  CAS  Google Scholar 

  155. Rabin S, Cleghorn V, Kaplan D. SNT, a differentiation specific target of neurotrophic factor induced tyrosine kinase activity in neurons and PC12 cells. Mol Cell Biol 1993; 13: 2203–13.

    PubMed  CAS  Google Scholar 

  156. Heasley LE, Benedict S, Gleavey J et al. Requirement of the adenovirus E1A transformation domain 1 for inhibiton of PC12 cell neuronal differentiation. Cell Regulation 1991; 2: 479–89.

    PubMed  CAS  Google Scholar 

  157. Boulukos KE, Ziff EB. Adenovirus 5 E1A proteins disrupt the neuronal phenotype and growth factor responsiveness of PC12 cells by a conserved region 1-dependent mechanism. Oncogene 1993; 8: 237–48.

    PubMed  CAS  Google Scholar 

  158. Kalman D, Whittaker K, Bishop JM et al. Domains of MA that bind p105Rb, p130, and p300 are required to block nerve growth factor-induced neurite growth in PC12 cells. Mol Biol Cell 1993; 4: 353–61.

    PubMed  CAS  Google Scholar 

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Authors
  1. Michael P. Myers
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  2. Kenneth D. Swanson
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  3. Gary Landreth
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© 1996 Springer-Verlag Berlin Heidelberg

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Myers, M.P., Swanson, K.D., Landreth, G. (1996). Mechanisms of Growth Factor-Mediated Signal Transduction in PC12 Cells. In: Genetic Mechanisms in Multiple Endocrine Neoplasia Type 2. Medical Intelligence Unit. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-21948-5_4

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  • DOI: https://doi.org/10.1007/978-3-662-21948-5_4

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