Mitogen-activated protein kinase cascades and regulation of gene expression

Current Opinion in Immunology

Volumn 8, Issue 3, 1996, Pages 402-411

  Su, Bing ^a   Karin, Michael ^b  

^a UNIVERSITY OF TEXAS   (United States)

^b San Diego   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; CYCLIC AMP; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN KINASE; REGULATOR PROTEIN; TRANSCRIPTION FACTOR;

AMINO TERMINAL SEQUENCE; BIOCHEMISTRY; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVATION; ENZYME SPECIFICITY; GENE EXPRESSION REGULATION; LYMPHOCYTE ACTIVATION; MOLECULAR CLONING; MOLECULAR GENETICS; NONHUMAN; PROTEIN PHOSPHORYLATION; REVIEW; SIGNAL TRANSDUCTION;

EID: 0030175485     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(96)80131-2     Document Type: Article

References (95)

1. Cobb MH, Goldsmith EJ. How MAP kinases are regulated. J Biol Chem. 270:1995;14843-14846.
2. Segar R, Krebs EG. The MAPK signaling cascade. FASEB J. 9:1995;726-735.
3. Boulton TG, Nye SH, Robbins DJ, Ip NY, Radziejewska E, Morgenbesser SD, DePinho RA, Panayotatos N, Cobb MH, Yancopoulos GD. ERK's: a family of protein serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF. Cell. 65:1991;663-675.
4. Ahn NG, Seger R, Bratlien RL, Diltz CD, Tonks NK, Krebs EG. Multiple components in an epidermal growth factor-stimulated protein kinase cascade: in vitro activation of myelin basic protein-1 microtubule-associated protein-2 kinase. J Biol Chem. 266:1991;4220-4227.
5. Derijard BB, Hibi M, Wu IH, Barrett T, Su B, Deng T, Karin M, Davis RJ. JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. of outstanding interest Cell. 76:1994;1025-1027 See annotation [6].
6. Kyriakis JM, Banerjee P, Nikolakaki E, Dai T, Rubie EA, Ahmad MF, Avruch J, Woodgett JR. The stress-activated protein kinase subfamily of c-Jun kinases. of outstanding interest Nature. 369:1994;156-160 These two papers [5,6] describe the molecular cloning of the JNK/SAPK genes, showing that they represent subgroups of MAPKs.
7. Kallunki T, Su B, Sluss HK, Derijard D, Moore G, Davis RJ, Karin M. JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation. of special interest Genes Dev. 8:1994;2996-3007 This paper presents evidence that members of JNK MAPKs have different substrate specificities.
8. Han J, Bibbs L, Ulevitch RJ. A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. of special interest Science. 265:1994;808-811 See annotation [9].
9. Lee JC, Laydon JT, McDonnel PC, Gallagher TF, Kumar S, Green D, McNulty D, Blumenthal MJ, Heys JR, Landvatter SW. A protein kinase involved in the regulation of inflammatory cytokine biosynthesis. of special interest Nature. 372:1994;739-746 These two papers [8,9] describe the molecular cloning of the murine and human p38 MAPK.
10. Freshney NW, Rawlinson L, Guesdon F, Jones E, Cowley S, Hsuan J, Saklatvala J. Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of Hsp27. Cell. 78:1995;1039-1049.
11. Rouse J, Cohen P, Trigon S, Morange M, Alonso-Llamazares A, Zamanillo D, Hunt T, Nebreda AR. A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins. Cell. 78:1995;1027-1037.
12. Deng T, Karin M. c-Fos transcriptional activity stimulated by H-Ras-activated protein kinase distinct from JNK and ERK. of special interest Nature. 371:1994;171-175 This paper demonstrates the existence of a novel MAPK that activates c-Fos transcriptional activity.
13. Zhou GC, Bao ZQ, Dixon JE. Components of a new human protein kinase signal transduction pathway. J Biol Chem. 270:1995;12665-12669.
14. Karin M. The regulation of AP-1 activity by mitogen-activated protein kinase. J Biol Chem. 270:1995;16843-16846.
15. Sturgil TW, Ray LB, Erikson E, Maller JL. Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II. Nature. 334:1988;715-718.
16. Su B, Jacinto E, Hibi M, Kallunki T, Karin M, Ben-Neriah Y. JNK is involved in signal integration during costimulation of T lymphocytes. of outstanding interest Cell. 77:1994;727-736 This paper shows that activation of the JNK, but the not ERK, MAPK cascade in T cells requires co-stimulation of both TCR/CD3 and CD28 auxiliary receptor. This co-stimulation of JNK activity is also inhibited by cyclosporin A.
17. Crews CM, Alessandrini A, Erikson RL. The primary structure of MEK, a protein kinase that phosphorylates the ERK gene product. Science. 258:1992;478-480.
18. Zheng CF, Guan KL. Cloning and characterization of two distinct human extracellular signal-regulated kinase activator kinases, MEK1 and MEK2. J Biol Chem. 268:1993;11435-11439.
19. Brott BK, Alessamdromo A, Largaespada DA, Copeland NG, Jenkins NA, Crews CM, Erikson RL. MEK2 is a kinase related to MEK1 and is differentially expressed in murine tissues. Cell Growth Differ. 4:1993;921-929.
20. Moodie SA, Willumsen MM, Weber MJ, Wofman A. Complexes of Ras. FTP with raf-1 and mitogen-activated protein kinase kinase. Science. 260:1993;1658-1661.
21. Kyriakis JM, App H, Zhang XF, Banerjee P, Brautigan DL, Rapp UR, Avruch J. Raf-1 activates MAP kinase-kinase. Nature. 358:1992;417-421.
22. Pham CD, Arlinghaus RB, Zheng CF, Guan KL, Singh B. Characterization of MEK1 phosphorylation by the v-Mos protein. Oncogene. 10:1995;1683-1688.
23. Lange-Carter CA, Pleiman CM, Gardner AM, Blumer KJ, Johnson GL. A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf. Science. 260:1993;315-317.
24. Egan SE, Weinberg RA. The pathway to signal achievement. Nature. 365:1993;781-783.
25. Kroll SD, Omri G, Landau EM, Iyengar R. Activated alpha subunit of Go protein induces oocyte maturation. Proc Natl Acad Sci USA. 88:1991;5182-5186.
26. Stevenson BJ, Rhodes N, Errede B, Sprague GF Jr. Constitutive mutants of the protein kinase STE11 activate the yeast pheromone response pathway in the absence of the G protein. Genes Dev. 6:1992;1293-1304.
27. Minden A, Lin A, McMahon M, Lange-Carter C, Derijard B, Davis RJ, Johnson GL, Karin M. Differential activation of ERK and JNK mitogen-activated protein kinases by Raf-I and MEKK. of outstanding interest Science. 266:1994;1719-1723 This paper shows that MEKK1 is an upstream activator of a JNK, rather than ERK.
28. Xu S, Robbins D, Frost J, Dang A, Lange-Carter C, Cobb MH. MEKK1 phosphorylates MEK1 and MEK2 but does not cause activation of mitogen-activated protein kinase. Proc Natl Acad Sci USA. 92:1995;6808-6812.
29. Maeda T, Takekawa M, Saito H. Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor. of outstanding interest Science. 269:1995;554-558 This paper presents evidence that PBS2, a member of MEK in yeast, is regulated by two distinct upstream activators.
30. Yamaguchi K, Shirakabe K, Shibuya H, Irie K, Oishi I, Ueno N, Taniguchi T, Nishida E, Matsumoto K. Identification of a member of the MAPKKK family as a potential mediator of TGF-β signal transduction. of outstanding interest Science. 270:1995;2008-2011 A novel MEPKK, TAK1, which is regulated by TGF-β is identified.
31. Cook SJ, McCormick F. Inhibition by cAMP of Ras-dependent activation of Raf. Science. 262:1993;1069-1072.
32. Peraldi P, Frodin M, Barnier JV, Calleja V, Scimeca JC, Filloux C, Calothy G, Van Obberghen E. 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 Lett. 357:1995;290-296.
33. Hsueh YP, Lai MZ. c-Jun N-terminal kinase but not mitogen-activated protein kinase is sensitive to cAMP inhibition in T lymphocytes. of special interest J Biol Chem. 270:1995;18094-18098 It is shown that the JNK, but not the ERK, pathway is inhibited by cAMP in T cells.
34. Binetruy B, Smeal T, Karin M. Ha-Ras augments c-Jun activity and stimulates phosphorylation of its activation domain. Nature. 351:1991;122-126.
35. Devary Y, Gottlieb RA, Karin M. Rapid and preferential activation of the cJun gene during the mammalian UV response. Mol Cell Biol. 11:1991;2804-2811.
36. Angel P, Hattori K, Smeal T, Karin M. The jun photo-oncogene is positively autoregulated by its product, Jun/AP-1. Cell. 55:1988;875-885.
37. Smeal T, Binetruy B, Mercola D, Birrer M, Karin M. Phosphorylation of c-Jun on Ser63 and 73 is required for oncogenic and transcriptional cooperation with Ha-ras. Nature. 354:1992;494-496.
38. Hibi M, Lin A, Smeal T, Minden A, Karin M. Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain. Genes Dev. 7:1993;2135-2148.
39. Mohit AA, Martin JH, Miller CA. p493F12 kinase: a novel MAP kinase expressed in a subset of neurons in the human nervous system. Neuron. 14:1995;67-78.
40. Sanchez I, Hughes RT, Mayer BJ, Yee K, Woodgett JR, Avruch J, Kyuriakis JM, Zon LI. Role of SAPK/ERK kinase-1 in the stress-activated pathway regulating transcription factor c-Jun. of special interest Nature. 372:1994;794-798 See annotation [42].
41. Derijard B, Raingeaud J, Barrett T, Wu IH, Han J, Ulevitch RJ, Davis RJ. Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms. of special interest Science. 267:1995;682-685 See annotation [42].
42. Lin A, Minden A, Martinetto H, Claret FX, Lange-Carter C, Mercurio F, Johnson GL, Karin M. Identification of a dual specificity kinase that activates the Jun kinases and p38-Mpk2. of special interest Science. 268:1995;288-290 These three papers [40-42] describe the molecular cloning of the JNK/SAPK activating kinase, SEK/JNKK/MKK4.
43. Cano E, Hazzalin CA, Mahadevan LC. Anisomycin-activated protein kinases p45 and p55 but not mitogen-activated protein kinases ERK-1 and -2 are implicated in the induction of c-fos and c-jun. Mol Cell Biol. 14:1964;7352-7362.
44. Raingeaud J, Gupta S, Rogers JS, Dickens M, Han J, Ulevitch RJ, Davis RJ. Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J Biol Chem. 270:1995;7420-7426.
45. Pombo CM, Bonventre JV, Avruch J, Woodgett JR, Kyriakis JM, Force T. The stress-activated protein kinases are major c-Jun amino-terminal kinases activated by ischemia and reperfusion. J Biol Chem. 269:1994;26546-26551.
46. Kharbanda S, Ren R, Pandey P, Shafman TD, Feller SM. Activation of the c-Abl tyrosine kinase in the stress response to DNA-damaging agents. Nature. 376:1995;785-788.
47. Minden A, Lin A, Smeal T, Derijard B, Cobb M, Davis R, Karin M. c-Jun N-terminal phosphorylation correlates with activation of the JNK subgroup but not the ERK subgroup of mitogen-activated protein kinases. Mol Cell Biol. 14:1994;6683-6688.
48. Minden A, Lin A, Abo A, Karin M. Selective activation of the JNK signaling cascade and c-jun transcriptional activity by the small GTPases Rac and Cdc42Hs. of special interest Cell. 81:1995;1147-1157 See annotation [50].
49. Coso OA, Chiariello M, Yu J-C, Teramoto H, Crespo P, Xu N, Miki T, Gutkind JS. The small GTP-binding proteins Racl and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. of special interest Cell. 81:1995;1137-1146 See annotation [50].
50. Hill CS, Wynne J, Treisman R. The Rho family GTPases RhoA, Racl, and CDC42Hs regulate transcriptional activation by SRF. of special interest Cell. 81:1995;1159-1170 These papers [48-50] provide evidence that small G proteins, Rac1 and Cdc42, act upstream of the JNK, but not ERK, MAPK cascade.
51. Ridley AJ. Rho-related proteins: actin cytoskeleton and cell cycle. Curr Opin Genet Dev. 5:1995;24-30.
52. Jullien-Flores V, Dorseuil O, Romero F, Letourneur F, Saragosti S, Berger R, Tavitian A, Gacon G, Camonis JH. Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity. J Biol Chem. 270:1995;22473-22477.
53. Kozma R, Ahmed S, Best A, Lim L. The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts. Mol Cell Biol. 15:1995;1942-1952.
54. Qiu RG, Chen J, Kirn D, McCornick F, Symons M. An essential role for Rac in Ras transformation. Nature. 374:1995;457-459.
55. Michiels F, Habets G, Stam JC, van der Kammen RA, Collard JG. A role for RAC in Tiami-induced membrane ruffling and invasion. Nature. 375:1995;338-340.
56. Martin GA, Bollag G, McCormick F, Abo A. A novel serine kinase activated by racl/CDC42Hs-dependent autophosphorylation is related to PAK 65 and STE20. of special interest EMBO J. 14:1995;1970-1978 See annotation [56,57].
57. Manser E, Leung T, Salihuddin H, Zhao ZS, Lim L. A brain serine-threonine protein kinase activated by Cdc42. of special interest Nature. 367:1994;40-46 These papers show that PAK1/PAK65, like its yeast homolog STE20, acts downstream of Rac1/Cdc42.
58. Leberer E, Dignard D, Harcus D, Thomas DY, Whiteway M. The protein kinase homologue Ste20p is required to link the yeast pheromone response G-protein beta gamma subunits to downstream signaling components. EMBO J. 11:1992;4815-4824.
59. Zhao ZS, Leung T, Manser E, Lim L. Pheromone signalling in Saccharomyces cerevisiae requires the small GTP-binding protein CDC42p and its activator. Mol Cell Biol. 15:1995;5246-5257.
60. Zhang S, Han J, Sells MA, Chernoff J, Knaus UG, Ulevitch RJ, Bokoch GM. Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1. J Biol Chem. 270:1995;23934-23936.
61. Pombo CM, Kehrl JH, Sanchez I, Katz P, Avruch J, Zon LE, Woodgett JR, Force T, Kyriakis JM. Activation of the SAPK pathway by the human STE20 homologue germinal centre kinase. Nature. 377:1995;750-754.
62. Han J, Lee JD, Tobias PS, Ulevitch RJ. Endotoxin induces rapid protein tyrosine phosphorylation in 70Z/3 cells expressing CD14. J Biol Chem. 268:1993;25009-25014.
63. Brewster JL, de Valoir T, Dwyer ND, Winter E, Gustin MC. An osmosensing signal transduction pathway in yeast. Science. 259:1993;1760-1763.
64. Choi KY, Satterberg B, Lyons DM, Elion EA. Ste5 tethers multiple protein kinase in the MAP kinase cascade required for mating in S. cerevisiae. of special interest Cell. 78:1994;499-512 See annotation [65].
65. Marcus S, Polverino A, Barr M, Wigler M. Complexes between STE5 and components of the pheromone-responsive mitogen-activated protein kinase module. of special interest Proc Natl Acad Sci USA. 91:1994;7762-7766 These papers [64,65] demonstrate that STE5 is a non-kinase component of the MEKK-MEK-MAPK module in yeast.
66. Hill CS, Treisman R. Transcriptional regulation by extracellular signals: mechanisms and specificity. of special interest Cell. 80:1995;199-211 A comprehensive review on transcriptional regulation by extracellular signals.
67. Herskowitz I. MAP kinase pathways in yeast: for mating and more. of special interest Cell. 80:1995;187-197 A comprehensive review on yeast MAPK cascades.
68. Treisman R. The serum response element. Trends Biochem Sci. 17:1992;423-426.
69. 2+-regulated transcription factor phosphorylated by calmodulin-dependent kinases. Science. 252:1991;1427-1430.
70. Darnell JE Jr, Kerr IM, Stark GR. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science. 264:1994;1415-1421.
71. Treisman R. Ternary complex factors: growth factor regulated transcriptional activators. Curr Opin Genet Dev. 4:1994;96-101.
72. Marais R, Wynne J, Treisman R. The SRF accessory protein EIk-1 contains a growth factor-regulated transcriptional activation domain. Cell. 73:1993;381-393.
73. Hipskind RA, Buscher D, Nordheim A, Baccarini M. Ras/MAP kinase-dependent and -independent signaling pathways target distinct ternary complex factors. Genes Dev. 8:1994;1803-1816.
74. Price MA, Rogers AE, Treisman R. Comparative analysis of the ternary complex factors EIk-1, SAP-Ia and SAP-2 (ERP/NET). EMBO J. 14:1995;2589-2601.
75. Whitmarsh AJ, Shore P, Sharrocks AD, Davis RJ. Integration of MAP kinase signal transduction pathways at the serum response element. of special interest Science. 269:1995;403-407 See annotation [76].
76. Cavigelli M, Dolfi F, Claret FX, Karin M. Induction of c-fos expression through JNK-mediated TCF/EIk-1 phosphorylation. of special interest EMBO J. 14:1995;5957-5964 These two papers [75,76] show that ternary complex factor EIk-1 can be activated by both JNK and ERK cascades.
77. Hunter T, Karin M. The regulation of transcription by phosphorylation. Cell. 70:1992;375-387.
78. Angel P, Karin M. The role of Jun, Fos and the AP-1 complex in cell-proliferation and transformation. Biochim Biophys Acta. 1072:1991;129-157.
79. Arany Z, Sellers WR, Livingston DM, Eckner R. EIA-associated p300 and CREB-associated CBP belong to a conserved family of coactivators. Cell. 77:1994;799-800.
80. Lundblad JR, Kwok RP, Laurance ME, Harter ML, Goodman RH. Adenoviral E1A-associated protein p300 as a functional homologue of the transcriptional co-activator CBP. Nature. 374:1995;85-88.
81. Gupta S, Campbell D, Derijard B, Davis R. Transcription factor ATF2 regulation by the JNK signal transduction pathway. Science. 267:1995;389-393.
82. Herr I, Van Dam H, Angel P. Binding of promoter-associated AP-1 is not altered during induction and subsequent repression of the cjun promoter by TPA and UV irradiation. Carcinogenesis. 15:1994;1105-1113.
83. Reimold AM, Grusby MJ, Kosaras B, Fries JWU, Mori R, Maniwa S, Clauss IM, Collins T, Sidman RL, Glimcher MJ, Glimcher LH. Chondrodysplasia and neurological abnormalities in ATF-2-deficient mice. Nature. 379:1995;262-265.
84. Sutherland JA, Cook A, Bannister AJ, Kouzarides T. Conserved motifs in Fos and Jun define a new class of activation domain. Genes Dev. 6:1992;1810-1819.
85. Pause A, Belsham GJ, Gingras AC, Donze O, Lin TA, Lawrence JC Jr, Sonenberg N. Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function. of special interest Nature. 371:1994;762-767 See annotation [86].
86. Lin TA, Kong X, Haystead TA, Pause A, Belsham G, Sonenberg N, Lawrence JC Jr. PHAS-1 as a link between mitogen-activated protein kinase and translation initiation. of special interest Science. 266:1994;653-656 These papers [85,86] show that the ERK MAPK cascade regulates the activity of the translation initiation complex.
87. Young P, McDonnell P, Dunnington D, Hand A, Laydon J, Lee J. Pyridinyl imidazoles inhibit IL-1 and TNF production at the protein level. Agents Actions. 39:1993;C67-C69.
88. Cuenda A, Rouse J, Doza YN, Meier R, Cohen P, Gallagher TF, Young PR, Lee JC. SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-I. FEBS Lett. 364:1995;229-233.
89. Nair AP, Hahn S, Banholzer R, Hirsch HH, Moroni C. Cyclosporin A inhibits growth of autocrine tumour cell lines by destabilizing interleukin-3 mRNA. of special interest Nature. 369:1994;239-242 This paper provides evidence that MAPK cascade may be involved in the regulation of mRNA stability.
90. Franklin RA, Tordai A, Patel H, Gardner AM, Johnson GL, Gelfand EW. Ligation of the T cell receptor complex results in activation of the Ras/Raf-1/MEK/MAPK cascade in human T lymphocytes. J Clin Invest. 93:1994;2134-2140.
91. Casillas A, Hanekom C, Williams K, Katz R, Nel AE. Stimulation of B-cells via the membrane immunoglobulin receptor or with phorbol myristate 13-acetate induces tyrosine phosphorylation and activation of a 42-kDa microtubule-associated protein-2 kinase. J Biol Chem. 266:1991;19088-19094.
92. Izquierdo M, Leevers SJ, Williams DH, Marshall CJ, Weiss A, Cantrell D. The role of protein kinase C in the regulation of extracellular signal-regulated kinase by the T cell antigen receptor. Eur J Immunol. 24:1994;2462-2468.
93. Owaki H, Varma R, Gillis B, Bruder JT, Rapp UR, Davis LS, Geppert TD. Raf-1 is required for T cell IL2 production. EMBO J. 12:1993;4367-4373.
94. Alberola-Ila J, Forbush KA, Seger R, Krebs EG, Perlmutter RM. Selective requirement for MAP kinase activation in thymocyte differentiation. of special interest Nature. 373:1995;620-623 This paper demonstrates that ERK cascade is involved in T cell differentiation in vivo.
95. Schwartz RH. Costimulation of T lymphocytes: the role of CD28, CTLA-4, and B7/BB1 in interleukin-2 production and immunotherapy. Cell. 71:1992;1065-1068.