Scaffolding and protein interactions in MAP kinase modules

Cell Calcium

Volumn 26, Issue 5, 1999, Pages 219-226

  Karandikar, M ^a   Cobb, M H ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN;

FLY; MAMMAL; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN INTERACTION; REVIEW; SIGNAL TRANSDUCTION; WORM; YEAST;

EID: 0033458831     PISSN: 01434160     EISSN: None     Source Type: Journal    
DOI: 10.1054/ceca.1999.0074     Document Type: Review

References (70)

1. Cobb M. H. MAP kinase pathways. Progress in Biophysics & Molecular Biology. 71:1999;479-500.
2. Lewis T. S., Shapiro P. S., Ahn N. G. Signal transduction through MAP kinase cascades. Advances in Cancer Research. 74:1998;49-139.
3. Kranz J. E., Satterberg B., Elion E. A. The MAP kinase Fus3 associates with and phosphorylates the upstream signaling component Ste5. Genes Dev. 8:1994;313-327.
4. Choi K-Y., Satterberg B., Lyons D. M., Elion E. A. Ste5 tethers multiple protein kinases in the MAP kinase cascade required for mating in S cerevisiae. Cell. 78:1994;499-512.
5. Marcus S., Polverino A., Barr M., Wigler M. Complexes between STE5 and components of the pheromone-responsive MAPK-module. Proc Natl Acad Sci USA. 91:1994;7762-7766.
6. Printen J. A., Sprague G. F. J. Protein-protein interactions in the yeast pheromone response pathway: Ste5p interacts with all members of the MAP kinase cascade. Genetics. 138:1994;609-619.
7. Choi K. Y., Kranz J. E., Mahanty S. K., Park K. S., Elion E. A. Characterization of fus3 localization: active fus3 localizes in complexes of varying size and specific activity. Mol Biol Cell. 10:1999;1553-1568.
8. Whiteway M. S., Wu C., Leeuw T. Association of the yeast pheromone response G protein βγ subunits with the MAP kinase scaffold Ste5p. Science. 269:1995;1572-1575.
9. Feng Y., Song L. Y., Kincaid E., Mahanty S. K., Elion E. A. Functional binding between Gbeta and the LIM domain of Ste5 is required to activate the MEKK Ste11. Curr Biol. 8:1998;267-278.
10. Dietzel C., Kurjan J. The yeast SCG1 gene: a G alpha-like protein implicated in the a- and alpha-factor response pathway. Cell. 50:1987;1001-1010.
11. Inouye C., Dhillon N., Thorner J. Ste5 RING-H2 domain: role in Ste4-promoted oligomerization for yeast pheromone signaling. Science. 278:1997;103-106.
12. Butty A. C., Pryciak P. M., Huang L. S., Herskowitz I., Peter M. The role of Far1p in linking the heterotrimeric G protein to polarity establishment proteins during yeast mating. Science. 282:1998;1511-1516.
13. Akada R., Kallal L., Johnson D. I., Kurjan J. Genetic relationships between the G protein beta gamma complex, Ste5p, Ste20p and Cdc42p: investigation of effector roles in the yeast pheromone response pathway. Genetics. 143:1996;103-117.
14. Mahanty S. K., Farley F. W., Elion E. Nuclear shuttling of the Ste5 scaffold protein is required for its localization to the plasma membrane and activation of the mating MAPK cascade. Cell. 1999.
15. Yablonski D., Marbach I., Levitzki A. Dimerization of Ste5, a mitogen-activated protein kinase cascade scaffold protein, is required for signal transduction. Proc Natl Acad Sci USA. 93:1996;13864-13869.
16. Levin D. E., Errede B. A Multitude of MAP Kinase Activation Pathways. J NIH Research. 5:1993;49-52.
17. Brewster J. L., de Valoir T., Dwyer N. D., Winter E., Gustin M. C. An Osmosensing Signal Transduction pathway in Yeast. Science. 259:1993;1760-1763.
18. Posas F., Saito H. Osmotic activation of the HOG MAPK pathway via Ste11p MAPKKK: scaffold role of Pbs2p MAPKK. Science. 276:1997;1702-1705.
19. Posas F., Wurgler-Murphy S. M., Maeda T., Witten E. A., Thai T. C., Saito H. Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 "two-component" osmosensor. Cell. 86:1996;865-875.
20. Moodie S. A., Willumsen B. M., Weber M. J., Wolfman A. Complexes of Ras-GTP with Raf-1 and mitogen-activated-protein kinase kinase. Science. 260:1993;1658-1660.
21. Ferrell J. E., Machleder E. M. The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes. Science. 280:1998;895-898.
22. Dang A., Frost J. A., Cobb M. H. The MEK1 proline-rich insert is required for efficient activation of the mitogen-activated protein kinases ERK1 and ERK2 in mammalian cells. J Biol Chem. 273:1998;19909-19913.
23. Bardwell L., Thorner J. A conserved motif at the amino termini of MEKs might mediate high-affinity interaction with the cognate MAPKs. Trends in Biochemical Sciences. 21:1996;373-374.
24. Fukuda M., Gotoh Y., Nishida E. Interaction of MAP kinase with MAP kinase kinase: its possible role in the control of nucleocytoplasmic transport of MAP kinase. EMBO J. 16:1997;1901-1908.
25. Xu, B. Wilsbacher, J. Collisson, T. Cobb, M. H. The N-terminal ERK binding site of MEK1 is required for efficient feedback phosphorylation by ERK2 in vitro and ERK activation in vivo. Submitted.
26. Yang S. H., Whitmarsh A. J., Davis R. J., Sharrocks A. D. Differential targeting of MAP kinases to the ETS-domain transcription factor Elk-1. EMBO J. 17:1998;1740-1749.
27. Hunter T. Protein Kinases and Phosphatases: The Yin and Yang of Protein Phosphorylation and Signaling. Cell. 80:1995;225-236.
28. mapkk) in Fibroblasts. J Cell Biol. 122:1993;1079-1088.
29. Fukuda M., Gotoh I., Gotoh Y., Nishida E. Cytoplasmic Localization of Mitogen-activated Protein Kinase Kinase Directed By Its NH2-Terminal, Leucine-Rich Short Amino Acid Sequence, Which Acts As a Nuclear Export Signal. J Biol Chem. 271:1996;20024-20028.
30. Khokhlatchev A., Canagarajah B., Wilsbacher J. Phosphorylation of the MAP kinase ERK2 promotes its homodimerization and nuclear translocation. Cell. 93:1998;605-615.
31. Wilsbacher J., Goldsmith E. J., Cobb M. H. Phosphorylation of MAP kinases by MAP/ERK kinases involves multiple regions of the MAP kinases. J Biol Chem. 27:1999;16988-16994.
32. Gotoh I., Fukuda M., Adachi M., Nishida E. Control of the cell morphology and the S phase entry by mitogen-activated protein kinase kinase. A regulatory role of its n-terminal region. J Biol Chem. 274:1999;11874-11880.
33. Bardwell L., Cook J. G., Chang E. C., Cairns B. R., Thorner J. Signaling in the yeast pheromone response pathway: specific and high-affinity interaction of the mitogen-activated protein (MAP) kinases Kss1 and Fus3 with the upstream MAP kinase kinase Ste7. Mol Cell Biol. 16:1996;3637-3650.
34. Catling A. D., Schaeffer H-J., Reuter C. W. M., Reddy G. R., Weber M. J. A proline-rich sequence unique to MEK1 and MEK2 is required for Raf binding and regulates MEK function. Mol Cell Biol. 15:1995;5214-5225.
35. Mansour S. J., Resing K. A., Candia J. M. Mitogen-activated protein (MAP) kinase phosphorylation of MAP kinase kinase: determination of phosphorylation sites by mass spectrometry and site-directed mutagenesis. J Biochem. 116:1994;304-314.
36. Gardner A. M., Vaillancourt R. R., Lange-Carter C. A., Johnson G. L. MEK-1 Phosphorylation by MEK kinase, Raf, and mitogen-activated protein kinase. Analysis of phosphopeptides and regulation of activity. Mol Biol Cell. 5:1994;193-201.
37. Cobb M. H., Xu S., Cheng M. Structural analysis of the MAP kinase ERK2 and studies of MAP kinase regulatory pathways. Adv Pharmacol. 36:1996;49-65.
38. Frost J. A., Steen H., Shapiro P. S. Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins. EMBO J. 16:1997;6426-6438.
39. Schaeffer H. J., Catling A. D., Eblen S. T., Collier L. S., Krauss A., Weber M. J. MP1: a MEK binding partner that enhances enzymatic activation of the MAP kinase cascade [see comments]. Science. 281:1998;1668-1671.
40. Therrien M., Chang H. C., Solomon N. M., Karim F. D., Wassarman D. A., Rubin G. M. KSR, a novel protein kinase required for RAS signal transduction. Cell. 83:1995;879-888.
41. Sundaram M., Han M. The C. elegans ksr-1 gene encodes a novel Raf-related kinase involved in Ras-mediated signal transduction. Cell. 83:1995;889-901.
42. Kornfeld K., Hom D. B., Horvitz H. R. The ksr-1 gene encodes a novel protein kinase involved in Ras-mediated signaling in C. elegans. Cell. 83:1995;903-913.
43. Therrien M., Michaud N. R., Rubin G. M., Morrison D. K. KSR modulates signal propagation within the MAPK cascade. Genes & Development. 10:1996;2684-2695.
44. Michaud N. R., Therrien M., Cacace A. KSR stimulates Raf-1 activity in a kinase-independent manner. Proc Natl Acad Sci USA. 94:1997;12792-12796.
45. Yu W., Fantl W. J., Harrowe G., Williams L. T. Regulation of the MAP kinase pathway by mammalian Ksr through direct interaction with MEK and ERK. Curr Biol. 8:1998;56-64.
46. Denouel-Galy A., Douville E. M., Warne P. H. Murine Ksr interacts with MEK and inhibits Ras-induced transformation. Curr Biol. 8:1998;46-55.
47. Stewart S., Sundaram M., Zhang Y., Lee J., Han M., Guan K. L. Kinase suppressor of ras forms a multiprotein signaling complex and modulates MEK localization. Mol Cell Biol. 19:1999;5523-5534.
48. Hunter T., Plowman G. D. The protein kinases of budding yeast: six score and more. TIBS. 22:1997;18-22.
49. Xing H., Kornfield K., Muslin A. J. The protein kinase KSR interacts with 14-3-3 protein and Raf. Curr Biol. 7:1997;294-300.
50. Bell B., Xing H., Yan K., Gautam N., Muslin A. J. KSR-1 binds to G-protein betagamma subunits and inhibits beta gamma-induced mitogen-activated protein kinase activation. J Biol Chem. 274:1999;7982-7986.
51. Knighton D. R., Zheng J., Ten Eyck L. F. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science. 253:1991;407-413.
52. Gibbs C. S., Zoller M. J. Rational scanning mutagenesis of a protein kinase identifies functional regions involved in catalysis and substrate interactions. J Biol Chem. 266:1991;8923-3931.
53. Robinson M. J., Harkins P. C., Zhang J. Mutation of position 52 in ERK2 creates a nonproductive binding mode for ATP. Biochem. 35:1996;5641-5646.
54. Dickens M., Rogers J. S., Cavanagh J. A cytoplasmic inhibitor of the JNK signal transduction pathway. Science. 277:1997;693-696.
55. Whitmarsh A. J., Cavanagh J., Tournier C., Yasuda J., Davis R. J. A mammalian scaffold complex that selectively mediates MAP kinase activation. Science. 281:1998;1671-1674.
56. Lange-Carter C. A., Pleiman C. M., Gardner A. M., Blumer K. J., Johnson G. L. A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf. Science. 260:1993;315-319.
57. Xu S., Robbins D. J., Christerson L. B., English J. M., Vanderbilt C. A., Cobb M. H. Cloning of rat MEKK1 cDNA reveals an endogenous membrane-associated 195 kDa Protein with a large regulatory domain. Proc Natl Acad Sci USA. 93:1996;5291-5295.
58. Xu S., Cobb M. H. MEKK1 binds directly to the c-Jun N-terminal kinases stress-activated protein kinases. J Biol Chem. 272:1997;32056-32060.
59. Xia Y., Wu Z., Su B., Murray B., Karin M. JNKK1 organizes a MAP kinase module through specific and sequential interactions with upstream and downstream components mediated by its amino-terminal extension. Genes Dev. 12:1998;3369-3381.
60. Minden A., Lin A., McMahon M. Differential Activation of ERK and JNK Mitogen-Activated Protein Kinases by Raf-1 and MEKK. Science. 266:1994;1719-1723.
61. Yujiri T., Sather S., Fanger G. R., Johnson G. L. Role of MEKK1 in cell survival and activation of JNK and ERK pathways defined by targeted gene disruption. Science. 282:1998;1911-1914.
62. Su Y-C., Han J., Xu S., Cobb M., Skolnik E. Y. Identification of a novel serine/threonine protein kinase that binds the SH3 domains of Nck and activates the MEKK1-MKK4-JNK/SAPK signaling pathway. EMBO J. 16:1997;1279-1290.
63. Kyriakis J. M. Signaling by the germinal center kinase family of protein kinases. J Biol Chem. 274:1999;5259-5262.
64. Kallunki T., Deng T., Hibi M., Karin M. c-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions. Cell. 87:1996;929-939.
65. Kallunki T., Su B., Tsigelny I. JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation. Genes Dev. 8:1994;2996-3007.
66. Yang S. H., Yates P. R., Whitmarsh A. J., Davis R. J., Sharrocks A. D. The Elk-1 ETS-domain transcription factor contains a mitogen-activated protein kinase targeting motif. Mol Cell Biol. 18:1998;710-720.
67. Jacobs D., Glossip D., Xing H., Muslin A. J., Kornfeld K. Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase. Genes Dev. 13:1999;163-175.
68. Therrien M. CNK, a RAF-binding multidomain protein required for RAS signaling. Cell. 95:1998;343-353.
69. Pawson T., Scott J. D. Signaling through scaffold, anchoring, and adaptor proteins. Science. 278:1997;2075-2080.
70. Sontag E., Federov S., Robbins D., Cobb M., Mumby M. The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the MAP kinase pathway and induces cell proliferation. Cell. 75:1993;887-897.