Using plasma membrane nanoclusters to build better signaling circuits

Trends in Cell Biology

Volumn 18, Issue 8, 2008, Pages 364-371

  Harding, Angus S ^a   Hancock, John F ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOLIPASE C; PROTEIN TYROSINE KINASE;

CALCIUM SIGNALING; CELL ACTIVITY; CELL MEMBRANE; IN VIVO CULTURE; LIPID RAFT; NANOCLUSTER; NONHUMAN; PRIORITY JOURNAL; REVIEW; SIGNAL TRANSDUCTION;

ANIMALS; CELL MEMBRANE; HUMANS; MEMBRANE MICRODOMAINS; RECEPTOR CROSS-TALK; SIGNAL TRANSDUCTION;

EID: 48449092211     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2008.05.006     Document Type: Review

References (71)

1. Ashe H.L., and Briscoe J. The interpretation of morphogen gradients. Development 133 (2006) 385-394
2. Stathopoulos A., and Levine M. Dorsal gradient networks in the Drosophila embryo. Dev. Biol. 246 (2002) 57-67
3. Traverse S., et al. Sustained activation of the mitogen-activated protein (MAP) kinase cascade may be required for differentiation of PC12 cells. Comparison of the effects of nerve growth factor and epidermal growth factor. Biochem. J. 288 (1992) 351-355
4. Marshall C.J. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80 (1995) 179-185
5. Kitano H. Towards a theory of biological robustness. Mol. Syst. Biol. 3 (2007) 137
6. Oliver B.M., et al. The philosophy of PCM. Proceedings of the I.R.E. 36 (1948) 1324-1331
7. Schimizu T.S., and Bray D. Computational cell biology - the stochastic approach. In: Kitano H. (Ed). Foundations of Systems Biology (2001), MIT Press 213-232
8. Hancock J.F. Lipid rafts: contentious only from simplistic standpoints. Nat. Rev. Mol. Cell Biol. 7 (2006) 456-462
9. Prior I.A., et al. Direct visualization of Ras proteins in spatially distinct cell surface microdomains. J. Cell Biol. 160 (2003) 165-170
10. Plowman S.J., et al. H-Ras, K-Ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 15500-15505
11. Hancock J.F., and Parton R.G. Ras plasma membrane signaling platforms. Biochem. J. 389 (2005) 1-11
12. Murakoshi H., et al. Single-molecule imaging analysis of Ras activation in living cells. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 7317-7322
13. Tian T., et al. Plasma membrane nanoswitches generate high-fidelity Ras signal transduction. Nat. Cell Biol. 9 (2007) 905-914
14. Marshall C.J. Ras effectors. Curr. Opin. Cell Biol. 8 (1996) 197-204
15. Hibino K., et al. Single- and multiple-molecule dynamics of the signaling from H-Ras to cRaf-1 visualized on the plasma membrane of living cells. ChemPhysChem 4 (2003) 748-753
16. Plowman, S.J. et al. Electrostatic interactions positively regulate K-Ras nanocluster formation and function. Mol. Cell. Biol. 28, 4377-4385
17. Orlean P., and Menon A.K. Thematic review series: lipid posttranslational modifications. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids. J. Lipid Res. 48 (2007) 993-1011
18. Stefanova I., et al. GPI-anchored cell-surface molecules complexed to protein tyrosine kinases. Science 254 (1991) 1016-1019
19. Simons K., and Ikonen E. Functional rafts in cell membranes. Nature 387 (1997) 569-572
20. Simons K., and Toomre D. Lipid rafts and signal transduction. Nat. Rev. Mol. Cell Biol. 1 (2000) 31-39
21. Brugger B., et al. The membrane domains occupied by glycosylphosphatidylinositol-anchored prion protein and Thy-1 differ in lipid composition. J. Biol. Chem. 279 (2004) 7530-7536
22. Gri G., et al. The inner side of T cell lipid rafts. Immunol. Lett. 94 (2004) 247-252
23. Eisenberg S., and Henis Y.I. Interactions of Ras proteins with the plasma membrane and their roles in signaling. Cell. Signal. 20 (2008) 31-39
24. Sharma P., et al. Nanoscale organization of multiple GPI-anchored proteins in living cell membranes. Cell 116 (2004) 577-589
25. Suzuki K.G., et al. Dynamic recruitment of phospholipase C gamma at transiently immobilized GPI-anchored receptor clusters induces IP3-Ca2+ signaling: single-molecule tracking study 2. J. Cell Biol. 177 (2007) 731-742
26. Suzuki K.G., et al. GPI-anchored receptor clusters transiently recruit Lyn and G alpha for temporary cluster immobilization and Lyn activation: single-molecule tracking study 1. J. Cell Biol. 177 (2007) 717-730
27. Harding A., and Hancock J.F. Ras nanoclusters: combining digital and analog signaling. Cell Cycle 7 (2008) 127-134
28. Yeung K., et al. Mechanism of suppression of the Raf/MEK/extracellular signal-regulated kinase pathway by the Raf kinase inhibitor protein. Mol. Cell. Biol. 20 (2000) 3079-3085
29. Yeung K., et al. Suppression of Raf-1 kinase activity and MAP kinase signaling by RKIP. Nature 401 (1999) 173-177
30. Munro S. Lipid rafts: elusive or illusive?. Cell 115 (2003) 377-388
31. Shaw A.S. Lipid rafts: now you see them, now you don't. Nat. Immunol. 7 (2006) 1139-1142
32. Harding A., et al. Subcellular localization determines MAP kinase signal output. Curr. Biol. 15 (2005) 869-873
33. Murphy L.O., et al. Molecular interpretation of ERK signal duration by immediate early gene products. Nat. Cell Biol. 4 (2002) 556-564
34. Schuster S., et al. Modelling of simple and complex calcium oscillations. From single-cell responses to intercellular signaling. Eur. J. Biochem. 269 (2002) 1333-1355
35. Abankwa D., et al. A novel switch region regulates H-Ras membrane orientation and signal output. EMBO J. 27 (2008) 727-735
36. Gorfe A.A., et al. Structure and dynamics of the full-length lipid-modified H-Ras protein in a 1,2-dimyristoylglycero-3-phosphocholine bilayer. J. Med. Chem. 50 (2007) 674-684
37. Rotblat B., et al. Three separable domains regulate GTP-dependent association of H-Ras with the plasma membrane. Mol. Cell. Biol. 24 (2004) 6799-6810
38. Roy S., et al. Individual palmitoyl residues serve distinct roles in H-Ras trafficking, microlocalization, and signaling. Mol. Cell. Biol. 25 (2005) 6722-6733
39. Abankwa D., et al. Ras nanoclusters: molecular structure and assembly. Semin. Cell Dev. Biol. 18 (2007) 599-607
40. Belanis L., et al. Galectin-1 is a novel structural component and a major regulator of H-Ras nanoclusters. Mol. Biol. Cell 19 (2008) 1404-1414
41. Kusumi A., et al. Single-molecule tracking of membrane molecules: plasma membrane compartmentalization and dynamic assembly of raft-philic signaling molecules. Semin. Immunol. 17 (2005) 3-21
42. Kusumi A., et al. Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts. Traffic 5 (2004) 213-230
43. Kusumi A., et al. Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: high-speed single-molecule tracking of membrane molecules. Annu. Rev. Biophys. Biomol. Struct. 34 (2005) 351-378
44. Mayor S., and Rao M. Rafts: scale-dependent, active lipid organization at the cell surface. Traffic 5 (2004) 231-240
45. Nicolau Jr. D.V., et al. Identifying optimal lipid raft characteristics required to promote nanoscale protein-protein interactions on the plasma membrane. Mol. Cell. Biol. 26 (2006) 313-323
46. Nicolau Jr. D.V., et al. Sources of anomalous diffusion on cell membranes: a Monte Carlo study. Biophys. J. 92 (2007) 1975-1987
47. Kyriakis J.M., and Avruch J. Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol. Rev. 81 (2001) 807-869
48. Ferrell Jr. J.E., and Machleder E.M. The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes. Science 280 (1998) 895-898
49. Kholodenko B.N. Negative feedback and ultrasensitivity can bring about oscillations in the mitogen-activated protein kinase cascades. Eur. J. Biochem. 267 (2000) 1583-1588
50. Markevich N.I., et al. Long-range signaling by phosphoprotein waves arising from bistability in protein kinase cascades. Mol. Syst. Biol. 2 (2006) 61
51. Schwacke J.H., and Voit E.O. The potential for signal integration and processing in interacting MAP kinase cascades. J. Theor. Biol. 246 (2007) 604-620
52. Wittinghofer A., and Pai E.F. The structure of Ras protein: a model for a universal molecular switch. Trends Biochem. Sci. 16 (1991) 382-387
53. Morrison D.K., and Cutler R.E. The complexity of Raf-1 regulation. Curr. Opin. Cell Biol. 9 (1997) 174-179
54. Fukuda M., et al. A novel regulatory mechanism in the mitogen-activated protein (MAP) kinase cascade. Role of nuclear export signal of MAP kinase kinase. J. Biol. Chem. 272 (1997) 32642-32648
55. Fukuda M., et al. 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
56. Yoon S., and Seger R. The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions. Growth Factors 24 (2006) 21-44
57. Harding A., et al. Identification of residues and domains of Raf important for function in vivo and in vitro. J. Biol. Chem. 278 (2003) 45519-45527
58. Zhu J., et al. Identification of Raf-1 S471 as a novel phosphorylation site critical for Raf-1 and B-Raf kinase activities and for MEK binding. Mol. Biol. Cell 16 (2005) 4733-4744
59. Terai K., and Matsuda M. Ras binding opens c-Raf to expose the docking site for mitogen-activated protein kinase kinase. EMBO Rep. 6 (2005) 251-255
60. Feng Y., et al. Functional binding between Gbeta and the LIM domain of Ste5 is required to activate the MEKK Ste11. Curr. Biol. 8 (1998) 267-278
61. Inouye C., et al. Ste5 RING-H2 domain: role in Ste4-promoted oligomerization for yeast pheromone signaling. Science 278 (1997) 103-106
62. Maeda T., et al. Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor. Science 269 (1995) 554-558
63. Reiser V., et al. Polarized localization of yeast Pbs2 depends on osmostress, the membrane protein Sho1 and Cdc42. Nat. Cell Biol. 2 (2000) 620-627
64. Cacace A.M., et al. Identification of constitutive and Ras-inducible phosphorylation sites of KSR: implications for 14-3-3 binding, mitogen-activated protein kinase binding, and KSR overexpression. Mol. Cell. Biol. 19 (1999) 229-240
65. Muller J., et al. C-TAK1 regulates Ras signaling by phosphorylating the MAPK scaffold. KSR1. Mol. Cell 8 (2001) 983-993
66. Teis D., et al. Localization of the MP1-MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction. Dev. Cell 3 (2002) 803-814
67. Torii S., et al. Sef is a spatial regulator for Ras/MAP kinase signaling. Dev. Cell 7 (2004) 33-44
68. Turner C.E., et al. Paxillin: a new vinculin-binding protein present in focal adhesions. J. Cell Biol. 111 (1990) 1059-1068
69. Luttrell L.M., et al. Activation and targeting of extracellular signal-regulated kinases by beta-arrestin scaffolds. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 2449-2454
70. Pryciak P.M., and Huntress F.A. Membrane recruitment of the kinase cascade scaffold protein Ste5 by the Gbetagamma complex underlies activation of the yeast pheromone response pathway. Genes Dev. 12 (1998) 2684-2697
71. Zhou M., et al. Solution structure and functional analysis of the cysteine-rich C1 domain of kinase suppressor of Ras (KSR). J. Mol. Biol. 315 (2002) 435-446