Association of P120 Ras GAP with endocytic components and colocalization with epidermal growth factor (EGF) receptor in response to EGF stimulation

Cell Growth and Differentiation

Volumn 7, Issue 1, 1996, Pages 123-133

  Wang, Zhixiang ^a   Tung, Pierre S ^a   Moran, Michael F ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN;

ANIMAL CELL; ARTICLE; CELL FRACTIONATION; CELL MEMBRANE; CELL STRAIN; ELECTRON MICROSCOPY; ENDOCYTOSIS; ENZYME ACTIVATION; IMMUNOBLOTTING; IMMUNOPRECIPITATION; MOUSE; NONHUMAN; ONCOGENE RAS; PRIORITY JOURNAL; PROTEIN LOCALIZATION; RECEPTOR DOWN REGULATION;

ANIMALS; BIOLOGICAL TRANSPORT; CELL FRACTIONATION; CELL LINE; CELL MEMBRANE; DOGS; ENDOCYTOSIS; ENDOSOMES; EPIDERMAL GROWTH FACTOR; FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT; GTPASE-ACTIVATING PROTEINS; IMMUNOBLOTTING; IMMUNOHISTOCHEMISTRY; KIDNEY TUBULES, DISTAL; MICROSCOPY, ELECTRON; PRECIPITIN TESTS; PROTEIN BINDING; PROTEINS; RAS GTPASE-ACTIVATING PROTEINS; RECEPTOR, EPIDERMAL GROWTH FACTOR; SIGNAL TRANSDUCTION;

ANIMALIA;

EID: 0030033689     PISSN: 10449523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (75)

1. Schlessinger, J., and Ullrich, A. Growth factor signaling by receptor tyrosine kinases. Neuron, 9: 383-391, 1992.
2. Carpenter, G. Receptors for epidermal growth factor and other polypeptide mitogens. Annu. Rev Biochem., 56: 881-914, 1987.
3. Moran, M. F., Koch, C. A., Anderson, D. A., Ellis, C., England, L., Martin, G. S., and Pawson, T. Src homology 2 domains direct protein-protein interactions in signal transduction. Proc. Natl. Acad. Sci. USA, 87: 8622-8626, 1990.
4. Anderson, D., Koch, C. A., Grey, L., Ellis, C., Moran, M. F., and Pawson, T Binding of SH2 domains of phospholipase Cγ1, GAP and Src to activated growth factor receptors. Science (Washington DC), 250: 979-982.
5. Koch, C. A., Anderson, D., Moran, M. F., Ellis, C., and Pawson, T. SH2 and SH3 domains elements that control interactions of cytoplasmic signaling proteins. Science (Washington DC), 252: 668-674, 1991.
6. Van Aelst, L., Barr, M., Marcus, S., Polverino, A., and Wigler, M. Complex formation between RAS and RAF and other protein kinases. Proc. Natl. Acad. Sci. USA., 90: 6213-6217, 1993.
7. ras proteins bind to the amino-terminal regulatory domain of c-Raf-1. Nature (Lond.), 364: 308-313, 1993.
8. Warne, P., Vaciana, R., and Downward, J. Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro. Nature (Lond.), 364: 352-355, 1993.
9. Vojtek, A., Hollenberg, S., and Cooper, J. Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell, 74: 205-214, 1993.
10. Moodie, S. A., Willumsen, B. M., Weber, W. J , and Wolfman, A. Complexes of Ras.GTP with Raf-1 and mitogen-activated protein kinase. Science (Washington DC), 260: 1658-1661, 1993.
11. Rodriguez-Vaciana, P., Warne, P., Dhand, R., Vanhaessebroeck, B., Gout, I., Fry, M., Waterfield, M., and Downward, J. Phosphatidylinositol-3-OH kinase as a direct target of Ras. Nature (Lond.), 370: 527-532, 1994
12. Downward, J. Regulation of p21ras by GTPase activating proteins and guanine nucleotide exchange proteins. Curr. Opin. Genet. Dev., 2: 13-18, 1992.
13. Lowy, D. R., and Wiliumsen, B. M. Function and Regulation of RAS. Annu. Rev Biochem., 62: 851-891, 1993.
14. McCormick, F How receptors turn Ras on. Nature (Lond.), 363: 15-16, 1993.
15. Feig, L , and Schaffhausen, B. The hunt for ras targets. Nature (Lond.), 370: 508-509, 1994.
16. Schlessinger, J. Allosteric regulation of the epidermal growth factor receptor kinase. J. Cell Biol., 103: 2067-2072, 1986.
17. Sorkin, A., and Carpenter, G. Interaction of activated epidermal growth factor receptors with coated pit adaptins. Science (Washington DC), 261: 612-615, 1993.
18. Doven, S., and Fava, R. Internalization of functional epidermal growth factor receptor kinase complexes in A431 cells. J. Biol. Chem., 260: 12351-12358, 1985.
19. Kay, D., Lai, W., Uchihashi, M., Khan, M., Posner, B., and Bergeron, J. Epidermal growth factor receptor kinase translocation and activation in vivo. J. Biol. Chem., 261: 8473-8480, 1986.
20. Lai, W. H., Cameron, P. H., Doherty, J., II, Posner, B. I., and Bergeron, J. J. Ligand-mediated autophosphorylation activity of the epidermal growth factor receptor during internalization. J. Cell Biol., 109: 2751-2760, 1989.
21. Lai, W. H., Cameron, P. H., Wada, I., Doherty, J., II, Kay, D. G , Posner, B. I., and Bergeron, J. J. Ligand-mediated internalization, recycling, and downregulation of the epidermal growth factor receptor in vivo J. Cell Biol., 109: 2741-2749, 1989.
22. Di Guglielmo, G., Baass, P., Ou, W., Posner, B., and Bergeron, J. Compartmentalization of SHC, GRB2, and mSOS and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma. EMBO J., 13: 4269-4277, 1994.
23. Felder, S., Miller, K., Moehren, B., Ullrich, A., Schlessinger, J., and Hopkins, C. Kinase activity controls the sorting of the epidermal growth factor receptor within the multivesicular body. Cell, 61: 623-634, 1990.
24. Futter, C., Felder, S., Schlessinger, J., Ullrich, A., and Hopkins, C. Annexin I is phosphorylated in the murtivesicular body during the processing of the epidermal growth factor receptor. J. Cell Biol., 120: 77-83, 1993.
25. Honegger, A., Schmidt, A., Ullrich, A., and Schlessinger, J. Separate endocytic pathways of kinase-defective and -active EGF receptor mutants expressed in same cells. J. Cell Biol., 110: 1541-1548, 1990.
26. Jing, S., Spencer, T., Miller, K., Hopkins, C , and Towbridge, I. Role of the human transferrin receptor cytoplasmic domain in endocytosis: localization of a specific signal sequence for internalization. J. Cell Biol., 110: 283-294, 1990.
27. Towbridge, I., Collawn, J., and Hopkins, C Signal-dependent membrane protein trafficking in the endocytic pathway. Annu. Rev. Cell Biol., 9: 129-161, 1993.
28. Chen, W., Lazar, C., Lund, K , Welsh, J., Chang, C-P., Der Walton, G., Wiley, C. H., Gill, G., and Rosenfeld, M. 1989. Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation. Cell, 59: 33-43, 1989.
29. Sorkin, A., Helin, K., Waters, C. M., Carpenter, G., and Beguinot, L. Multiple autophosphorylation sites of the epidermal growth factor receptor are essential for receptor kinase activity and internalization. Contrasting significance of tyrosine 992 in the native and truncated receptors. J. Biol. Chem., 267: 8672-8678, 1992.
30. Lamaze, C., and Schmid, S. Recruitment of epidermal growth factor receptors into coated pits requires their activated tyrosine kinase. J. Cell Biol., 129: 47-54, 1995.
31. ras GTPase activating protein. Mol. Cell Biol., 77: 1804-1812, 1991
32. Molloy, C J., Bottaro, D. P., Fleming, T. P., Marshall, M. S., Gibbs, J. B., and Aaronson, S A. PDGF induction of tyrosine phosphorylation of GTPase activating protein. Nature (Lond.), 342: 711-714, 1989.
33. Rozengurt, E., Brown, K. D., and Pettican, P. Vasopressin inhibition of epidermal growth factor binding to cultured mouse cells. J. Biol. Chem., 256: 716-722, 1981
34. GAP that confers membrane localization. Oncogene, 10: 817-825, 1995.
35. 2+-dependent phospholipid binding domain (CaLB) within p120 ras GAP. Biochem. J., 307: 487-491, 1995.
36. Ellis, C., Moran, M F., McCormick, F., and Pawson, T. Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases. Nature (Lond.), 343: 377-381, 1990.
37. Bouton, A., Kanner, S., Vines, R., Wang, H., Gibbs, J., and Parsons, J Transformation by pp60src or stimulation of cells with epidermal growth factor induces the stable association of tyrosine-phosphorylated cellular proteins with GTPase-activating protein. Mol. Cell. Biol., 11: 945-953, 1991.
38. Khan, M., Savoie, S., Bergeron, J., and Posner, B. Characterization of rat liver endosomal fractions J. Biol. Chem., 261: 8462-8472, 1986.
39. Soler, C., Benguinot, L., Sorkin, A., and Carpenter, G. Tyrosine phosphorylation of ras GTPase-activating protein does not require association with the epidermal growth factor receptor. J. Biol. Chem., 268: 22010-22019, 1993.
40. Soler, C., Beguinot, L., and Carpenter, G. Individual epidermal growth factor receptor autophosphorylation sites do not stringently define association motifs for several SH2-containing proteins. J. Biol. Chem . 269: 12320-12324, 1994.
41. Clark, G. J., Quilliam, L. A., Hisaka, M. M., and Der, C. J. Differential antagonism of Ras biological activity by catalytic and Src homology domains of Ras GTPase activation protein. Proc. Natl. Acad. Sci. USA, 90: 4887-4891, 1993.
42. Huang, D., Marshall, C. J., and Hancock, J. F. Plasma membrane-targeted ras GTPase-activating protein is a potent suppressor of p21(ras) function. Mol. Cell. Biol., 13: 2420-2431, 1993.
43. Nori, M., Vogel, U., Gibbs, J., and Weber, M. Inhibition of v-src-induced transformation by a GTPase-activating protein. Mol. Cell Biol., 11: 2812-2818, 1991.
44. Zhang, K., DeClue, J. E., Vass, W. C., Papageorge, A. G., McCormick, F., and Lowy, D. R. Suppression of c-ras transformation by GTPase-activating protein. Nature (Lond.), 346: 754-756, 1990.
45. DeClue, J. E., Zhang, K., Redford, P., Vass, W. C., and Lowy, D R. Suppression of src transformation by overexpression of full-length GTPase-activating protein (GAP) or of the GAP C terminus. Mol. Cell. Biol., 11: 2819-2825, 1991.
46. Pawson, T. Protein motifs and signaling networks. Nature (Lond.), 373: 573-580, 1995.
47. Marshall, C Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell, 80: 179-185, 1995.
48. Trahey, M., Wong, G., Halenbeck, R, Rubinfeld, B., Martin, G A., Ladner, M., Long, C. M., Crosier, W. J., Watt, K., Koths, K., and McCormick, F. Molecular cloning of two types of GAP complementary DNA from human placenta. Science (Washington DC), 242: 1697-1700, 1988.
49. Settleman, J., Albright, C., Foster, L., and Weinberg, R. Association between GTPase activators for Rho and Ras families. Nature (Lond.), 359: 153-154, 1992.
50. Ridley, A., Self, A., Kasmi, F., Paterson, H., Hall, A , Marshall, C., and Ellis, C. rho Family GTPase activating proteins p190, bcr and rhoGAP show distinct specificities in vitro and in vivo. EMBO J., 12: 5151-5160, 1993.
51. McGlade, J., Brunkhorst, B., Anderson, D., Mbamalu, G., Settleman, J., Dedhar, S., Rozakis-Adcock, M., Chen, L., and Pawson, T. The N-terminal region of GAP regulates cytoskeletal structure and cell adhesion. EMBO J., 12: 3073-3081, 1993.
52. Ando, A., Yonezawa, K., Gout, I., Nakata, T., Ueda, H., Hara, K., Kitamura, Y., Noda, Y., Takenawa, T., Hirokawa, N., Waterfield, M. D., and Kasuga, M. A complex of GRB2-dynamin binds to tyrosine-phosphorylated insulin receptor substrate-1 after insulin treatment. EMBO J., 133: 3033-3038, 1994.
53. Gout, I., Dhand, R., Hiles, I., Fry, M., Panayotou, G., Das, P., Truong, O., Totty, N., Hsuan, J., Booker, G., Campbell, I. D., and Waterfield, M D. The GTPase dynamin binds to and is activated by a subset of SH3 domains. Cell, 75: 25-36, 1993.
54. Herskovits, J., Shpetner, H., Burgess, C., and Vallee, R. Microtubules and Src homology 3 domains stimulate the dynamin GTPase via its C-terminal domain Proc. Natl Acad. Sci. USA, 90: 11468-11472, 1993
55. McPherson, P., Takei, K., Schmid, S., and De Camilli, P. p145, a major Grb2-binding protein in brain, is co-localized with dynamin in nerve terminals where it undergoes activity-dependent dephosphorylation. J Biol. Chem., 269: 30132-30139, 1994.
56. Miki, H., Miura, K., Matuoka, K., Nakata, T., Hirokawa, N., Orita, S., Kaibuchi, K., Takai, Y., and Takenawa, T. Association of Ash/Grb-2 with dynamin through the Src homology 3 domain. J. Biol. Chem , 269. 5489-5492, 1994.
57. Scaife, R., Gout, I., Waterfield, M., and Margolis, R. Growth factor-induced binding of dynamin to signal transduction proteins involves sorting to distinct and separate proline-rich dynamin sequences. EMBO J., 13: 2574-2582, 1994
58. Seedorf, K., Kostka, G., Lammers, R., Bashkin, P., Daly, R., Burgess, W., vanderBliek, A , Schlessinger, J., and Ullrich, A. Dynamin binds to SH3 domains of phospholipase C gamma and GRB-2. J. Biol. Chem 269: 16009-16014, 1994.
59. Chen, W , Goldstein, J., and Brown, M. NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. J. Biol. Chem., 265: 3116-3123, 1990.
60. Khan, M., Lai, W., Burgess, J., Posner, B., and Bergeron, J. Potential role of endosomes in transmembrane signaling. Subcell. Biochem., 19: 223-254, 1993.
61. Blaikie, P., Immanuel, D., Wu, J., Li, N., Yajnik, V., and Margolis, B. A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors. J. Biol. Chem., 269: 32031-32034, 1994.
62. Kavanaugh, W. M., and Williams, L. T. An alternative to SH2 domains for binding tyrosine-phosphorylated proteins. Science (Washington DC), 266. 1862-1865, 1994.
63. van der Geer, P., Wiley, S., Lai, V., Olivier, J., Gish, G., Stephens, R., Kaplan, D., Shoelson, S., and Pawson, T. A conserved amino-terminal Shc domain binds to phosphotyrosine motifs in activated receptors and phosphopeptides. Curr. Biol., 5: 404-412, 1995.
64. Gustafson, T., He, W., Craparo, A., Schaub, C., and O'Neill, T. Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain. Mol. Cell. Biol., 15: 2500-2508, 1995.
65. ras with phosphatidylinositol 3-kinase. Proc. Natl. Acad. Sci. USA, 88: 7908-7912, 1991.
66. Kapeller, R., Chakrabarti, R., Cantley, L., Fay, F., and Corvera, S. Internalization of activated platelet-derived growth factor receptor-phosphatidylinositol-3′ kinase complexes: potential interactions with microtubule cytoskeleton. Mol. Cell. Biol., 13: 6052-6063, 1993.
67. Herman, P., and Emr, S. Characterization of VPS34, a gene required for vacuolar protein sorting and vacuole segregation in Saccaromyces cerevisiae. Mol. Cell. Biol., 10: 6742-6754, 1990.
68. Hiles, I., Otsu, M., Volinia, S., Fry, M., Gout, I., Dhand, R., Panayotou, G., Ruiz-Larrea, F., Thompson, A., Totty, N., Hsuan, J., Courtneidge, S., Parker, P., and Waterfield, M. Phosphatidylinositol 3-kinase: structure and expression of the 110 kd catalytic subunit. Cell, 70: 419-430, 1992.
69. Pizon, V., Desjardins, M., Bucci, C., Parton, R. G., and Zerial, M. Association of Rap1a and Rap1b proteins with late endocytic/phagocytic compartments and Rap2a with the Golgi complex. J. Cell Sci., 107: 1661-1670, 1994.
70. Kitayama, H., Sugimoto, Y., Matsuzaki, T., Ikawa, Y., and Noda, M. A ras-related gene with transformation suppressor activity. Cell, 56: 77-84, 1989.
71. Hubbard, A., Wall, D., and Ma, A. Isolation of rat hepatocyte plasma membranes. I. Presence of the three major domains. J. Cell Biol., 96: 217-229, 1983.
72. Campbell, C., Squicciarini, J., Shia, M., Pilch, P., and Fine, R. Identification of a protein kinase as an intrinsic component of rat liver coated vesicles. Biochemistry, 23: 4420-4426, 1984.
73. Corvera, S., and Capocasale, R. J. Enhanced phosphorylation of a coated vesicle polypeptide in response to insulin stimulation of rat adipocytes. J. Biol. Chem., 265: 15963-15969, 1990.
74. Bradford, M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72: 6052-6061, 1976.
75. Wang, Z., and Haunerland, N. Ultrastructural study of storage protein granules in fat body of the com earthworm, Heliothis zea. J. Insect. Physiol., 37: 353-363, 1991.