v-Src induces constitutive macropinocytosis in rat fibroblasts

Journal of Cell Science

Volumn 109, Issue 8, 1996, Pages 2005-2012

  Veithen, Alex ^a   Cupers, Philippe ^a   Baudhuin, Pierre ^a   Courtoy, Pierre J ^a  

^a UNIVERSITY OF LOUVAIN MEDICAL SCHOOL   (Belgium)

Author keywords

Endocytosis; Macropinocytosis; v Src

Indexed keywords

HORSERADISH PEROXIDASE; PROTEIN TYROSINE KINASE; TRANSFERRIN;

ANIMAL CELL; ARTICLE; CELL TRANSFORMATION; ELECTRON MICROSCOPY; ENDOCYTOSIS; FIBROBLAST; MICROSCOPY; NONHUMAN; PHENOTYPE; PINOCYTOSIS; PRIORITY JOURNAL; PROTEIN SYNTHESIS INHIBITION; RAT; TEMPERATURE SENSITIVITY;

AMILORIDE; ANIMALS; CELL LINE, TRANSFORMED; FIBROBLASTS; HORSERADISH PEROXIDASE; KINETICS; ONCOGENE PROTEIN PP60(V-SRC); PINOCYTOSIS; RATS;

ANIMALIA; ARMORACIA RUSTICANA;

EID: 0029791453     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (41)

1. Alpuche-Aranda, C. M., Racoosin, E. L., Swanson, J. A. and Miller, S. I. (1994). Salmonella stimulate macrophage macropinocytosis and persist within spacious phagosomes. J. Exp. Med. 179, 601-608.
2. Ambros, V. R., Chen, L. B. and Buchanan, J. M. (1975). Surface ruffles as markers for studies of cell transformation by Rous sarcoma virus. Proc. Nat. Acad. Sci. USA 72, 3144-3148.
3. Anderson, R. G. W. (1991). Molecular motors that shape endocytic membrane. In Intracellular Trafficking of Proteins (ed. C. J. Steer and J. A. Hanover), pp. 13-46. Cambridge University Press, Cambridge.
4. Bar-Sagi, D. and Feramisco, J. R. (1986). Induction of membrane ruffling and fluid-phase pinocytosis in quiescent fibroblasts by ras proteins. Science 233, 1061-1068.
5. Bar-Sagi, D., McCormick, F., Milley. F and Feramisco, J. R. (1987). Inhibition of cell surface ruffling and fluid-phase pinocytosis by microinjection of anti-ras antibodies into living cells. J. Cell. Physiol. Suppl. 5, 69-73.
6. Boschek, C. B., Jockusch, B. M., Friis, R. R., Back, E., Gandemann, E. and Bauer, H. (1981). Early changes in the distribution and organization of microfilament proteins during cell transformation. Cell 24, 174-184.
7. Carpentier, J.-L., Lew, D. P., Paccaud, J.-P., Gil, R., Iacopeta, B., Kazatchine, M., Stendahl, O. and Pozzan, T. (1991). Internalization pathway of C3b receptors in human neutrophils and its transmodulation by chemoattractant receptors stimulation. Cell Regul. 2, 41-55.
8. Catling, A. D., Fincham, V. J., Frame, M. C., Haefner, B. and Wyke, J. A. (1994). Mutations in v-Src SH3 and catalytic domains that jointly confer temperature-sensitive transformation with minimal temperature-dependent changes in cellular tyrosine phosphorylation. J. Virol. 68, 4392-4399.
9. Cupers, P., Veithen, A., Kiss, A., Baudhuin, P. and Courtoy, P. J. (1994). Clathrin polymerisation is not required for bulk phase endocytosis in rat fetal fibroblast. J. Cell Biol. 127, 725-735.
10. Dowrick, P. P., Kenworthy, P., McCann, B. and Warn, R. (1993). Circular ruffle formation and closure lead to macropinocytosis in hepatocyte growth factors/scatter factor-treated cells. Eur. J. Cell Biol. 61, 44-53.
11. Ellis, C., Moran, M., McCormick, F. and Pawson, T. (1990). Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases. Nature 343, 377-381.
12. v-src association with the cytoskeleton induces actin reorganization without affecting polymerization status. Eur. J. Cell Biol. 52, 47-59.
13. Francis, C. L., Ryan, T. A., Jones, B. D., Smith, S. J. and Falkow, S. (1993). Ruffles induced by Salmonella and other stimuli direct macropinocytosis of bacteria. Nature 364, 639-642.
14. Haigler, H. T., McKanna, J. A. and Cohen, S. (1979). Rapid stimulation of pinocytosis in human carcinoma cells A-431 by epidermal growth factor. J. Cell Biol. 83, 82-90.
15. Hansen, S. H., Sandvig, K. and van Deurs, B. (1991). The preendosomal compartment comprises distinct coated and noncoated vesicle populations. J. Cell Biol. 113, 731-741.
16. Hewlettt, L. J., Prescott, A. R. and Watts, C. (1994). The coated pit and macropinocytosis pathways serve distinct endosome populations. J. Cell Biol. 124, 689-703.
17. Keller, H. U. (1990). Diacylglycerol and PMA are particularly effective stimulators of fluid-phase pinocytosis in human neutrophils. J. Cell. Physiol. 145, 465-471.
18. Keller, H. U. and Niggli, V. (1993). The PKC-inhibitor Ro 31-8220 selectively suppresses PMA- and diacylglycerol-induced fluid pinocytosis and actin polymerisation in PMNS. Biochem. Biophys. Res. Commun. 194, 1111-1116.
19. Lavoie, J. N., Hickey, E., Weber, L. and Landry, J. (1993). Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27. J. Biol. Chem. 268, 24210-24214.
20. McFarlane, A. S. (1958). Efficient trace labelling of proteins with iodine. Nature 183, 53.
21. McGlade, J., Brunkhorst, B., Anderson, D., Mhalmalu, G., Settleman, J., Dedhar, S., Rozakis-Adcock, M., Chen, L. B. and Pawson, T. (1993). The N-terminal region of GAP regulates cytoskeletal structure and cell adhesion. EMBO J. 12, 3073-3081.
22. Peterson, J. E., Jelinek, T., Kalenko, M., Siddle, K. and Weber, M. J. (1994). Phosphorylation and activation of the IGF-1 receptor in src-transformed cells. J. Biol. Chem. 269, 27315-27321
23. Qiu, R.-G., Chen, J., Kirn, D., McCormick, F. and Symons, M. (1995). An essential role for Rac in Ras transformation. Nature 374, 475-459.
24. Racoosin, E. L. and Swanson, J. A. (1989). Macrophage colony-stimulating factor (rM-CSF) stimulates pinocytosis in bone marrow-derived macrophages. J. Exp. Med. 170, 1635-1648.
25. Racoosin, E. L. and Swanson, J. A. (1992). M-CSF-induced macropinocytosis increases solute endocytosis but not receptor-mediated endocytosis in mouse macrophages. J. Cell Sci. 102, 867-880.
26. Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D. and Hall, A. (1992). The small GTP-binding protein rac regulates gowth factor-induced membrane ruffling. Cell 70, 401-410.
27. Ridley, A. J. (1994). Membrane ruffling and signal transduction. BioEssays 16, 321-327.
28. Sandvig, K. and van Deurs, B. (1994). Endocytosis without clathrin. Trends Cell Biol. 4, 275-277.
29. Smith, P. K., Krhon, R. I., Hermanson, G. T., Malia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Gorke, N. M., Olson, B. J. and Klenk, D. C. (1985). Measurement of protein using bicinchoninic acid. Anal. Biochem. 150, 76-85.
30. Smythe, E. and Warren, G. (1991). The mechanism of receptor-mediated endocytosis. Eur. J. Biochem. 202, 689-699.
31. Steinmann, R. M., Brodie, S. E. and Cohn, Z. A. (1976). The interaction of soluble horseradish peroxidase with mouse peritoneal macrophages in vitro. J. Cell Biol. 68, 665-687.
32. Swanson, J. A. (1989). Phorbol esters stimulate macropinocytosis and solute flow through macrophages. J. Cell Sci. 94, 135-142.
33. Takei, M., Nakagawa, H. and Endo, K. (1993). Mast cell activation by pedicellar toxin of sea urchin Toxopneustes pileolus. FEBS Lett. 328, 59-62.
34. Tan, P. K., Davis, N. G., Sprague, G. F. and Payne, G. S. (1993). Clathrin facilitates the internalization of seven transmembrane segment receptors for mating pheromones in yeast. J. Cell Biol. 123, 1707-1716.
35. v-Src alters ionic permeability of the membrane in rat cells. J. Biol. Chem. 262, 2431-2434.
36. Watts, C. and Marsh, M. (1992). Endocytosis: what goes in and how ? J. Cell Sci. 103, 1-8.
37. Watts, C. and Swanson. (1995). Macropinocytosis. Trends Cell Biol. 5, 424-428.
38. v-src is not accompained by increased expression of immediate early response genes. Oncogene 5, 161-169.
39. Wennström, S., Siegbahn, A., Yokote, K., Arvidsson, A.-K., Heldin, C. H., Mori, S. and Cleasson-Welsh, L. (1994). Membrane ruffling and chemotaxis transduced by PDGF β-receptor require the binding site for phosphatidylinositol 3′ kinase. Oncogene 9, 651-660.
40. West, M. A., Bretscher, M. S. and Watts, C. (1989). Distinct endocytic pathways in epidermal growth factor stimulated human carcinoma A431 cells. J. Cell Biol. 109, 2731-2739.
41. White, M. K. and Weber, M. J. (1988). Transformation by src oncogene alters glucose transport into rat chicken cells by different mechanisms. Mol. Cell. Biol. 8, 138-144.