Advertisement

Subcellular Localization of pp60src in RSV-Transformed Cells

  • James G. Krueger
  • Ellen A. Garber
  • Allan R. Goldberg
Chapter
Part of the Current Topics in Microbiology and Immunology book series (CT MICROBIOLOGY, volume 107)

Abstract

In 1911 Rous demonstrated that a retrovirus, subsequently named Rous sarcoma virus (RSV), could cause a tumor in a chicken. Nearly 60 years elapsed before it was shown that a specific virus function encoded by the src gene of RSV was required for the maintenance of the transformed state. Martin (1970) isolated a temperature-sensitive RSV mutant whose properties indicated that the viral transforming gene product is required for transformation, but not for viral replication. Seven years later, Martin’s genetic experiment was provided with a biochemical foundation when Brugge and Erikson (1977) showed that the transformation gene src encoded a 60 000–dalton (60-kd) protein present in RSV-transformed cells. Since 1977, many genes capable of inducing oncogenic transformation, and hence given the generic name onc, have been recognized, and many of the oncogenes’ protein products have been identified. The molecular biology of retroviruses is reviewed extensively and in great detail by Weiss et al. (1982), and the reader is referred to this volume and numerous reviews referenced therein on specific aspects of retrovirology.

Keywords

Cellular Fractionation Rous Sarcoma Virus Adhesion Plaque Discontinuous Sucrose Gradient Avian Sarcoma Virus 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Abercrombie M, Heaysman JEM, Pegrum SM (1971) The locomotion of fibroblasts in culture. IV. Electron microscopy of the leading lamella. Exp Cell Res 67: 359–367Google Scholar
  2. Amini S, Kaji A (1983) Association of pp36, a phosphorylated form of the presumed target protein for the src protein of Rous sarcoma virus, with the membrane of chicken cells transformed by Rous sarcoma virus. Proc Natl Acad Sci USA 80: 960–964PubMedPubMedCentralCrossRefGoogle Scholar
  3. Anderson DD, Beckmann RP, Harms EH, Nakamura K, Weber MJ (1981) Biological properties of “partial” transformation mutants of Rous sarcoma virus and characterization of their pp60src kinase. J Virol 37: 445–458PubMedPubMedCentralGoogle Scholar
  4. Antler A, Greenberg ME, Goldberg AR, Edelman GM, Hanafusa H (to be published) Transformation by avian sarcoma viruses and the distribution of vinculin and actin in transformed cells: the role of vinculin phosphorylationGoogle Scholar
  5. Barnekow A, Bauer H, Boschek CB, Friis RR, Ziemiecki A (1981) Rous sarcoma virus transformation: action of the src gene product. In: Schweiger H (ed) International cell biology 1980–1981. Springer, Berlin, pp 457–466Google Scholar
  6. Barnekow A, Boschek CB, Ziemiecki A, Friis RR, Bauer H (1982) Demonstration of the Rous sarcoma virus pp60src and its associated protein kinase on the surface of intact cells. In: Winnacker E, Schoene H-H (eds) Genes and tumor genes. Raven, New York, pp 65–73Google Scholar
  7. Bauer H, Barnekow A, Rose G (1982) The transforming protein of Rous sarcoma virus pp60src: growth and cell proliferation inducing properties. In: Dumont JE, Nunez J, Schultz G (eds) Hormones and cell regulation, vol 6. Elsevier, New York, pp 187–205Google Scholar
  8. Beaufay H, Amar-Costesec A (1976) Cell fractionation techniques. In: Korn ED (ed) Methods in membrane biology, vol 6. Plenum, New York, pp 1–100CrossRefGoogle Scholar
  9. Beemon K, Hunter T (1978) Characterization of Rous sarcoma virus src gene products synthesized in vitro. J Virol 28: 551–566PubMedPubMedCentralGoogle Scholar
  10. Beemon K, Ryden T, McNelly EA (1982) Transformation by avian sarcoma viruses leads to phosphorylation of multiple cellular proteins on tyrosine residues. J Virol 42: 742–747PubMedPubMedCentralGoogle Scholar
  11. Ben-Ze’ev A, Duerr A, Solomon F, Penman S (1979) The outer boundary of the cytoskeleton: a lamina derived from plasma membrane proteins. Cell 17: 859–865PubMedCrossRefGoogle Scholar
  12. Birchmeier W, Liberman TA, Imhof BA, Kreis TE (1982) Intracellular and extracellular components involved in the formation of ventral cell surfaces of fibroblasts. Cold Spring Harbor Symp Quant Biol 46: 755–768PubMedCrossRefGoogle Scholar
  13. Bishop JM, Courtneidge SA, Levinson AD, Oppermann H, Quintrell N, Sheiness DK, Weiss SR, Varmus HE (1980) Origin and function of avian retrovirus transforming genes. Cold Spring Harbor Symp Quant Biol 44: 919–930PubMedCrossRefGoogle Scholar
  14. Blithe DB, Richert ND, Pastan IH (1982) Purification of a tyrosine-specific protein kinase from Rous sarcoma virus-induced rat tumor. J Biol Chem 257: 7135–7142PubMedGoogle Scholar
  15. Blobel G (1980) Intracellular protein topogenesis. Proc Natl Acad Sci USA 77: 1496–1500PubMedPubMedCentralCrossRefGoogle Scholar
  16. Brown S, Levinson W, Spudich JA (1976) Cytoskeletal elements of chick embryo fibroblasts revealed by detergent extraction. J Supramol Struct Cell Biochem 5: 119–130CrossRefGoogle Scholar
  17. Brugge JS, Erikson RL (1977) Identification of a transformation-specific antigen induced by an avian sarcoma virus. Nature 269: 346–348PubMedCrossRefGoogle Scholar
  18. Brugge JS, Darrow D (1982) Rous sarcoma virus-induced phosphorylation of a 50,000-molecular weight cellular protein. Nature 295: 250–253PubMedCrossRefGoogle Scholar
  19. Brugge JS, Steinbaugh PJ, Erikson RL (1978) Characterization of the avian sarcoma virus protein p60src. Virology 91: 130–140PubMedCrossRefGoogle Scholar
  20. Brugge JS, Erikson E, Erikson RL (1981) The specific interaction of the Rous sarcoma virus transforming protein, pp605rc, with two cellular proteins. Cell 25: 363–372PubMedCrossRefGoogle Scholar
  21. Brugge JS, Yonemoto W, Darrow D (1983) Interaction between the Rous sarcoma virus transforming protein and two cellular phosphoproteins: analysis of the turnover and distribution of this complex. Mol Cell Biol 3: 9–19PubMedPubMedCentralCrossRefGoogle Scholar
  22. Bryant D, Parsons JT (1982) Site-directed mutagenesis of the src gene of Rous sarcoma virus: construction and characterization of a deletion mutant temperature sensitive for transformation. J Virol 44: 683–691PubMedPubMedCentralGoogle Scholar
  23. Bunte T, Owada MK, Donner P, Boschek CB, Moelling K (1981) Association of the transformation-speciflc protein pp60src with the membrane of an avian sarcoma virus. J Virol 38: 1034–1047PubMedPubMedCentralGoogle Scholar
  24. Burr JG, Dreyfuss G, Penman S, Buchanan JM (1980) Association of the src gene product of Rous sarcoma virus with cytoskeletal structures of chicken embryo fibroblasts. Proc Natl Acad Sci USA 77: 3484–3488PubMedPubMedCentralCrossRefGoogle Scholar
  25. Burr JG, Lee SR, Buchanan JM (1981) In situ phosphorylation of proteins associated with the cytoskeleton of chick embryo fibroblasts. Cold Spring Harbor Conf Cell Prolif 8: 1217–1232Google Scholar
  26. Carr SA, Biemann K, Shoji S, Parmalee DC, Titani K (1982) n-Tetradecanoyl is the NH2-terminal blocking group of the catalytic subunit of cyclic AMP-dependent protein kinase from bovine cardiac muscle. Proc Natl Acad Sci USA 79: 6128–6131Google Scholar
  27. Cheng YSE, Chen LB (1981 a) Detection of phosphotyrosine-containing 34,000-dalton protein in the framework of cells transformed with Rous sarcoma virus. Proc Natl Acad Sci USA 78: 2388–2392Google Scholar
  28. Cheng YSE, Chen LB (1981b) Alterations in protein phosphorylation in cells transformed by Rous sarcoma virus. Cold Spring Harbor Conf Cell Prolif 8: 1233–1246Google Scholar
  29. Collett MS, Erikson RL (1978) Protein kinase activity associated with the avian sarcoma virus src gene product. Proc Natl Acad Sci USA 75: 2021–2024PubMedPubMedCentralCrossRefGoogle Scholar
  30. Collett MS, Purchio AF, Erikson RL (1980) Avian sarcoma virus transforming protein, pp60src, shows protein kinase activity specific for tyrosine. Nature 285: 167–169PubMedCrossRefGoogle Scholar
  31. Cooper JA, Hunter T (1981a) Changes in protein phosphorylation in Rous sarcoma virus-transformed chicken embryo cells. Mol Cell Biol 1: 165–178PubMedPubMedCentralCrossRefGoogle Scholar
  32. Cooper JA, Hunter T (1981b) Four different classes of retroviruses induce phosphorylation of tyrosines present in similar cellular proteins. Mol Cell Biol 1: 394–407PubMedPubMedCentralCrossRefGoogle Scholar
  33. Cooper JA, Hunter T (1981c) Similarities and differences between the effects of epidermal growth factor and Rous sarcoma virus. J Cell Biol 91: 878–883PubMedCrossRefGoogle Scholar
  34. Cooper JA, Hunter T (1982) Discrete primary locations of a tyrosine protein kinase and of three proteins that contain phosphotyrosine in virally transformed chick fibroblasts. J Cell Biol 94: 287–296PubMedCrossRefGoogle Scholar
  35. Cooper JA, Hunter T (1983) Identification and characterization of cellular targets for tyrosine protein kinases. J Biol Chem 258: 1108–1115PubMedGoogle Scholar
  36. Cooper JA, Hunter T (to be published) Analysis of substrates for tyrosine protein kinases. In: Squaw Valley Symposium: tumor viruses and differentiationGoogle Scholar
  37. Cooper JA, Nakamura KD, Hunter T, Weber MJ (1983 a) Phosphotyrosine-containing proteins and expression of transformation parameters in cells infected with partial transformation mutants of Rous sarcoma virus. J Virol 46: 15–28Google Scholar
  38. Cooper JA, Reiss NA, Schwartz RJ, Hunter T (1983 b) Three glycolytic enzymes are phosphorylated at tyrosine in cells transformed by Rous sarcoma virus. Nature 302: 218–223Google Scholar
  39. Courtneidge SA, Bishop JM (1982) The transit of pp60v -src to the plasma membrane. Proc Natl Acad Sci USA 79:7117–7121Google Scholar
  40. Courtneidge SA, Levinson AD, Bishop JM (1980) The protein encoded by the transforming gene of avian sarcoma virus (pp60src) and a homologous protein in normal cells (pp60proto-src) are associated with the plasma membrane. Proc Natl Acad Sci USA 77: 3783–3787PubMedPubMedCentralCrossRefGoogle Scholar
  41. Courtneidge SA, Ralston R, Alitalo K, Bishop JM (1983) Subcellular location of an abundant substrate (p36) for tyrosine-specific protein kinases. Mol Cell Biol 3: 340–350PubMedPubMedCentralCrossRefGoogle Scholar
  42. Curtis ASG (1964) The mechanism of adhesion of cells to glass. A study by interference reflection microscopy. J Cell Biol 20: 199–215PubMedPubMedCentralCrossRefGoogle Scholar
  43. David-Pfeuty T, Singer SJ (1980) Altered distributions of cytoskeletal proteins vinculin and alpha-actinin in cultured fibroblasts transformed by Rous sarcoma virus. Proc Natl Acad Sci USA 77: 6687–6691PubMedPubMedCentralCrossRefGoogle Scholar
  44. de Duve C (1971) Tissue fractionation. J Cell Biol 50: 20D–55DPubMedCrossRefGoogle Scholar
  45. de Petris S (1978) Immunoelectron microscopy and immunofluorescence in membrane biology. In: Korn ED (ed) Methods in membrane biology, vol 9. Plenum, New York, pp 1–201CrossRefGoogle Scholar
  46. Dunn GA, Heath JP (1976) A new hypothesis of contact guidance in tissue cells. Exp Cell Res 101: 1–14PubMedCrossRefGoogle Scholar
  47. Emmelot P, Bos JC (1966) Differences in the association of two glycolytic enzymes with plasma membranes isolated from rat liver and hepatoma. Biochim Biophys Acta 121: 434–436PubMedCrossRefGoogle Scholar
  48. Erikson E, Erikson RL (1980) Identification of a cellular protein substrate phosphorylated by the avian sarcoma virus-transforming gene product. Cell 21: 829–836PubMedCrossRefGoogle Scholar
  49. Erikson E, Collett MS, Erikson RL (1978) In vitro synthesis of a functional avian sarcoma virus transforming gene product. Nature 274: 919–921PubMedCrossRefGoogle Scholar
  50. Erikson E, Cook R, Miller GJ, Erikson RL (1981a) The same normal cell protein is phosphorylated after transformation by avian sarcoma viruses with unrelated transforming genes. Mol Cell Biol 1: 43–50PubMedPubMedCentralCrossRefGoogle Scholar
  51. Erikson E, Shealy DJ, Erikson RL (1981b) Evidence that viral transforming gene products and epidermal growth factor stimulate phosphorylation of the same cellular protein with similar specificity. J Biol Chem 256: 11381–11384PubMedGoogle Scholar
  52. Erikson RL (1981) The transforming protein of avian sarcoma viruses and its homologue in normal cells. Curr Top Microbiol Immunol 91: 25–40PubMedGoogle Scholar
  53. Erikson RL, Collett MS, Erikson E, Purchio AF (1979) Evidence that the avian sarcoma virus transforming gene product is a cyclic AMP-independent protein kinase. Proc Natl Acad Sci USA 76: 6260–6264PubMedPubMedCentralCrossRefGoogle Scholar
  54. Erikson RL, Collett MS, Erikson E, Purchio AF, Brugge JS (1980) Protein phosphorylation mediated by partially purified avian sarcoma virus transforming-gene product. Cold Spring Harbor Symp Quant Biol 44: 907–917PubMedCrossRefGoogle Scholar
  55. Feldman RA, Wang E, Hanafusa H (1983) Cytoplasmic localization of the transforming protein of Fujinami sarcoma virus: salt-sensitive association with subcellular components. J Virol 45: 782–791PubMedPubMedCentralGoogle Scholar
  56. Fleischer S, Packer L (1974) Biomembranes (part A). Methods Enzymology, vol 31. Academic, New YorkGoogle Scholar
  57. Gallis B, Bornstein P, Brautigan DL (1981) Tyrosylprotein kinase and phosphatase activities in membrane vesicles from normal and Rous sarcoma virus-transformed rat cells. Proc Natl Acad Sci USA 78: 6689–6693PubMedPubMedCentralCrossRefGoogle Scholar
  58. Garber EA, Krueger JG, Goldberg AR (1982) Novel localization of pp60src in Rous sarcoma virus-transformed rat and goat cells and in chicken cells transformed by viruses rescued from these mammalian cells. Virology 118: 419–429PubMedCrossRefGoogle Scholar
  59. Garber EA, Krueger JG, Hanafusa H, Goldberg AR (1983 a) Temperature-sensitive membrane association of pp60src in tsNY68-infected cells correlates with increased tyrosine phosphorylation of membrane-associated proteins. Virology 126: 73–86Google Scholar
  60. Garber EA, Krueger JG, Hanafusa H, Goldberg AR (1983 b) Only membrane-associated RSV src proteins have amino-terminally bound lipid. Nature 302: 161–163Google Scholar
  61. Geiger B (1979) A 130K protein from chicken gizzard: its localization at the termini of microfilament bundles in cultured cells. Cell 18: 193–205PubMedCrossRefGoogle Scholar
  62. Geiger B (1982) Microheterogeneity of avian and mammalian vinculin: distinctive subcellular distribution of different isovinculins. J Mol Biol 159: 685–701PubMedCrossRefGoogle Scholar
  63. Geiger B, Tokuyasu KT, Dutton AH, Singer SJ (1980) Vinculin, an intracellular protein localized at specialized sites where actin microfilament bundles terminate at cell membranes. Proc Natl Acad Sci USA 77: 4127–4131PubMedPubMedCentralCrossRefGoogle Scholar
  64. Gilmer TM, Erikson RL (1981) Rous sarcoma virus transforming protein, p60src, expressed in E. coli, functions as a protein kinase. Nature 294: 771–773PubMedGoogle Scholar
  65. Gilmore T, Radke K, Martin GS (1982) Tyrosine phosphorylation of a 50k cellular polypeptide associated with the Rous sarcoma virus-transforming protein, pp60src. Mol Cell Biol 2: 199–206PubMedPubMedCentralCrossRefGoogle Scholar
  66. Glick MC (1975) Isolation of surface membranes from mammalian cells. In: Jamieson GA, Robinson DM (eds) Mammalian cell membranes, vol 1. Butterworth, Boston, pp 47–71Google Scholar
  67. Goldberg AR, Krueger JG, Wang E (1980) Localization and characterization of the src-gene product of Rous sarcoma virus. Cold Spring Harbor Symp Quant Biol 44: 991–1005PubMedCrossRefGoogle Scholar
  68. Graziani Y, Erikson E, Erikson RL (1983) Evidence that the Rous sarcoma virus transforming gene product is associated with glycerol kinase activity. J Biol Chem 258: 2126–2129PubMedGoogle Scholar
  69. Greenberg ME, Edelman GM (1983 a) Comparison of the 34,000 dalton pp60src substrate and a 38,000 dalton phosphoprotein identified by monoclonal antibodies. J Biol Chem 258: 8497–8502Google Scholar
  70. Greenberg ME, Edelman GM (1983 b) The 34kD-pp60src substrate is located at the inner face of the plasma membrane. Cell 33: 767–779Google Scholar
  71. Hanafusa H (1977) Cell transformation by RNA tumor viruses. In: Fraenkel-Conrat H, Wagner RR (eds) Comprehensive virology, vol 10. Plenum, New York, pp 401–483Google Scholar
  72. Hanafusa H, Halpern CC, Buchhagen DL, Kawai S (1977) Recovery of avian sarcoma virus from tumors induced by transformation-defective mutants. J Exp Med 146: 1735–1747PubMedCrossRefGoogle Scholar
  73. Hay AJ (1974) Studies on the formation of the influenza virus envelope. Virology 60: 398–418PubMedCrossRefGoogle Scholar
  74. Heath JP, Dunn GA (1978) Cell to substratum contacts of chick fibroblasts and their relation to the microfilament system. A correlated interference-reflection and high-voltage electron-microscope study. J Cell Sci 29: 197–212Google Scholar
  75. Heaysman JEM, Pegrum SM (1973) Early contacts between fibroblasts. Exp Cell Res 78: 71–78PubMedCrossRefGoogle Scholar
  76. Henderson D, Weber K (1979) Three-dimensional organization of microfilaments and microtubules in the cytoskeleton. Exp Cell Res 124: 301–316PubMedCrossRefGoogle Scholar
  77. Henderson LE, Krutzsch HC, Oroszlan S (1983) Myristyl amino-terminal acylation of murine retrovirus proteins: an unusual post-translational protein modification. Proc Natl Acad Sci USA 80: 339–343PubMedPubMedCentralCrossRefGoogle Scholar
  78. Hunter T (1980) Proteins phosphorylated by the RSV transforming function. Cell 22:647–648Google Scholar
  79. Hunter T, Sefton BM (1980) The transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proc Natl Acad Sci USA 77: 1311–1315Google Scholar
  80. Hunter T, Cooper J A (1981) Epidermal growth factor induces rapid tyrosine phosphorylation of proteins in A431 human tumor cells. Cell 24: 741–752PubMedCrossRefGoogle Scholar
  81. Hunter T, Sefton BM, Cooper JA (1981) Phosphorylation of tyrosine: its importance in viral transformation and normal cell metabolism. Cold Spring Harbor Conf Cell Prolif 8: 1189–1202Google Scholar
  82. Hynes R (1982) Phosphorylation of vinculin by pp60src: what might it mean? Cell 28: 437–438PubMedCrossRefGoogle Scholar
  83. Hynes RO, Destree AT (1978) Relationships between flbronectin ( LETS) protein and actin. Cell 15: 875–886Google Scholar
  84. Ito S, Richert N, Pastan I (1982) Phospholipids stimulate phosphorylation of vinculin by the tyrosine-specifle protein kinase of Rous sarcoma virus. Proc Natl Acad Sci USA 79: 4628–4631PubMedPubMedCentralCrossRefGoogle Scholar
  85. Izzard CS, Lochner LR (1976) Cell-to-substrate contacts in living fibroblasts: an interference reflexion study with an evaluation of the technique. J Cell Sci 21: 129–159PubMedGoogle Scholar
  86. Kahn P, Nakamura K, Shin S, Smith RE, Weber MJ (1982) Tumorigenicity of partial transformation mutants of Rous sarcoma virus. J Virol 42: 602–611PubMedPubMedCentralGoogle Scholar
  87. Kamine J, Buchanan JM (1978) Processing of 60,000 dalton sarc gene protein synthesized by cell-free translation. Proc Natl Acad Sci USA 75: 4399–4403PubMedPubMedCentralCrossRefGoogle Scholar
  88. Kamine J, Burr JG, Buchanan JM (1980) In vitro synthesis and processing of Rous sarcoma virus src-gene products. Cold Spring Harbor Symp Quant Biol 44: 943–948PubMedCrossRefGoogle Scholar
  89. Karess RE, Hanafusa H (1981) Viral and cellular src genes contribute to the structure of recovered avian sarcoma virus transforming protein. Cell 24: 155–164PubMedCrossRefGoogle Scholar
  90. Kawai S, Hanafusa H (1971) The effect of temperature on the transformed state of cells infected with a Rous sarcoma virus mutant. Virology 46: 470–479PubMedCrossRefGoogle Scholar
  91. Kelley PM, Schlesinger MJ (1982) Antibodies to two major chicken heat shock proteins cross-react with similar proteins in widely divergent species. Mol Cell Biol 2: 267–274PubMedPubMedCentralCrossRefGoogle Scholar
  92. Kobayashi N, Kaji AJ (1980) Phosphoprotein associated with activation of the src gene product in myogenic cells. Biochem Biophys Res Comm 93: 278–284PubMedCrossRefGoogle Scholar
  93. Kobayashi N, Tanaka A, Kaji A (1981) In vitro phosphorylation of the 36 k protein in extracts from Rous sarcoma virus-transformed chicken fibroblasts. J Biol Chem 256: 3053–3058PubMedGoogle Scholar
  94. Krebs EG, Beavo J A (1979) Phosphorylation-dephosphorylation of enzymes. Ann Rev Biochem 48: 923–959PubMedCrossRefGoogle Scholar
  95. Krueger JG, Wang E, Goldberg AR (1980 a) Evidence that the src gene product of Rous sarcoma virus is membrane associated. Virology 101: 25–40Google Scholar
  96. Krueger JG, Wang E, Garber EA, Goldberg AR (1980 b) Differences in intracellular location of pp60src in rat and chicken cells transformed by Rous sarcoma virus. Proc Natl Acad Sci USA 77: 4142–4146Google Scholar
  97. Krueger JG, Garber EA, Goldberg AR, Hanafusa H (1982) Changes in aminoterminal sequences of pp60src lead to decreased membrane association and decreased in vivo tumorigenicity. Cell 28: 889–896PubMedCrossRefGoogle Scholar
  98. Krzyzek RA, Mitchell RL, Lau AF, Faras AJ (1980) Association of pp60src and src protein kinase activity with the plasma membrane of nonpermissive and permissive avian sarcoma virus-infected cells. J Virol 36: 805–815PubMedPubMedCentralGoogle Scholar
  99. Lau AF, Krzyzek RA, Brugge JS, Erikson RL, Schollmeyer J, Faras AJ (1979) Morphological revertants of an avian sarcoma virus-transformed mammalian cell line exhibit tumorigenicity and contain pp60src. Proc Natl Acad Sci USA 76: 3904–3908PubMedPubMedCentralCrossRefGoogle Scholar
  100. Lau AF, Krzyzek RA, Faras AJ (1981) Loss of tumorigenicity correlates with a reduction in pp60src kinase activity in a revertant subclone of avian sarcoma virus-infected field vole cells. Cell 23: 815–823PubMedCrossRefGoogle Scholar
  101. Lee JS, Varmus HE, Bishop JM (1979) Virus-specific messenger RNAs in permissive cells infected by avian sarcoma virus. J Biol Chem 254: 8015–8022PubMedGoogle Scholar
  102. Levinson AD, Oppermann H, Levintow L, Varmus HE, Bishop JM (1978) Evidence that the transforming gene of avian sarcoma virus encodes a protein kinase associated with a phosphoprotein. Cell 15: 561–572PubMedCrossRefGoogle Scholar
  103. Levinson AD, Oppermann H, Varmus HE, Bishop JM (1980) The purified product of the transforming gene of avian sarcoma virus phosphorylates tyrosine. J Biol Chem 255: 11973–11980PubMedGoogle Scholar
  104. Levinson AD, Courtneidge SA, Bishop JM (1981) Structural and functional domains of the Rous sarcoma virus transforming protein (pp60src). Proc Natl Acad Sci USA 78: 1624–1628PubMedPubMedCentralCrossRefGoogle Scholar
  105. Lipsich LA, Cutt JR, Brugge JS (1982) Association of the transforming proteins of Rous, Fujinami, and Y73 avian sarcoma viruses with the same two cellular proteins. Mol Cell Biol 2: 875–880PubMedPubMedCentralCrossRefGoogle Scholar
  106. Maness P, Engeser H, Greenberg ME, O’Farrell M, Gall WE, Edelman GM (1979) Characterization of the protein kinase activity of avian sarcoma virus src gene product. Proc Natl Acad Sci USA 76: 5028–5032PubMedPubMedCentralCrossRefGoogle Scholar
  107. Martin GS (1970) Rous sarcoma virus: a function required for the maintenance of the transformed state. Nature 227: 1021–1023PubMedCrossRefGoogle Scholar
  108. Martinez R, Nakamura KD, Weber MJ (1982) Identification of phosphotyrosine-containing proteins in untransformed and Rous sarcoma virus-transformed chicken embryo fibroblasts. Mol Cell Biol 2: 653–665PubMedPubMedCentralCrossRefGoogle Scholar
  109. McGrath JP, Levinson AD (1982) Bacterial expression of an enzymatically active protein encoded by RSV src gene. Nature 295: 423–425PubMedCrossRefGoogle Scholar
  110. Nakamura KD, Weber MJ (1982) Phosphorylation of a 36,000 Mr cellular protein in cells infected with partial transformation mutants of Rous sarcoma virus. Mol Cell Biol 2: 147–153PubMedPubMedCentralCrossRefGoogle Scholar
  111. Nakamura KD, Martinez R, Weber MJ (1983) Tyrosine phosphorylation of specific proteins after mitogen stimulation of chicken embryo fibroblasts. Mol Cell Biol 3: 380–390PubMedPubMedCentralCrossRefGoogle Scholar
  112. Neville DM (1975) Isolation of cell surface membrane fractions from mammalian cells and organs. In: Korn ED (ed) Methods in membrane biology, vol 3. Plenum, New York, pp 1–49CrossRefGoogle Scholar
  113. Nigg EA, Sefton BM, Hunter T, Walter G, Singer SJ (1982 a) Immunofluorescent localization of the transforming protein of Rous sarcoma virus with antibodies against a synthetic src peptide. Proc Natl Acad Sci USA 79: 5322–5326Google Scholar
  114. Nigg EA, Walter G, Singer SJ (1982 b) On the nature of crossreactions observed with antibodies directed to defined epitopes. Proc Natl Acad Sci USA 79: 5939–5943Google Scholar
  115. O’Farrell PH (1975) High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250: 4007–4021PubMedPubMedCentralGoogle Scholar
  116. O’Farrell PZ, Goodman HM, O’Farrell PH (1977) High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12: 1133–1142PubMedCrossRefGoogle Scholar
  117. Oppermann H, Levinson AD, Levintow L, Varmus HE, Bishop JM, Kawai S (1981a) Two cellular proteins that immunoprecipitate with the transforming protein of Rous sarcoma virus. Virology 113: 736–751PubMedCrossRefGoogle Scholar
  118. Oppermann H, Levinson W, Bishop JM (1981b) A cellular protein that associates with the transforming protein of Rous sarcoma virus is also a heat-shock protein. Proc Natl Acad Sci USA 78: 1067–1071PubMedPubMedCentralCrossRefGoogle Scholar
  119. Osborn M, Weber K (1977) The detergent-resistant cytoskeleton of tissue culture cells includes the nucleus and the microfilament bundles. Exp Cell Res 106: 339–349PubMedCrossRefGoogle Scholar
  120. Owada M-K, Donner P, Scott A, Moelling K (1981) Isolation of an avian sarcoma virus-specific protein kinase from virus particles. Virology 110: 333–343PubMedCrossRefGoogle Scholar
  121. Pastan IH, Willingham M, de Crombrugghe B, Gottesman MM (1982) Aging and cancer: cyclic 3/,5/-adenosine monophosphate and altered gene activity. Natl Cancer Inst Monogr 60: 7–15Google Scholar
  122. Purchio AF, Erikson E, Erikson RL (1977) Translation of 35S and of subgenomic regions of avian sarcoma virus RNA. Proc Natl Acad Sci USA 74: 4661–4665PubMedPubMedCentralCrossRefGoogle Scholar
  123. Purchio AF, Jananovich S, Erikson RL (1980) Sites of synthesis of viral proteins in avian sarcoma virus-infected chicken cells. J Virol 35: 629–636PubMedPubMedCentralGoogle Scholar
  124. Quinn PJ (1976) The molecular biology of cell membranes. University Park Press, BaltimoreGoogle Scholar
  125. Radke K, Martin GS (1979) Transformation by Rous sarcoma virus: effects of the src gene expression on the synthesis and phosphorylation of cellular polypeptides. Proc Natl Acad Sci USA 76: 5212–5216PubMedPubMedCentralCrossRefGoogle Scholar
  126. Radke K, Martin GS (1980) Transformation by Rous sarcoma virus: effects of the src gene expression on the synthesis and phosphorylation of cellular polypeptides. Cold Spring Harbor Symp Quant Biol 44: 975–982PubMedCrossRefGoogle Scholar
  127. Radke K, Gilmore T, Martin GS (1980) Transformation by Rous sarcoma virus: a cellular protein substrate for transformation-specific protein phosphorylation contains phosphotyrosine. Cell 21: 821–828PubMedCrossRefGoogle Scholar
  128. Revel JP, Wolken K (1973) Electron microscope investigations of the underside of cells in culture. Exp Cell Res 78: 1–14PubMedCrossRefGoogle Scholar
  129. Richert ND, Blithe DB, Pastan IH (1982) Properties of the src kinase purified from Rous sarcoma virus-induced rat tumors. J Biol Chem 257: 7143–7150PubMedGoogle Scholar
  130. Robinson GB (1975) The isolation and composition of membranes. In: Parsons DS (ed) Biological membranes. Clarendon, Oxford, pp 8-54Google Scholar
  131. Rohrschneider LR (1979) Immunofluorescence on avian sarcoma virus-transformed cells: localization of the src gene product. Cell 16: 11–24Google Scholar
  132. Rohrschneider LR (1980) Adhesion plaques of Rous sarcoma virus-transformed cells contain the src gene product. Proc Natl Acad Sci USA 77: 3514–3518PubMedPubMedCentralCrossRefGoogle Scholar
  133. Rohrschneider LR, Rosok MJ (1983) Transformation parameters and pp60src localization in cells infected with partial transformation mutants of Rous sarcoma virus. Mol Cell Biol 3: 731–746PubMedPubMedCentralCrossRefGoogle Scholar
  134. Rohrschneider LR, Rosok M, Shriver K (1982) Mechanism of transformation by Rous sarcoma virus: events within adhesion plaques. Cold Spring Harbor Symp Quant Biol 46: 953–965PubMedCrossRefGoogle Scholar
  135. Rosok MJ, Rohrschneider LR (1983) Increased phosphorylation of vinculin on tyrosine does not occur during the release of stress fibers before mitosis in normal cells. Mol Cell Biol 3: 475–479PubMedPubMedCentralCrossRefGoogle Scholar
  136. Rous P (1911) A sarcoma of the fowl transmissible by an agent separable from the tumor cells. J Exp Med 13: 397–411PubMedPubMedCentralCrossRefGoogle Scholar
  137. Rubsamen H, Friis RR, Bauer H (1979) src Gene product from different strains of avian sarcoma virus: kinetics and possible mechanism of heat inactivation of protein kinase activity from cells infected by transformation-defective, temperature-sensitive mutant and wildtype virus. Proc Natl Acad Sci USA 76: 967–971Google Scholar
  138. Rubsamen H, Saltenberger K, Friis RR, Eigenbrodt E (1982) Cytosolic malic dehydrogenase activity is associated with a putative substrate for the transforming gene product of Rous sarcoma virus. Proc Natl Acad Sci USA 79: 228–232PubMedPubMedCentralCrossRefGoogle Scholar
  139. Schaffhausen BS, Dorai H, Arakere G, Benjamin TL (1982) Polyoma virus middle T antigen: relationship to cell membranes and apparent lack of ATP-binding activity. Mol Cell Biol 2: 1187–1198PubMedPubMedCentralCrossRefGoogle Scholar
  140. Schlesinger MJ, Magee AI, Schmidt MFG (1980) Fatty acid acylation of proteins in cultured cells. J Biol Chem 255: 10021–10024PubMedGoogle Scholar
  141. Schliwa M, van Blerkom J, Porter KR (1981) Stabilization of the cytoplasmic ground substance in detergent opened cells and a structural and biochemical analysis of its composition. Proc Natl Acad Sci USA 78: 4329–4333PubMedPubMedCentralCrossRefGoogle Scholar
  142. Schmidt MFG (1982) Acylation of viral spike glycoproteins: a feature of enveloped RNA viruses. Virology 116: 327–338PubMedCrossRefGoogle Scholar
  143. Schmidt MFG, Schlesinger MJ (1979) Fatty acid binding to vesicular stomatitis virus glycoprotein: a new type of post-translational modification of viral glycoproteins. Cell 17: 813–819PubMedCrossRefGoogle Scholar
  144. Schmidt MFG, Schlesinger MJ (1980) Relation of fatty acid attachment to the translation and maturation of vesicular stomatitis and Sindbis virus membrane glycoproteins. J Biol Chem 255: 3334–3339PubMedGoogle Scholar
  145. Schmidt MFG, Bracha M, Schlesinger MJ (1979) Evidence for covalent attachment of fatty acids to Sindbis virus glycoproteins. Proc Natl Acad Sci USA 76: 1687–1691PubMedPubMedCentralCrossRefGoogle Scholar
  146. Schultz AM, Oroszlan S (1983) In vivo modification of retroviral gag gene-encoded polyproteins by myristic acid. J Virol 46: 355–361PubMedPubMedCentralGoogle Scholar
  147. Sefton BM, Walter G (1982) Antiserum specific for the carboxy terminus of the transforming protein of Rous sarcoma virus. J Virol 44: 467–474PubMedPubMedCentralGoogle Scholar
  148. Sefton BM, Beemon K, Hunter T (1978) Comparison of the expression of the src gene of the Rous sarcoma virus in vitro and in vivo. J Virol 28: 957–971PubMedPubMedCentralGoogle Scholar
  149. Sefton BM, Hunter T, Beemon K (1979) Product of in vitro translation of the Rous sarcoma virus src gene has protein kinase activity. J Virol 30: 311–318PubMedPubMedCentralGoogle Scholar
  150. Sefton BM, Hunter T, Beemon K (1980 a) Temperature-sensitive transformation by Rous sarcoma virus and temperature-sensitive protein kinase activity. J Virol 33: 220–229Google Scholar
  151. Sefton BM, Hunter T, Beemon K, Eckhart W (1980 b) Evidence that the phosphorylation of tyrosine is essential for cellular transformation by Rous sarcoma virus. Cell 20: 807–816Google Scholar
  152. Sefton BM, Hunter T, Ball EH, Singer SJ (1981) Vinculin: a cytoskeletal target of the transforming protein of Rous sarcoma virus. Cell 24: 165–174PubMedCrossRefGoogle Scholar
  153. Sefton BM, Hunter T, Nigg EA, Singer SJ, Walter G (1982a) Cytoskeletal targets for viral transforming proteins with tyrosine protein kinase activity. Cold Spring Harbor Symp Quant Biol 46: 939–951PubMedCrossRefGoogle Scholar
  154. Sefton BM, Trowbridge IS, Cooper JA, Scolnick EM (1982b) The transforming proteins of Rous sarcoma virus, Harvey sarcoma virus, and Abelson virus contain tightly-bound lipid. Cell 31: 465–474Google Scholar
  155. Shriver K, Rohrschneider LR (1981 a) Organization of pp60src and selected cytoskeletal proteins within adhesion plaques and junctions of Rous sarcoma virus-transformed rat cells. J Cell Biol 89: 525–535Google Scholar
  156. Shriver K, Rohrschneider LR (1981b) Spatial and enzymatic interaction of pp60src with cytoskeletal proteins in isolated adhesion plaques and junctions from RSV-transformed NRK cells. Cold Spring Harbor Conf Cell Prolif 8: 1247–1262Google Scholar
  157. Singer I (1979) The fibronexus: a transmembrane association of fibronectin-containing fibers and bundles of 5 nm microfilaments in hamster and human fibroblasts. Cell 16: 675–685PubMedCrossRefGoogle Scholar
  158. Singer I, Paradiso PR (1981) A transmembrane relationship between flbronectin and vinculin (130 kd protein): serum modulation in normal and transformed hamster fibroblasts. Cell 24: 481–492PubMedCrossRefGoogle Scholar
  159. Singer SJ (1974) The molecular organization of membranes. Ann Rev Biochem 43: 805–833PubMedCrossRefGoogle Scholar
  160. Smuckler EA, Koplitz M, Smuckler DE (1976) Isolation of animal cell nuclei. In: Birnie GD (ed) Subnuclear components; preparation and fractionation. Butterworth, Boston, pp 1–58CrossRefGoogle Scholar
  161. Takeya T, Hanafusa H (1982) DNA sequence of the viral and cellular src gene of chickens. II. Comparison of the src genes of two strains of ASV and of the cellular homolog. J Virol 44: 12–18PubMedPubMedCentralGoogle Scholar
  162. Takeya T, Feldman RA, Hanafusa H (1982) DNA sequence of the viral and cellular src gene of chickens. I. Complete nucleotide sequence of an EcoRI fragment of recovered avian sarcoma virus which codes for gp37 and pp60src. J Virol 44: 1–11PubMedPubMedCentralGoogle Scholar
  163. Trotter J A, Foerder BA, Keller JM (1978) Intracellular fibres in cultured cells: analysis by scanning and transmission microscopy and by SDS-polyacrylamide gel electrophoresis. J Cell Sci 31: 369–392PubMedGoogle Scholar
  164. Wang E, Yin HL, Krueger JG, Caliguiri LA, Tamm I (to be published) Unphosphorylated gelsolin is localized in regions of cell substratum contact or attachment in Rous sarcoma virus-transformed rat cells. J Cell BiolGoogle Scholar
  165. Warren L, Glick MC (1971) The isolation of surface membranes of animal cells: a survey. In: Manson LA (ed) Biomembranes, vol 1. Plenum, New York, pp 257–288CrossRefGoogle Scholar
  166. Warren L, Glick MC, Nass MK (1966) Membranes of animal cells. I. Methods of isolation of the surface membrane. J Cell Physiol 68: 269–288Google Scholar
  167. Webster RE, Henderson D, Osborn M, Weber K (1978) Three-dimensional electron microscopical visualization of the cytoskeleton of animal cells: immunoferritin identification of actin- and tubulin-containing structures. Proc Natl Acad Sci USA 75: 5511–5515PubMedPubMedCentralCrossRefGoogle Scholar
  168. Wehland J, Osborn M, Weber K (1979) Cell-to-substratum contacts in living cells: a direct correlation between interference-reflection and indirect-immunofluorescence microscopy using antibodies against actin and alpha-actinin. J Cell Sci 37: 257–273PubMedGoogle Scholar
  169. Weiss R, Teich N, Varmus H, Coffin J (eds) (1982) RNA tumor viruses. Molecular biology of tumor viruses, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, New YorkGoogle Scholar
  170. Willingham MC, Yamada SS, Pastan I (1978) Ultrastructural antibody localization of alpha-2-macroglobulin in membrane-limited vesicles in cultured cells. Proc Natl Acad Sci USA 75: 4359–4363PubMedPubMedCentralCrossRefGoogle Scholar
  171. Willingham MC, Jay G, Pastan I (1979) Localization of ASV src gene product to the plasma membrane of transformed cells by electron microscopic immunocytochemistry. Cell 18: 125–134PubMedCrossRefGoogle Scholar
  172. Willingham MC, Pastan I, Shih TY, Scolnick EM (1980) Localization of the src gene product of the Harvey strain of MSV to plasma membrane of transformed cells by electron microscopic immunocytochemistry. Cell 19: 1005–1014PubMedCrossRefGoogle Scholar
  173. Witt DP, Gordon JA (1980) Specific dephosphorylation of membrane proteins in Rous sarcoma virus-transformed chick embryo fibroblasts. Nature 287: 241–244PubMedCrossRefGoogle Scholar
  174. Yu J, Fischman DA, Steck TL (1973) Selective solubilization of proteins and phospholipids from red blood cell membranes by nonionic detergents. J Supramol Struct 1: 233–248PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin · Heidelberg 1983

Authors and Affiliations

  • James G. Krueger
    • 1
  • Ellen A. Garber
    • 1
  • Allan R. Goldberg
    • 1
  1. 1.The Rockefeller UniversityNew YorkUSA

Personalised recommendations