The Gene Order of Avian RNA Tumor Viruses Derived from Biochemical Analyses of Deletion Mutants and Viral Recombinants

Lh, Wang

doi:10.1146/annurev.mi.32.100178.003021

Cited by 63 publications

(20 citation statements)

References 64 publications

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“…These findings indicate that the evolutionary derivation of src may have involved little or no modification of its cellular progenitor and could account for the apparent ease and frequency with which partially deleted src genes can be reconstituted by recombination with avian proto-src (Wang et al 1978).…”

Section: Is Oncucv Responsible For Neoplasticmentioning

confidence: 91%

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Origin and Function of Avian Retrovirus Transforming Genes

Bishop

Courtneidge

Levinson

et al. 1980

Cold Spring Harbor Symposia on Quantitative Biology

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Section: Is Oncucv Responsible For Neoplasticmentioning

confidence: 91%

“…The linear order of viral genes illustrated here has been documented elsewhere (Hu et al 1979;Mellon et al 1978;Wang 1978). A, denotes poly(A); c denotes a region of the avian retrovirus genome whose function is presently unknown.…”

Section: Methodsmentioning

confidence: 99%

Origin and Function of Avian Retrovirus Transforming Genes

Bishop

Courtneidge

Levinson

et al. 1980

Cold Spring Harbor Symposia on Quantitative Biology

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“…The transforming function of the virus is encoded in a single gene called src (1) and, so far, only a single transforming protein has been identified as the src gene product (2). This protein is a 60,000 Mr phosphoprotein (termed pp60Wc) (3-5) containing two major phosphorylation sites per molecule (6).…”

mentioning

confidence: 99%

Adhesion plaques of Rous sarcoma virus-transformed cells contain the src gene product.

Rohrschneider¹

1980

Proc. Natl. Acad. Sci. U.S.A.

299

143

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Another intracellular location of the Rous sarcoma virus (RSU) src gene product (pp6O(W) has been detected within RSV-transformed cells by indirect immunofluorescence. By using rabbit anti-tumor serum specific for pp6Os, a speckled pattern of fluorescence was found on the ventral surface of RSV (Schmidt-Ruppin strain)transformed normal rat kidney cells. Several tests indicated that this pattern was specific for pp6Orc. In addition, interference-reflection microscopy was used to visualize cellular adhesion plaques, which are the points at which cells attach to the substratum. Simultaneous immunofluorescence and interference-reflection microscopy indicated that the speckles of pp6Osrc fluorescence corresponded exactly to the adhesion p a ue structures. The presence of pp6C within the adhesion plaques was further demonstrated by indirect immunofluorescence on isolated adhesion plaques that remained bound to gass after removal of the cells. pEosrc also was observed in adhesion plaques of RSV-transformed chicken embryo fibroblasts (CEF) and mouse fibroblasts, as well as CEF infected with the temperature-sensitive RSV mutant tsNY68 and grown at permissive temperature. At nonpermissive temperature, pp60s was not detectable in adhesion plaques of the tsNY68-infected CEF. Adhesion plaques serve as focal points of microfilament bundle attachment, and these results suggest that pp6Osrc interacts directly with cellular cytoskeletal components.Rous sarcoma virus (RSV) has been a valuable tool for examining the mechanism of neoplastic transformation because it transforms a broad spectrum of avian and mammalian cells. The transforming function of the virus is encoded in a single gene called src (1) and, so far, only a single transforming protein has been identified as the src gene product (2). This protein is a 60,000 Mr phosphoprotein (termed pp60Wc) (3-5) containing two major phosphorylation sites per molecule (6). One site is probably regulated by a cyclic AMP-dependent protein kinase, whereas the second site may involve autophosphorylation through a unique kinase activity associated with pp60src. This kinase activity phosphorylates substrate proteins on tyrosine residues (7). That the kinase activity is indeed encoded in the src gene has been suggested by its invariable association with pp6Ofrc (8, 9), its temperature dependence in T-class mutants (4-6, 8, 9), and its copurification with partially purified pp6Osrc (10,11). These results all suggest that transformation in this system may result from mechanisms involving phosphorylation by pp6src.It is not known whether pp6Wrc interacts with many cellular target sites or whether a monofunctional pp60Wc acts at a single target to effect transformation and the numerous alterations associated with transformed cells (12). Transformation by RSV, however, is known to disrupt microfilament bundles, and therefore a cytoplasmic target for pp6osrc may directly or indirectly control the organization of microfilament bundles within the cytoplasm (13,14). This possibility is comp...

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“…Review: Avian retroviruses cellular gene (for reviews, see Bishop, 1978;Vogt & Hu, 1978;Wang, 1978;Coffin, 1979). This gene was subsequently shown to code for a protein of 60000 mol.…”

Section: Avian Sarcoma Virusesmentioning

confidence: 99%

Transforming Proteins of Avian Retroviruses

Hayman

1981

Journal of General Virology

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The Gene Order of Avian RNA Tumor Viruses Derived from Biochemical Analyses of Deletion Mutants and Viral Recombinants

Cited by 63 publications

References 64 publications

Origin and Function of Avian Retrovirus Transforming Genes

Origin and Function of Avian Retrovirus Transforming Genes

Adhesion plaques of Rous sarcoma virus-transformed cells contain the src gene product.

Transforming Proteins of Avian Retroviruses

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