Phosphorylation of a 36,000 Molecular Weight Cellular Polypeptide in Rous Sarcoma Virus-Transformed Fibroblasts

The phosphorylation of a 34,000-molecular-weight (34K) cell protein, purported to be a substrate of the avian retrovirus pp60src-associated protein kinase activity, was compared in three types of Rous sarcoma virus-infected vole cells: fully transformed cells, partial revertants which are morphologically normal in appearance but retain their tumorigenic potential, and full revertants which are similar to normal vole cells in all parameters including a lack of tumorigenicity. Although similar amounts of 34K protein are present in all three cell types, phosphorylation of the 34K protein was significantly reduced in the full revertant cell type. The reduced phosphorylation occurred at the tyrosine residue.

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COMPARATIVE STUDIES IN ROUS SARCOMA WITH VIRUS, TUMOR CELLS, AND CHICK EMBRYO CELLS TRANSFORMED IN VITRO BY VIRUS

Journal of Experimental Medicine ◽

10.1084/jem.115.1.245 ◽

1962 ◽

Vol 115 (1) ◽

pp. 245-251 ◽

Cited By ~ 4

Author(s):

Robert M. Dougherty ◽

Herbert R. Morgan

Keyword(s):

Chick Embryo ◽

Tumor Cells ◽

Comparative Studies ◽

Rous Sarcoma Virus ◽

Rous Sarcoma ◽

Transformed Fibroblasts ◽

Embryo Cells ◽

Sarcoma Virus

Chick embryo fibroblasts infected in vitro with Rous sarcoma virus have properties similar to tumor cells when injected into virus-immune chickens. When such virus-transformed fibroblasts are injected into normal chickens, they apparently participate in the production of tumors independent of their release of virus and are thus apparently malignant in vivo.

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The low molecular weight RNAs of Rous sarcoma virus

Virology ◽

10.1016/0042-6822(70)90251-5 ◽

1970 ◽

Vol 42 (1) ◽

pp. 182-195 ◽

Cited By ~ 90

Author(s):

J.Michael Bishop ◽

Warren E. Levinson ◽

Nancy Quintrell ◽

Drew Sullivan ◽

Lois Fanshier ◽

...

Keyword(s):

Molecular Weight ◽

Rous Sarcoma Virus ◽

Low Molecular Weight ◽

Rous Sarcoma ◽

Sarcoma Virus

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Rous sarcoma virus-transformed fibroblasts and cells of monocytic origin display a peculiar dot-like organization of cytoskeletal proteins involved in microfilament-membrane interactions*1

Experimental Cell Research ◽

10.1016/0014-4827(87)90238-2 ◽

1987 ◽

Vol 169 (1) ◽

pp. 202-214 ◽

Cited By ~ 144

Author(s):

P MARCHISIO

Keyword(s):

Rous Sarcoma Virus ◽

Cytoskeletal Proteins ◽

Membrane Interactions ◽

Rous Sarcoma ◽

Transformed Fibroblasts ◽

Sarcoma Virus

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Correlation between phosphorylation of a 34,000-molecular-weight protein, pp60src-associated kinase activity, and tumorigenicity in transformed and revertant vole cells.

Molecular and Cellular Biology ◽

10.1128/mcb.4.1.212 ◽

1984 ◽

Vol 4 (1) ◽

pp. 212-215 ◽

Cited By ~ 5

Author(s):

J F Nawrocki ◽

A F Lau ◽

A J Faras

Keyword(s):

Molecular Weight ◽

Rous Sarcoma Virus ◽

Kinase Activity ◽

Cell Types ◽

Cell Protein ◽

Protein Kinase Activity ◽

Rous Sarcoma ◽

Tumorigenic Potential ◽

Sarcoma Virus ◽

Weight Protein

The phosphorylation of a 34,000-molecular-weight (34K) cell protein, purported to be a substrate of the avian retrovirus pp60src-associated protein kinase activity, was compared in three types of Rous sarcoma virus-infected vole cells: fully transformed cells, partial revertants which are morphologically normal in appearance but retain their tumorigenic potential, and full revertants which are similar to normal vole cells in all parameters including a lack of tumorigenicity. Although similar amounts of 34K protein are present in all three cell types, phosphorylation of the 34K protein was significantly reduced in the full revertant cell type. The reduced phosphorylation occurred at the tyrosine residue.

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