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Phosphorylation of a 36,000 M/sub r/ cellular protein in cells infected with partial transformation mutants of Rous sarcoma virus

Journal Article · · Mol. Cell. Biol.; (United States)
DOI:https://doi.org/10.1128/MCB.2.2.147· OSTI ID:5996257
The authors isolated and characterized mutants of Rous sarcoma virus which induce some parameters of transformation but fail to fully induce other parameters. They believe these mutants code for a pp60/sup src/ which phosphorylates some targets well but phosphorylates others poorly. Using these mutants, they examined the phosphorylation of a 36,000 M/sub r/ protein which is phosphorylated on a tyrosine in cells transformed by Rous sarcoma virus, in an attempt to correlate this phosphorylation with the expression of specific transformation parameters. The authors found that phosphorylation of the 36,000 M/sub r/ protein was neither necessary nor sufficient for loss of fibronectin or for loss of density-dependent inhibition of growth. Phosphorylation of the protein was not sufficient for morphological alterations, increased hexose transport, or loss of adhesiveness. For the parameters measured, the best correlation was with increased plasminogen activator. In addition, it is noteworthy that cells infected with the mutant CU2 displayed low levels of phosphorylation of the 36,000 M/sub r/ protein and also were deficient in anchorage- independent growth and tumorigenicity, raising the possibility that the phosphorylation of the 36,000 M/sub r/ protein may be required for malignant growth properties.
Research Organization:
Dept. of Microbiology, Univ. of Illinois, Urbana, IL 61801
OSTI ID:
5996257
Journal Information:
Mol. Cell. Biol.; (United States), Journal Name: Mol. Cell. Biol.; (United States) Vol. 2:2; ISSN MCEBD
Country of Publication:
United States
Language:
English