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Cartwright CA, Kaplan PL, Cooper JA, et al. Altered sites of tyrosine phosphorylation in pp60c-src associated with polyomavirus middle tumor antigen. Mol Cell Biol. 1986;6(5):1562-70doi: 10.1128/mcb.6.5.1562-1570.1986.
Cartwright, C. A., Kaplan, P. L., Cooper, J. A., Hunter, T., & Eckhart, W. (1986). Altered sites of tyrosine phosphorylation in pp60c-src associated with polyomavirus middle tumor antigen. Molecular and cellular biology, 6(5), 1562-70. https://doi.org/10.1128/mcb.6.5.1562-1570.1986
Cartwright, C A, et al. "Altered sites of tyrosine phosphorylation in pp60c-src associated with polyomavirus middle tumor antigen." Molecular and cellular biology vol. 6,5 (1986): 1562-70. doi: https://doi.org/10.1128/mcb.6.5.1562-1570.1986
Cartwright CA, Kaplan PL, Cooper JA, Hunter T, Eckhart W. Altered sites of tyrosine phosphorylation in pp60c-src associated with polyomavirus middle tumor antigen. Mol Cell Biol. 1986 May;6(5):1562-70. doi: 10.1128/mcb.6.5.1562-1570.1986. PMID: 2431281; PMCID: PMC367682.
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Atypon Free PMC Article

Mol Cell Biol. 1986 May;6(5):1562-70. doi: 10.1128/mcb.6.5.1562-1570.1986.

Altered sites of tyrosine phosphorylation in pp60c-src associated with polyomavirus middle tumor antigen.

Molecular and cellular biology

C A Cartwright, P L Kaplan, J A Cooper, T Hunter, W Eckhart

PMID: 2431281 PMCID: PMC367682 DOI: 10.1128/mcb.6.5.1562-1570.1986
Free PMC Article

Abstract

We characterized the tyrosine phosphorylation sites of free pp60c-src and of pp60c-src associated with the polyomavirus middle tumor antigen (mT) in transformed avian and rodent cells. The sites of tyrosine phosphorylation in the two populations of pp60c-src were different, both in vitro and in vivo. Free pp60c-src was phosphorylated in vitro at a single site, tyrosine 416. pp60c-src associated with mT was phosphorylated in vitro on tyrosine 416 and on one or more additional tyrosine residues located in the amino-terminal region of the molecule. Free pp60c-src in polyomavirus mT-transformed cells was phosphorylated in vivo on tyrosine 527. In contrast, pp60c-src associated with mT was phosphorylated in vivo on tyrosine 416 and not detectably on tyrosine 527. Thus, the in vivo phosphorylation sites of pp60c-src associated with mT in transformed cells are identical to those of pp60v-src, the Rous sarcoma virus transforming protein. The results suggest that altered phosphorylation of pp60c-src associated with mT may play a role in the enhancement of the pp60c-src protein kinase activity and in cell transformation by polyomavirus.

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