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. 1989 Jun;9(6):2724–2727. doi: 10.1128/mcb.9.6.2724

Transformation of NIH 3T3 fibroblasts by an activated form of p59hck.

S F Ziegler 1, S D Levin 1, R M Perlmutter 1
PMCID: PMC362345  PMID: 2503711

Abstract

Phosphorylation of a tyrosine residue near the carboxy terminus of src-family protein tyrosine kinases is believed to regulate the biological activity of these gene products. Conversion of this tyrosine in p59hck (Tyr-501) to a phenylalanine residue by using oligonucleotide-directed mutagenesis yielded a product (p59hckF501) with very potent transforming activity. Quantitative analysis by a soft-agar cloning assay revealed that p59hckF501 was more than 100-fold more effective than a closely related transforming element, p56lckF505, in colony formation. Cells bearing p59hckF501 had increased levels of protein phosphotyrosine. The ability of p59hckF501 to transform NIH 3T3 cells was abolished by a second mutation believed to destroy the ATP-binding domain.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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