Transformation of NIH 3T3 fibroblasts by an activated form of p59hck.
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.
Ziegler
S F
SF
Howard Hughes Medical Institute, University of Washington, Seattle 98195.
Levin
S D
SD
Perlmutter
R M
RM
D000595:Amino Acid Sequence; D000818:Animals; D002471:Cell Transformation, Neoplastic; D004247:DNA / Q000235:genetics*; D005347:Fibroblasts / Q000648:ultrastructure; D008239:Lysine / Q000235:genetics / Q000378:metabolism; D051379:Mice; D008979:Moloney murine leukemia virus / Q000235:genetics / Q000502:physiology; D009154:Mutation; D010641:Phenotype; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000235:genetics* / Q000378:metabolism; D014162:Transfection; D014443:Tyrosine / Q000378:metabolism
D014443:Tyrosine; D004247:DNA; D011505:Protein-Tyrosine Kinases; D008239:Lysine