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Activation of the receptor kinase domain of the trk oncogene by recombination with two different cellular sequences.

1988; Springer Nature; Volume: 7; Issue: 1 Linguagem: Inglês

10.1002/j.1460-2075.1988.tb02794.x

1460-2075

Sara C. Kozma, Shelagh Redmond, Xuebin Fu, Susanne Saurer, Bernd Groner, Nancy E. Hynes,

HER2/EGFR in Cancer Research

A new chimeric oncogene, trk-2h, has been generated by recombination of two segments of MDA-MB231 human breast carcinoma cell line DNA after transfection in NIH/3T3 cells. The rearranged DNA segments form a fused transcriptional unit. Sequences at the 3' end are homologous to the tyrosine kinase receptor moiety found in the trk oncogene which resembles a truncated growth factor receptor lacking part of its extracellular domain (Martin-Zanca et al., 1986). The 5' sequence of the trk-2h oncogene is contributed by a gene which is expressed in all human cells tested, and is not related to any known gene. Transfection of the receptor kinase domain DNA fragment into NIH/3T3 cells generated another oncogene, trk-3mh, which contains a mouse-specific sequence fused 5' to the receptor kinase. All three trk recombinants have the receptor kinase moiety fused to an activating amino terminus at the same nucleotide in their transcriptional product.