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. 1989 Jan;8(1):137–147. doi: 10.1002/j.1460-2075.1989.tb03358.x

Deletion of an N-terminal regulatory domain of the c-abl tyrosine kinase activates its oncogenic potential.

W M Franz 1, P Berger 1, J Y Wang 1
PMCID: PMC400782  PMID: 2496972

Abstract

The requirements for the oncogenic conversion of the c-abl proto-oncogene have been determined by the expression of N-terminal deleted forms and viral gag-fused forms of the c-abl proteins from a selectable retroviral vector. To activate the transforming potential of c-abl, it is necessary that (i) specific N-terminal amino acids are deleted to release the kinase from negative regulation in vivo; (ii) an N-terminal myristylation site is part of the activated kinase; (iii) the fatty-acylated, activated kinase is overproduced. The N-terminal amino acids found to be necessary for the cellular inhibition of c-abl tyrosine phosphorylation are part of a homologous region present in many non-receptor tyrosine kinases, the v-crk oncogene and phospholipase C-II. Overproduction of a deregulated and myristylated c-abl tyrosine kinase induces the transformation of NIH 3T3 cells.

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Selected References

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