Homology between phosphotyrosine acceptor site of human c-abl and viral oncogene products

Nature
|July 14, 1983
PubMed

Insights

Researchers identified the tyrosine phosphorylation acceptor sites of the Abelson murine leukaemia virus oncogene (v-abl) and its human homologue (c-abl). This revealed extensive sequence homology with other viral oncogenes, suggesting a common evolutionary origin.

Area of Science:

  • Molecular Biology
  • Oncology
  • Biochemistry

Background:

  • Viral oncogenes encoding tyrosine-specific protein kinases are crucial in cancer development.
  • Known oncogenes like v-src, v-yes, and v-fes/fps share sequence homology, particularly at phosphorylation sites.

Purpose of the Study:

  • To identify and determine the nucleic acid sequences of tyrosine phosphorylation acceptor sites for v-abl and c-abl.
  • To investigate the evolutionary relationship between c-abl and other tyrosine kinase oncogenes.

Main Methods:

  • Nucleic acid sequencing to determine the genetic sequences of specific oncogene regions.
  • Comparative sequence analysis to identify homologies between different oncogenes.

Main Results:

  • The nucleic acid sequences for the tyrosine phosphorylation acceptor sites of v-abl and c-abl were determined.
  • Extensive sequence homology was found between the c-abl acceptor domain and those of v-src, v-yes, and v-fes/fps.
  • Distant relatedness was also observed with the catalytic chain of cyclic AMP-dependent protein kinase.

Conclusions:

  • The findings suggest a common progenitor for the examined retroviral oncogene homologues with tyrosine protein kinase activity.
  • These oncogenes likely represent a diverse family of cellular protein kinases.
  • This evolutionary link provides insights into the development and function of protein kinases in cellular processes.

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