Author(s): Bellacosa A, Testa JR, Staal SP, Tsichlis PN, Bellacosa A, Testa JR, Staal SP, Tsichlis PN
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Abstract The v-akt oncogene codes for a 105-kilodalton fusion phosphoprotein containing Gag sequences at its amino terminus. Sequence analysis of v-akt and biochemical characterization of its product revealed that it codes for a protein kinase C-related serine-threonine kinase whose cellular homolog is expressed in most tissues, with the highest amount found in thymus. Although Akt is a serine-threonine kinase, part of its regulatory region is similar to the Src homology-2 domain, a structural motif characteristic of cytoplasmic tyrosine kinases that functions in protein-protein interactions. This suggests that Akt may form a functional link between tyrosine and serine-threonine phosphorylation pathways.
This article was published in Science
and referenced in Journal of Biodiversity, Bioprospecting and Development