A novel viral oncogene with structural similarity to phospholipase C
BJ Mayer, M Hamaguchi, H Hanafusa - Nature, 1988 - nature.com
BJ Mayer, M Hamaguchi, H Hanafusa
Nature, 1988•nature.comNumerous oncogenes have been isolated from acutely transforming retroviruses. To date,
the products of these viral oncogenes have been protein kinases, nuclear proteins, growth
factors, or GTP-binding proteins1, 2. We have cloned the previously uncharacterized avian
sarcoma virus CT10 and sequenced its genome. This virus encodes a protein, p47 gag-crk,
that has blocks of sequence similarity to the amino-terminal, non-catalytic region of the non-
receptor class of tyrosine kinases. In addition, the structure of p47 gag-crk has striking …
the products of these viral oncogenes have been protein kinases, nuclear proteins, growth
factors, or GTP-binding proteins1, 2. We have cloned the previously uncharacterized avian
sarcoma virus CT10 and sequenced its genome. This virus encodes a protein, p47 gag-crk,
that has blocks of sequence similarity to the amino-terminal, non-catalytic region of the non-
receptor class of tyrosine kinases. In addition, the structure of p47 gag-crk has striking …
Abstract
Numerous oncogenes have been isolated from acutely transforming retroviruses. To date, the products of these viral oncogenes have been protein kinases, nuclear proteins, growth factors, or GTP-binding proteins1,2. We have cloned the previously uncharacterized avian sarcoma virus CT10 and sequenced its genome. This virus encodes a protein, p47gag-crk, that has blocks of sequence similarity to the amino-terminal, non-catalytic region of the non-receptor class of tyrosine kinases. In addition, the structure of p47gag-crk has striking similarity to a 180-amino acid region of bovine brain phospholipase C. Biochemical data suggest that p47gag-crk activates one or several endogenous tyrosine kinases.
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