Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho
P Cicchetti, BJ Mayer, G Thiel, D Baltimore - Science, 1992 - science.org
P Cicchetti, BJ Mayer, G Thiel, D Baltimore
Science, 1992•science.orgA Src homology 3 (SH3) region is a sequence of approximately 50 amino acids found in
many nonreceptor tyrosine kinases and other proteins. Deletion of the SH3 region from the
protein encoded by the c-abl proto-oncogene activates the protein's transforming capacity,
thereby suggesting the participation of the SH3 region in the negative regulation of
transformation. A complementary DNA was isolated that encoded a protein, 3BP-1, to which
the SH3 region of Abl bound with high specificity and to which SH3 regions from other …
many nonreceptor tyrosine kinases and other proteins. Deletion of the SH3 region from the
protein encoded by the c-abl proto-oncogene activates the protein's transforming capacity,
thereby suggesting the participation of the SH3 region in the negative regulation of
transformation. A complementary DNA was isolated that encoded a protein, 3BP-1, to which
the SH3 region of Abl bound with high specificity and to which SH3 regions from other …
A Src homology 3 (SH3) region is a sequence of approximately 50 amino acids found in many nonreceptor tyrosine kinases and other proteins. Deletion of the SH3 region from the protein encoded by the c-abl proto-oncogene activates the protein's transforming capacity, thereby suggesting the participation of the SH3 region in the negative regulation of transformation. A complementary DNA was isolated that encoded a protein, 3BP-1, to which the SH3 region of Abl bound with high specificity and to which SH3 regions from other proteins bound differentially. The sequence of the 3BP-1 protein is similar to that of a COOH-terminal segment of Bcr and to guanosine triphosphatase-activating protein (GAP)-rho, which suggests that it might have GAP activity for Ras-related proteins. The 3BP-1 protein may therefore be a mediator of SH3 function in transformation inhibition and may link tyrosine kinases to Ras-related proteins.
AAAS