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Science 7 August 1992:
Vol. 257. no. 5071, pp. 803 - 806
DOI: 10.1126/science.1379745

Articles

Science, Vol 257, Issue 5071, 803-806
Copyright © 1992 by American Association for the Advancement of Science


articles

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, and D Baltimore

Rockefeller University, New York, NY 10021.

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.


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C M Horvath, Z Wen, and J E Darnell (1995)
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A Novel Ligand for SH3 Domains.
M. M. Chou and H. Hanafusa (1995)
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J. Biol. Chem. 270, 5680-5685
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AFAP-120.
D. C. Flynn, T. C. Koay, C. G. Humphries, and A. C. Guappone (1995)
J. Biol. Chem. 270, 3894-3899
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Crk Interacts with Tyrosine-phosphorylated p116 upon T Cell Activation.
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Characterization of an Autoinhibitory Domain in Human Mitogen-activated Protein Kinase-activated Protein Kinase 2.
Y.-L. Zu, Y. Ai, and C.-K. Huang (1995)
J. Biol. Chem. 270, 202-206
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SH3 Domains Specifically Regulate Kinase Activity of Expressed Src Family Proteins.
C. S. Abrams and W. Zhao (1995)
J. Biol. Chem. 270, 333-339
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S Feng, J. Chen, H Yu, J. Simon, and S. Schreiber (1994)
Science 266, 1241-1247
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Cloning of a Grb2 isoform with apoptotic properties.
I Fath, F Schweighoffer, I Rey, M. Multon, J Boiziau, M Duchesne, and B Tocque (1994)
Science 264, 971-974
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Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites..
R Ren, Z S Ye, and D Baltimore (1994)
Genes & Dev. 8, 783-795
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Activation of phosphatidylinositol-3' kinase by Src-family kinase SH3 binding to the p85 subunit.
C. Pleiman, W. Hertz, and J. Cambier (1994)
Science 263, 1609-1612
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The Molecular Basis of Leukemia.
M. J. Cline (1994)
N. Engl. J. Med. 330, 328-336
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B. Skalhegg, K Tasken, V Hansson, H. Huitfeldt, T Jahnsen, and T Lea (1994)
Science 263, 84-87
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Aspects of growth factor signal transduction in the cell cytoplasm.
B. Panaretto (1994)
J. Cell Sci. 107, 747-752
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Closing in on SH2 specificity.
R. Birge and H Hanafusa (1993)
Science 262, 1522-1524
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Interaction of Shc with the zeta chain of the T cell receptor upon T cell activation.
K. Ravichandran, K. Lee, Z Songyang, L. Cantley, P Burn, and S. Burakoff (1993)
Science 262, 902-905
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Binding of the Ras activator son of sevenless to insulin receptor substrate-1 signaling complexes.
K Baltensperger, L. Kozma, A. Cherniack, J. Klarlund, A Chawla, U Banerjee, and M. Czech (1993)
Science 260, 1950-1952
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The function of GRB2 in linking the insulin receptor to Ras signaling pathways.
E. Skolnik, A Batzer, N Li, C. Lee, E Lowenstein, M Mohammadi, B Margolis, and J Schlessinger (1993)
Science 260, 1953-1955
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Human Sos1: a guanine nucleotide exchange factor for Ras that binds to GRB2.
P Chardin, J. Camonis, N. Gale, L van Aelst, J Schlessinger, M. Wigler, and D Bar-Sagi (1993)
Science 260, 1338-1343
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Identification of a ten-amino acid proline-rich SH3 binding site.
R Ren, B. Mayer, P Cicchetti, and D Baltimore (1993)
Science 259, 1157-1161
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Identification of the SH3 domain of GAP as an essential sequence for Ras-GAP-mediated signaling.
M Duchesne, F Schweighoffer, F Parker, F Clerc, Y Frobert, M. Thang, and B Tocque (1993)
Science 259, 525-528
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Binding of the alpha-fodrin SH3 domain to the leading lamellae of locomoting chicken fibroblasts.
J Merilainen, R Palovuori, R Sormunen, V. Wasenius, and V. Lehto (1993)
J. Cell Sci. 105, 647-654
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Solution structure of the SH3 domain of Src and identification of its ligand-binding site.
H Yu, M. Rosen, T. Shin, C Seidel-Dugan, J. Brugge, and S. Schreiber (1992)
Science 258, 1665-1668
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Cytoskeleton--plasma membrane interactions.
E. Luna and A. Hitt (1992)
Science 258, 955-964
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A Nuclear SH3 Domain-binding Protein That Colocalizes with mRNA Splicing Factors and Intermediate Filament-containing Perinuclear Networks.
G. Craggs, P. M. Finan, D. Lawson, J. Wingfield, T. Perera, S. Gadher, N. F. Totty, and S. Kellie (2001)
J. Biol. Chem. 276, 30552-30560
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RICH, a Rho GTPase-activating Protein Domain-containing Protein Involved in Signaling by Cdc42 and Rac1.
N. Richnau and P. Aspenstrom (2001)
J. Biol. Chem. 276, 35060-35070
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