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Science 26 May 1995:
Vol. 268. no. 5214, pp. 1177 - 1179
DOI: 10.1126/science.7539155

Articles

Science, Vol 268, Issue 5214, 1177-1179
Copyright © 1995 by American Association for the Advancement of Science


articles

PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine

WM Kavanaugh, CW Turck, and LT Williams

Department of Medicine, University of California, San Francisco 94143, USA.

Src homology 2 (SH2) domains mediate assembly of signaling complexes by binding specifically to tyrosine-phosphorylated proteins. A phosphotyrosine binding (PTB) domain has been identified which also binds specifically to tyrosine-phosphorylated targets, but is structurally different from SH2 domains. Expression cloning was used to identify targets of PTB domains. PTB domains bound to phosphotyrosine within a sequence motif, asparagine-X1-X2-phosphotyrosine (where X represents any amino acid), that is found in many signaling proteins and is not recognized by SH2 domains. Mutational studies indicated that high affinity binding of PTB domains may require a specific conformation of the motif.


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A. Charest, J. Wagner, S. Jacob, C. J. McGlade, and M. L. Tremblay (1996)
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Interaction between the Insulin Receptor and Its Downstream Effectors.
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J. Biol. Chem. 271, 6998-7003
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Cyclin G1 and Cyclin G2 Comprise a New Family of Cyclins with Contrasting Tissue-specific and Cell Cycle-regulated Expression.
M. C. Horne, G. L. Goolsby, K. L. Donaldson, D. Tran, M. Neubauer, and A. F. Wahl (1996)
J. Biol. Chem. 271, 6050-6061
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In Vivo Association of v-Abl with Shc Mediated by a Non-phosphotyrosine-dependent SH2 Interaction.
G. D. Raffel, K. Parmar, and N. Rosenberg (1996)
J. Biol. Chem. 271, 4640-4645
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Interaction between the Phosphotyrosine Binding Domain of Shc and the Insulin Receptor Is Required for Shc Phosphorylation by Insulin in Vivo.
S. J. Isakoff, Y.-P. Yu, Y.-C. Su, P. Blaikie, V. Yajnik, E. Rose, K. M. Weidner, M. Sachs, B. Margolis, and E. Y. Skolnik (1996)
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Identification of Residues within the SHC Phosphotyrosine Binding/Phosphotyrosine Interaction Domain Crucial for Phosphopeptide Interaction.
V. Yajnik, P. Blaikie, P. Bork, and B. Margolis (1996)
J. Biol. Chem. 271, 1813-1816
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Affinity, Specificity, and Kinetics of the Interaction of the SHC Phosphotyrosine Binding Domain with Asparagine-X-X-Phosphotyrosine Motifs of Growth Factor Receptors.
A. A. Laminet, G. Apell, L. Conroy, and W. M. Kavanaugh (1996)
J. Biol. Chem. 271, 264-269
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Src Homologous and Collagen (Shc) Protein Binds to F-actin and Translocates to the Cytoskeleton upon Nerve Growth Factor Stimulation in PC12 Cells.
D. Thomas, S. D. Patterson, and R. A. Bradshaw (1995)
J. Biol. Chem. 270, 28924-28931
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PTB Domains of IRS-1 and Shc Have Distinct but Overlapping Binding Specificities.
G. Wolf, T. Trüb, E. Ottinger, L. Groninga, A. Lynch, M. F. White, M. Miyazaki, J. Lee, and S. E. Shoelson (1995)
J. Biol. Chem. 270, 27407-27410
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Distinct Modes of Interaction of SHC and Insulin Receptor Substrate-1 with the Insulin Receptor NPEY Region via Non-SH2 Domains.
W. He, T. J. O'Neill, and T. A. Gustafson (1995)
J. Biol. Chem. 270, 23258-23262
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Binding of Shc to the NPXY Motif Is Mediated by Its N-terminal Domain.
S. A. Prigent, T. S. Pillay, K. S. Ravichandran, and W. J. Gullick (1995)
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