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Science 3 May 1991:
Vol. 252. no. 5006, pp. 668 - 674
DOI: 10.1126/science.1708916

Articles

Science, Vol 252, Issue 5006, 668-674
Copyright © 1991 by American Association for the Advancement of Science


articles

SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins

CA Koch, D Anderson, MF Moran, C Ellis, and T Pawson

Division of Molecular and Developmental Biology, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada.

Src homology (SH) regions 2 and 3 are noncatalytic domains that are conserved among a series of cytoplasmic signaling proteins regulated by receptor protein-tyrosine kinases, including phospholipase C-gamma, Ras GTPase (guanosine triphosphatase)-activating protein, and Src-like tyrosine kinases. The SH2 domains of these signaling proteins bind tyrosine phosphorylated polypeptides, implicated in normal signaling and cellular transformation. Tyrosine phosphorylation acts as a switch to induce the binding of SH2 domains, thereby mediating the formation of heteromeric protein complexes at or near the plasma membrane. The formation of these complexes is likely to control the activation of signal transduction pathways by tyrosine kinases. The SH3 domain is a distinct motif that, together with SH2, may modulate interactions with the cytoskeleton and membrane. Some signaling and transforming proteins contain SH2 and SH3 domains unattached to any known catalytic element. These noncatalytic proteins may serve as adaptors to link tyrosine kinases to specific target proteins. These observations suggest that SH2 and SH3 domains participate in the control of intracellular responses to growth factor stimulation.


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C. K. Sung, W. S. Choi, and V. Sanchez-Margalet (1998)
Endocrinology 139, 2392-2398
   Abstract »    Full Text »    PDF »
Paxillin Phosphorylation and Association with Lck and Pyk2 in Anti-CD3- or Anti-CD45-stimulated T Cells.
H. L. Ostergaard, O. Lou, C. W. Arendt, and N. N. Berg (1998)
J. Biol. Chem. 273, 5692-5696
   Abstract »    Full Text »    PDF »
Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses.
E. Stein, A. A. Lane, D. P. Cerretti, H. O. Schoecklmann, A. D. Schroff, R. L. Van Etten, and T. O. Daniel (1998)
Genes & Dev. 12, 667-678
   Abstract »    Full Text »
Molecular Cloning of a T Cell-specific Adapter Protein (TSAd) Containing an Src Homology (SH) 2 Domain and Putative SH3 and Phosphotyrosine Binding Sites.
A. Spurkland, J. E. Brinchmann, G. Markussen, F. Pedeutour, E. Munthe, T. Lea, F. Vartdal, and H.-C. Aasheim (1998)
J. Biol. Chem. 273, 4539-4546
   Abstract »    Full Text »    PDF »
Genes in the pX region of human T cell leukemia virus I influence Vav phosphorylation in T cells.
W. Mahana, T. M. Zhao, R. Teller, M. A. Robinson, and T. J. Kindt (1998)
PNAS 95, 1782-1787
   Abstract »    Full Text »    PDF »
Screening Assay for the Detection of the Protein-Protein Interaction Between HIV-1 Nef Protein and the SH3 Domain of Hck.
A. E. Jones, K. Saksela, S. M. Game, G. O'Beirne, and N. D. Cook (1998)
J Biomol Screen 3, 37-41
   Abstract »    PDF »
small wing encodes a phospholipase C-(gamma) that acts as a negative regulator of R7 development in Drosophila.
J. Thackeray, P. Gaines, P Ebert, and J. Carlson (1998)
Development 125, 5033-5042
   Abstract »    PDF »
An Essential Function of a Phosphoinositide-Specific Phospholipase C Is Relieved by Inhibition of a Cyclin-Dependent Protein Kinase in the Yeast Saccharomyces cerevisiae.
(1998)
Genetics 148, 33-48
Overexpression of Cellular Src in Fibroblasts Enhances Endocytic Internalization of Epidermal Growth Factor Receptor.
M. F. Ware, D. A. Tice, S. J. Parsons, and D. A. Lauffenburger (1997)
J. Biol. Chem. 272, 30185-30190
   Abstract »    Full Text »    PDF »
Molecular Cloning and Functional Expression of a cDNA Encoding a New Member of Mixed Lineage Protein Kinase from Human Brain.
H. Sakuma, A. Ikeda, S. Oka, Y. Kozutsumi, J.-P. Zanetta, and T. Kawasaki (1997)
J. Biol. Chem. 272, 28622-28629
   Abstract »    Full Text »    PDF »
Activated Phosphatidylinositol 3-Kinase and Akt Kinase Promote Survival of Superior Cervical Neurons.
K. L. Philpott, M. J. McCarthy, A. Klippel, and L. L. Rubin (1997)
J. Cell Biol. 139, 809-815
   Abstract »    Full Text »    PDF »
The 66-kDa Shc Isoform Is a Negative Regulator of the Epidermal Growth Factor-stimulated Mitogen-activated Protein Kinase Pathway.
S. Okada, A. W. Kao, B. P. Ceresa, P. Blaikie, B. Margolis, and J. E. Pessin (1997)
J. Biol. Chem. 272, 28042-28049
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Characterization of Phosphotyrosine Binding Motifs in the Cytoplasmic Domain of Platelet/Endothelial Cell Adhesion Molecule-1 (PECAM-1) That Are Required for the Cellular Association and Activation of the Protein-tyrosine Phosphatase, SHP-2.
D. E. Jackson, K. R. Kupcho, and Peter. J. Newman (1997)
J. Biol. Chem. 272, 24868-24875
   Abstract »    Full Text »    PDF »
Calcium Release at Fertilization in Starfish Eggs Is Mediated by Phospholipase C{gamma}.
D. J. Carroll, C. S. Ramarao, L. M. Mehlmann, S. Roche, M. Terasaki, and L. A. Jaffe (1997)
J. Cell Biol. 138, 1303-1311
   Abstract »    Full Text »    PDF »
Insulin Receptor Substrate Proteins Create a Link between the Tyrosine Phosphorylation Cascade and the Ca2+-ATPases in Muscle and Heart.
P. Algenstaedt, D. A. Antonetti, M. B. Yaffe, and C. R. Kahn (1997)
J. Biol. Chem. 272, 23696-23702
   Abstract »    Full Text »    PDF »
FAP52, a Novel, SH3 Domain-containing Focal Adhesion Protein.
J. Merilainen, V.-P. Lehto, and V.-M. Wasenius (1997)
J. Biol. Chem. 272, 23278-23284
   Abstract »    Full Text »    PDF »
Localization and Functional Expression of Splice Variants of the P2X2 Receptor.
J. Simon, E. J. Kidd, F. M. Smith, I. P. Chessell, R. Murrell-Lagnado, P. P. A. Humphrey, and E. A. Barnard (1997)
Mol. Pharmacol. 52, 237-248
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Suppression of Tyrosine Kinase Activity Inhibits [3H]Thymidine Uptake in Cultured Human Pituitary Tumor Cells.
T. H. Jones, S. K. Justice, and A. Price (1997)
J. Clin. Endocrinol. Metab. 82, 2143-2147
   Abstract »    Full Text »    PDF »
Involvement of Phospholipase C-gamma 2 in Activation of Mitogen-Activated Protein Kinase and Phospholipase A2 by Zooxanthellatoxin-A in Rabbit Platelets.
M.-C. Rho, N. Nakahata, H. Nakamura, A. Murai, and Y. Ohizumi (1997)
J. Pharmacol. Exp. Ther. 282, 496-504
   Abstract »    Full Text »



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