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Science 3 May 1991: Vol. 252. no. 5006, pp. 668 - 674 DOI: 10.1126/science.1708916
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Articles
Science, Vol 252, Issue 5006, 668-674
Copyright © 1991 by American Association for the Advancement of Science
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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- Guanosine Triphosphatase-Activating Protein-Associated Protein, But Not src-Associated Protein p68 in Mitosis, Is a Part of Insulin Signaling Complexes.
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Endocrinology
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- Molecular Cloning of a T Cell-specific Adapter Protein (TSAd) Containing an Src Homology (SH) 2 Domain and Putative SH3 and Phosphotyrosine Binding Sites.
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PNAS
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- Screening Assay for the Detection of the Protein-Protein Interaction Between HIV-1 Nef Protein and the SH3 Domain of Hck.
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- small wing encodes a phospholipase C-(gamma) that acts as a negative regulator of R7 development in Drosophila.
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Development
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- An Essential Function of a Phosphoinositide-Specific Phospholipase C Is Relieved by Inhibition of a Cyclin-Dependent Protein Kinase in the Yeast Saccharomyces cerevisiae.
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- Molecular Cloning and Functional Expression of a cDNA Encoding a New Member of Mixed Lineage Protein Kinase from Human Brain.
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- Activated Phosphatidylinositol 3-Kinase and Akt Kinase Promote Survival of Superior Cervical Neurons.
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- Calcium Release at Fertilization in Starfish Eggs Is Mediated by Phospholipase C{gamma}.
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- FAP52, a Novel, SH3 Domain-containing Focal Adhesion Protein.
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