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Please use this identifier to cite or link to this item: http://hdl.handle.net/1807/9443

Title: Binding of SH2 Domains of Phospholipase Cγ1, GAP, and Src to Activated Growth Factor Receptors
Authors: Anderson, Deborah
Koch, C. Anne
Grey, Laura
Ellis, Christine
Moran, Michael
Pawson, Tony
Keywords: Phospholipase C
GTPase-Activating Proteins
Receptor, Epidermal Growth Factor
Receptors, Platelet-Derived Growth Factor
Sequence Homology, Nucleic Acid
Genes, src
Issue Date: 16-Nov-1990
Publisher: American Association for the Advancement of Science
Citation: Science. 1990 Nov 16;250(4983):979-82.
Abstract: Phospholipase Cγ1 (PLCγl) and p21ras guanosine triphosphatase (GTPase) activating protein (GAP) bind to and are phosphorylated by activated growth factor receptors. Both PLCγl and GAP contain two adjacent copies of the noncatalytic Src homology 2 (SH2) domain. The SH2 domains of PLCγl synthesized individually in bacteria formed high affinity complexes with the epidermal growth factor (EGF)- or platelet derived growth factor (PDGF)-receptors in cell lysates, and bound synergistically to activated receptors when expressed together as one bacterial protein. In vitro complex formation was dependent on prior growth factor stimulation and was competed by intracellular PLCγl. Similar results were obtained for binding of GAP SH2 domains to the PDGF-receptor. The isolated SH2 domains of other signaling proteins, such as p60src and Crk, also bound activated PDGF-receptors in vitro. SH2 domains, therefore, provide a common mechanism by which enzymatically diverse regulatory proteins can physically associate with the same activated receptors and thereby couple growth factor stimulation to intracellular signal transduction pathways.
URI: http://www.sciencemag.org/
http://hdl.handle.net/1807/9443
Appears in Collections:Pawson, Tony
Pawson, Tony

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