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Science 26 February 1999:
Vol. 283. no. 5406, pp. 1332 - 1335
DOI: 10.1126/science.283.5406.1332
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Reports

Resolution of a Signal Transfer Region from a General Binding Domain in Gbeta for Stimulation of Phospholipase C-beta 2

Elizabeth Buck, 1 Jinrong Li, 1 Yibang Chen, 1 Gezhi Weng, 1 Suzanne Scarlata, 2 Ravi Iyengar 1*

Signaling by guanine nucleotide-binding proteins (G proteins) involves sequential protein-protein interactions. G protein-beta gamma subunit (Gbeta gamma ) interactions with phospholipase C-beta 2 (PLC-beta 2) were studied to determine if all Gbeta contacts are required for signaling. A peptide encoding Gbeta amino acid residues 86 to 105 stimulated PLC-beta 2. Six residues (96 to 101) within this sequence could transfer signals and thus constitute a core signal transfer region. Another peptide, encoding Gbeta amino acid residues 115 to 135, did not substantially stimulate PLC-beta 2 by itself but inhibited Gbeta gamma stimulation, indicating that residues 115 to 135 constitute a general binding domain. Resolution of signal transfer regions from general binding domains indicates that all protein-protein contacts are not required for signal transfer and that it may be feasible to synthesize agonists and antagonists that regulate intracellular signal flow.

1  Department of Pharmacology, Mount Sinai School of Medicine, New York, NY 10029, USA.
2 Department of Physiology and Biophysics, State University of New York at Stonybrook, Stonybrook, NY 11729, USA.
*   To whom correspondence should be addressed. E-mail: iyengar{at}msvax.mssm.edu

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