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Biochim Biophys Acta

Title:		Signal transduction in the vomeronasal organ of garter snakes: ligand-receptor binding-mediated protein phosphorylation
Author(s):		Liu J; Chen P; Wang D; Halpern M;
Address:		"Department of Biochemistry, SUNY Health Science Center at Brooklyn, 450 Clarkson Avenue, Brooklyn, NY 11203, USA"
Journal Title:		Biochim Biophys Acta
Year:		1999
Volume:		1450
Issue:		3
Page Number:		320 - 330
DOI:		10.1016/s0167-4889(99)00061-0
ISSN/ISBN:		0006-3002 (Print) 0006-3002 (Linking)
Abstract:		"The vomeronasal (VN) system of garter snakes plays an important role in several species-typical behaviors, such as prey recognition and responding to courtship pheromones. We (X.C. Jiang et al., J. Biol. Chem. 265 (1990) 8736-8744 and Y. Luo et al., J. Biol. Chem. 269 (1994) 16867-16877) have demonstrated previously that in the snake VN sensory epithelium, the chemoattractant ES20, a 20-kDa glycoprotein derived from electric shock-induced earthworm secretion, binds to its receptor which is coupled to PTX-sensitive G-proteins. Such binding results in elevated levels of IP3. We now report that ES20-receptor binding regulates the phosphorylation of two membrane-bound proteins with molecular masses of 42- and 44-kDa (p42/44) in both intact and cell-free preparations of the VN sensory epithelium. ES20 and DAG regulate the phosphorylation of p42/44 in a similar manner. ES20-receptor binding-mediated phosphorylation of p42/44 is rapid and transient, reaching a peak value within 40 seconds and decaying thereafter. Phosphorylation of p42/44 appears to be regulated by the countervailing actions of a specific membrane-bound protein kinase and a protein phosphatase. The phosphorylation of these membrane-bound proteins significantly reduces the activity of G-proteins as evidenced by a decrease in GTPase activity, but has little effect on ligand-receptor binding. These findings suggest that p42/44 play a role in modulating the signal transduction induced by ES20 in the vomeronasal system"
Keywords:		"Animals Calcium/pharmacology Colubridae/*physiology Diglycerides/pharmacology Epithelium/metabolism GTP-Binding Protein alpha Subunits, Gi-Go GTP-Binding Proteins/antagonists & inhibitors/metabolism Glycoproteins/pharmacology Intercellular Signaling Pepti;"
Notes:		"MedlineLiu, J Chen, P Wang, D Halpern, M eng DC 00104/DC/NIDCD NIH HHS/ Research Support, U.S. Gov't, P.H.S. Netherlands 1999/07/09 Biochim Biophys Acta. 1999 Jul 8; 1450(3):320-30. doi: 10.1016/s0167-4889(99)00061-0"