Document Detail


AGS-3 alters Caenorhabditis elegans behavior after food deprivation via RIC-8 activation of the neural G protein G αo.
MedLine Citation:
PMID:  21832186     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Proteins containing the G protein regulator (GPR) domain bind the major neural G protein Gα(o) in vitro. However, the biological functions of GPR proteins in neurons remain undefined, and based on the in vitro activities of GPR proteins it is unclear whether these proteins activate or inhibit G protein signaling in vivo. We found that the conserved GPR domain protein AGS-3 activates Gα(o) signaling in vivo to allow Caenorhabditis elegans to alter several behaviors after food deprivation, apparently so that the animals can more effectively seek food. AGS-3 undergoes a progressive change in its biochemical fractionation upon food deprivation, suggesting that effects of food deprivation are mediated by modifying this protein. We analyzed one C. elegans food-regulated behavior in depth; AGS-3 activates Gα(o) in the ASH chemosensory neurons to allow food-deprived animals to delay response to the aversive stimulus octanol. Genetic epistasis experiments show the following: (1) AGS-3 and the guanine nucleotide exchange factor RIC-8 act in ASH in a mutually dependent fashion to activate Gα(o); (2) this activation requires interaction of the GPR domains of AGS-3 with Gα(o); and (3) Gα(o)-GTP is ultimately the signaling molecule that acts in ASH to delay octanol response. These results identify a biological role for AGS-3 in response to food deprivation and indicate the mechanism for its activation of Gα(o) signaling in vivo.
Authors:
Catherine Hofler; Michael R Koelle
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  The Journal of neuroscience : the official journal of the Society for Neuroscience     Volume:  31     ISSN:  1529-2401     ISO Abbreviation:  J. Neurosci.     Publication Date:  2011 Aug 
Date Detail:
Created Date:  2011-08-11     Completed Date:  2011-10-04     Revised Date:  2013-06-28    
Medline Journal Info:
Nlm Unique ID:  8102140     Medline TA:  J Neurosci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  11553-62     Citation Subset:  IM    
Affiliation:
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8024, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Animals, Genetically Modified
Caenorhabditis elegans
Caenorhabditis elegans Proteins / metabolism,  physiology*
Cells, Cultured
Drosophila
Food Deprivation / physiology*
GTP-Binding Protein alpha Subunits, Gi-Go / metabolism*,  physiology
Guanine Nucleotide Dissociation Inhibitors / metabolism,  physiology*
Humans
Neurons / metabolism*
Nuclear Proteins / metabolism*,  physiology
Protein Binding / genetics
Signal Transduction / genetics
Grant Support
ID/Acronym/Agency:
NS36918/NS/NINDS NIH HHS; R01 NS036918/NS/NINDS NIH HHS; R01 NS036918-14/NS/NINDS NIH HHS; R01 NS036918-15/NS/NINDS NIH HHS
Chemical
Reg. No./Substance:
0/Caenorhabditis elegans Proteins; 0/GPSM1 protein, human; 0/Guanine Nucleotide Dissociation Inhibitors; 0/Nuclear Proteins; 0/RIC-8 protein, C elegans; EC 3.6.5.1/GTP-Binding Protein alpha Subunits, Gi-Go
Comments/Corrections

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