scholarly journals Multiple RGS proteins alter neural G protein signaling to allow C. elegans to rapidly change behavior when fed

2000 ◽  
Vol 14 (16) ◽  
pp. 2003-2014 ◽  
Author(s):  
Meng-Qiu Dong ◽  
Daniel Chase ◽  
Georgia A. Patikoglou ◽  
Michael R. Koelle
Keyword(s):  
G Protein ◽  
Egg Laying ◽  
G Protein Signaling ◽  
Rgs Proteins ◽  
Protein Signaling ◽  
C Elegans ◽  
Change Behavior ◽  
Rgs Protein ◽  
Heterotrimeric G Protein Signaling

Regulators of G protein signaling (RGS proteins) inhibit heterotrimeric G protein signaling by activating G protein GTPase activity. Many mammalian RGS proteins are expressed in the brain and can act in vitro on the neural G protein Go, but the biological purpose of this multiplicity of regulators is not clear. We have analyzed all 13 RGS genes in Caenorhabditis elegans and found that three of them influence the aspect of egg-laying behavior controlled by Go signaling. A previously studied RGS protein, EGL-10, affects egg laying under all conditions tested. The other two RGS proteins, RGS-1 and RGS-2, act as Go GTPase activators in vitro but, unlike EGL-10, they do not strongly affect egg laying when worms are allowed to feed constantly. However, rgs-1; rgs-2double mutants fail to rapidly induce egg-laying behavior when refed after starvation. Thus EGL-10 sets baseline levels of signaling, while RGS-1 and RGS-2 appear to redundantly alter signaling to cause appropriate behavioral responses to food.

scholarly journals Heterotrimeric G protein signaling functions with dynein to promote spindle positioning in C. elegans

2007 ◽  
Vol 179 (1) ◽  
pp. 15-22 ◽  
Author(s):  
Claudia Couwenbergs ◽  
Jean-Claude Labbé ◽  
Morgan Goulding ◽  
Thomas Marty ◽  
Bruce Bowerman ◽  
...  
Keyword(s):  
G Protein ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Dynein Light Chain ◽  
Loss Of Function ◽  
Functional Link ◽  
Heterotrimeric G Protein ◽  
Spindle Positioning ◽  
C Elegans ◽  
Heterotrimeric G Protein Signaling

Proper orientation and positioning of the mitotic spindle is essential for the correct segregation of fate determinants during asymmetric cell division. Although heterotrimeric G proteins and their regulators are essential for spindle positioning in many cell types, their mechanism of action remains unclear. In this study, we show that dyrb-1, which encodes a dynein light chain, provides a functional link between heterotrimeric G protein signaling and dynein activity during spindle positioning in Caenorhabditis elegans. Embryos depleted of dyrb-1 display phenotypes similar to a weak loss of function of dynein activity, indicating that DYRB-1 is a positive regulator of dynein. We find that the depletion of dyrb-1 enhances the spindle positioning defect of weak loss of function alleles of two regulators of G protein signaling, LIN-5 and GPR-1/2, and that DYRB-1 physically associates with these two proteins. These results indicate that dynein activity functions with regulators of G protein signaling to regulate common downstream effectors during spindle positioning in the early C. elegans embryo.

scholarly journals Gα and regulator of G-protein signaling (RGS) protein pairs maintain functional compatibility and conserved interaction interfaces throughout evolution despite frequent loss of RGS proteins in plants

2016 ◽  
Vol 216 (2) ◽  
pp. 562-575 ◽  
Author(s):  
Dieter Hackenberg ◽  
Michael R. McKain ◽  
Soon Goo Lee ◽  
Swarup Roy Choudhury ◽  
Tyler McCann ◽  
...  
Keyword(s):  
G Protein ◽  
G Protein Signaling ◽  
Rgs Proteins ◽  
Protein Signaling ◽  
Rgs Protein

scholarly journals RSBP-1 Is a Membrane-targeting Subunit Required by the Gαq-specific But Not the Gαo-specific R7 Regulator of G protein Signaling in Caenorhabditis elegans

2010 ◽  
Vol 21 (2) ◽  
pp. 232-243 ◽  
Author(s):  
Morwenna Y. Porter ◽  
Michael R. Koelle
Keyword(s):  
Plasma Membrane ◽  
Caenorhabditis Elegans ◽  
G Protein ◽  
Cultured Cells ◽  
Membrane Targeting ◽  
G Protein Signaling ◽  
Rgs Proteins ◽  
Protein Signaling ◽  
Functional Requirements ◽  
Rgs Protein

Regulator of G protein signaling (RGS) proteins inhibit G protein signaling by activating Gα GTPase activity, but the mechanisms that regulate RGS activity are not well understood. The mammalian R7 binding protein (R7BP) can interact with all members of the R7 family of RGS proteins, and palmitoylation of R7BP can target R7 RGS proteins to the plasma membrane in cultured cells. However, whether endogenous R7 RGS proteins in neurons require R7BP or membrane localization for function remains unclear. We have identified and knocked out the only apparent R7BP homolog in Caenorhabditis elegans, RSBP-1. Genetic studies show that loss of RSBP-1 phenocopies loss of the R7 RGS protein EAT-16, but does not disrupt function of the related R7 RGS protein EGL-10. Biochemical analyses find that EAT-16 coimmunoprecipitates with RSBP-1 and is predominantly plasma membrane-associated, whereas EGL-10 does not coimmunoprecipitate with RSBP-1 and is not predominantly membrane-associated. Mutating the conserved membrane-targeting sequence in RSBP-1 disrupts both the membrane association and function of EAT-16, demonstrating that membrane targeting by RSBP-1 is essential for EAT-16 activity. Our analysis of endogenous R7 RGS proteins in C. elegans neurons reveals key differences in the functional requirements for membrane targeting between members of this protein family.

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