scholarly journals Oriented Cell Division in the C. elegans Embryo Is Coordinated by G-Protein Signaling Dependent on the Adhesion GPCR LAT-1

PLoS Genetics ◽  
2015 ◽  
Vol 11 (10) ◽  
pp. e1005624 ◽  
Author(s):  
Antje Müller ◽  
Jana Winkler ◽  
Franziska Fiedler ◽  
Tania Sastradihardja ◽  
Claudia Binder ◽  
...  
Keyword(s):  
Cell Division ◽  
G Protein ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
C Elegans ◽  
Oriented Cell Division ◽  
Adhesion Gpcr

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 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 Dauer pheromone and G-protein signaling modulate the coordination of intraflagellar transport kinesin motor proteins in C. elegans

2010 ◽  
Vol 123 (12) ◽  
pp. 2077-2084 ◽  
Author(s):  
J. Burghoorn ◽  
M. P. J. Dekkers ◽  
S. Rademakers ◽  
T. de Jong ◽  
R. Willemsen ◽  
...  
Keyword(s):  
G Protein ◽  
Motor Proteins ◽  
Intraflagellar Transport ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Kinesin Motor ◽  
C Elegans ◽  
Kinesin Motor Proteins

scholarly journals Localization of Giα proteins in the centrosomes and at the midbody: implication for their role in cell division

2007 ◽  
Vol 178 (2) ◽  
pp. 245-255 ◽  
Author(s):  
Hyeseon Cho ◽  
John H. Kehrl
Keyword(s):  
Cell Division ◽  
G Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Direct Interaction ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Heterotrimeric G Proteins ◽  
Independent Functions ◽  
G Protein Coupled

At the plasma membrane, heterotrimeric G proteins act as molecular switches to relay signals from G protein–coupled receptors; however, Gα subunits also have receptor-independent functions at intracellular sites. Regulator of G protein signaling (RGS) 14, which enhances the intrinsic GTPase activity of Giα proteins, localizes in centrosomes, which suggests the coexpression of Giα. We show expression of Giα1, Giα2, and Giα3 in the centrosomes and at the midbody. Fluorescence resonance energy transfer analysis confirms a direct interaction between RGS14 and Giα1 in centrosomes. Expression of GTPase-deficient Giα1 results in defective cytokinesis, whereas that of wild-type or GTPase-deficient Giα3 causes prolonged mitosis. Cells treated with pertussis toxin, with reduced expression of Giα1, Giα2, and Giα3 or with decreased expression of RGS14 also exhibit cytokinesis defects. These results suggest that Giα proteins and their regulators at these sites may play essential roles during mammalian cell division.

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