scholarly journals Polarity mediates asymmetric trafficking of the G  heterotrimeric G-protein subunit GPB-1 in C. elegans embryos

Development ◽  
2011 ◽  
Vol 138 (13) ◽  
pp. 2773-2782 ◽  
Author(s):  
K. Thyagarajan ◽  
K. Afshar ◽  
P. Gonczy
Keyword(s):  
G Protein ◽  
Protein Subunit ◽  
Heterotrimeric G Protein ◽  
C Elegans

scholarly journals Heterotrimeric G Protein Subunit Gαq Is a Master Switch for Gβγ-Mediated Calcium Mobilization by Gi-Coupled GPCRs

2020 ◽  
Vol 80 (6) ◽  
pp. 940-954.e6 ◽  
Author(s):  
Eva Marie Pfeil ◽  
Julian Brands ◽  
Nicole Merten ◽  
Timo Vögtle ◽  
Maddalena Vescovo ◽  
...  
Keyword(s):  
G Protein ◽  
Calcium Mobilization ◽  
Protein Subunit ◽  
Heterotrimeric G Protein

scholarly journals Illuminating the role of the Gα heterotrimeric G protein subunit, RGA1, in regulating photoprotection and photoavoidance in rice

2018 ◽  
Vol 41 (2) ◽  
pp. 451-468 ◽  
Author(s):  
Ángel Ferrero-Serrano ◽  
Zhao Su ◽  
Sarah M. Assmann
Keyword(s):  
G Protein ◽  
Protein Subunit ◽  
Heterotrimeric G Protein

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 Heterotrimeric G Protein Subunit G 13 Is Critical to Olfaction

2013 ◽  
Vol 33 (18) ◽  
pp. 7975-7984 ◽  
Author(s):  
F. Li ◽  
S. Ponissery-Saidu ◽  
K. K. Yee ◽  
H. Wang ◽  
M.-L. Chen ◽  
...  
Keyword(s):  
G Protein ◽  
Protein Subunit ◽  
Heterotrimeric G Protein ◽  
G 13

scholarly journals Dominant-negative Gα subunits are a mechanism of dysregulated heterotrimeric G protein signaling in human disease

2016 ◽  
Vol 9 (423) ◽  
pp. ra37-ra37 ◽  
Author(s):  
Arthur Marivin ◽  
Anthony Leyme ◽  
Kshitij Parag-Sharma ◽  
Vincent DiGiacomo ◽  
Anthony Y. Cheung ◽  
...  
Keyword(s):  
G Protein ◽  
Mammalian Cells ◽  
Neural Crest Cell ◽  
Craniofacial Development ◽  
Dominant Negative ◽  
Protein Subunit ◽  
Protein Activity ◽  
Guanine Nucleotide Binding Protein ◽  
Heterotrimeric G Protein

Auriculo-condylar syndrome (ACS), a rare condition that impairs craniofacial development, is caused by mutations in a G protein–coupled receptor (GPCR) signaling pathway. In mice, disruption of signaling by the endothelin type A receptor (ETAR), which is mediated by the G protein (heterotrimeric guanine nucleotide–binding protein) subunit Gαq/11 and subsequently phospholipase C (PLC), impairs neural crest cell differentiation that is required for normal craniofacial development. Some ACS patients have mutations in GNAI3, which encodes Gαi3, but it is unknown whether this G protein has a role within the ETAR pathway. We used a Xenopus model of vertebrate development, in vitro biochemistry, and biosensors of G protein activity in mammalian cells to systematically characterize the phenotype and function of all known ACS-associated Gαi3 mutants. We found that ACS-associated mutations in GNAI3 produce dominant-negative Gαi3 mutant proteins that couple to ETAR but cannot bind and hydrolyze guanosine triphosphate, resulting in the prevention of endothelin-mediated activation of Gαq/11 and PLC. Thus, ACS is caused by functionally dominant-negative mutations in a heterotrimeric G protein subunit.

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