Adhesion G protein-coupled receptors in nervous system development and disease

2016 ◽  
Vol 17 (9) ◽  
pp. 550-561 ◽  
Author(s):  
Tobias Langenhan ◽  
Xianhua Piao ◽  
Kelly R. Monk
2009 ◽  
Vol 20 (17) ◽  
pp. 3865-3877 ◽  
Author(s):  
Damir Kopein ◽  
Vladimir L. Katanaev

G protein–coupled receptors (GPCRs) transduce their signals through trimeric G proteins, inducing guanine nucleotide exchange on their Gα-subunits; the resulting Gα-GTP transmits the signal further inside the cell. GoLoco domains present in many proteins play important roles in multiple trimeric G protein–dependent activities, physically binding Gα-subunits of the Gαi/o class. In most cases GoLoco binds exclusively to the GDP-loaded form of the Gα-subunits. Here we demonstrate that the poly-GoLoco–containing protein Pins of Drosophila can bind to both GDP- and GTP-forms of Drosophila Gαo. We identify Pins GoLoco domain 1 as necessary and sufficient for this unusual interaction with Gαo-GTP. We further pinpoint a lysine residue located centrally in this domain as necessary for the interaction. Our studies thus identify Drosophila Pins as a target of Gαo-mediated GPCR receptor signaling, e.g., in the context of the nervous system development, where Gαo acts downstream from Frizzled and redundantly with Gαi to control the asymmetry of cell divisions.


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