The Evidence for G-Protein-Coupled Receptors and Heterotrimeric G Proteins in Protozoa and Ancestral Metazoa

Neurosignals ◽  
1998 ◽  
Vol 7 (2) ◽  
pp. 98-108 ◽  
Author(s):  
David C. New ◽  
Joseph T.Y. Wong
Keyword(s):  
G Protein ◽  
G Proteins ◽  
G Protein Coupled Receptors ◽  
Heterotrimeric G Proteins ◽  
G Protein Coupled

scholarly journals Signaling from G Protein-coupled Receptors to ERK5/Big MAPK 1 Involves Gαqand Gα12/13Families of Heterotrimeric G Proteins

2000 ◽  
Vol 275 (28) ◽  
pp. 21730-21736 ◽  
Author(s):  
Shigetomo Fukuhara ◽  
Maria Julia Marinissen ◽  
Mario Chiariello ◽  
J. Silvio Gutkind
Keyword(s):  
G Protein ◽  
G Proteins ◽  
G Protein Coupled Receptors ◽  
Heterotrimeric G Proteins ◽  
G Protein Coupled

scholarly journals When Heterotrimeric G Proteins Are Not Activated by G Protein-Coupled Receptors: Structural Insights and Evolutionary Conservation

Biochemistry ◽  
2017 ◽  
Vol 57 (3) ◽  
pp. 255-257 ◽  
Author(s):  
Vincent DiGiacomo ◽  
Arthur Marivin ◽  
Mikel Garcia-Marcos
Keyword(s):  
G Protein ◽  
G Proteins ◽  
Evolutionary Conservation ◽  
G Protein Coupled Receptors ◽  
Heterotrimeric G Proteins ◽  
G Protein Coupled ◽  
Structural Insights

scholarly journals G Protein‐Coupled receptors and heterotrimeric G proteins as cancer drivers

FEBS Letters ◽  
2020 ◽  
Vol 594 (24) ◽  
pp. 4201-4232
Author(s):  
Nadia Arang ◽  
J. Silvio Gutkind
Keyword(s):  
G Protein ◽  
G Proteins ◽  
G Protein Coupled Receptors ◽  
Heterotrimeric G Proteins ◽  
Cancer Drivers ◽  
G Protein Coupled

scholarly journals II. Regulation of neuropeptide receptors in enteric neurons

1998 ◽  
Vol 274 (5) ◽  
pp. G792-G796
Author(s):  
Karen McConalogue ◽  
Nigel W. Bunnett
Keyword(s):  
G Protein ◽  
G Proteins ◽  
Target Cell ◽  
Biological Effects ◽  
G Protein Coupled Receptors ◽  
Enteric Neurons ◽  
Heterotrimeric G Proteins ◽  
High Affinity ◽  
Neuropeptide Receptors ◽  
G Protein Coupled

Neuropeptides exert their diverse biological effects by interacting with G protein-coupled receptors (GPCRs). In this review we address the question, What regulates the ability of a target cell, in particular a neuron, to respond to a neuropeptide? Available evidence from studies of many GPCRs in reconstituted systems and transfected cell lines indicates that much of this regulation occurs at the level of the receptor and serves to alter the capacity of the receptor to bind ligands with high affinity and to couple to heterotrimeric G proteins. Although some of the knowledge gained from these studies is applicable to the regulation of neuropeptide receptors on neurons, at present there are far more questions than answers.

scholarly journals Heterotrimeric G proteins precouple with G protein-coupled receptors in living cells

2005 ◽  
Vol 102 (51) ◽  
pp. 18706-18711 ◽  
Author(s):  
M. Nobles ◽  
A. Benians ◽  
A. Tinker
Keyword(s):  
G Protein ◽  
G Proteins ◽  
Living Cells ◽  
G Protein Coupled Receptors ◽  
Heterotrimeric G Proteins ◽  
G Protein Coupled

scholarly journals PRECOG: PREdicting COupling probabilities of G-protein coupled receptors

2019 ◽  
Vol 47 (W1) ◽  
pp. W395-W401 ◽  
Author(s):  
Gurdeep Singh ◽  
Asuka Inoue ◽  
J Silvio Gutkind ◽  
Robert B Russell ◽  
Francesco Raimondi
Keyword(s):  
G Protein ◽  
G Proteins ◽  
Protein Sequence ◽  
Web Server ◽  
Structural Features ◽  
G Protein Coupled Receptors ◽  
Heterotrimeric G Proteins ◽  
Eukaryotic Organism ◽  
Extracellular Stimuli ◽  
G Protein Coupled

Abstract G-protein coupled receptors (GPCRs) control multiple physiological states by transducing a multitude of extracellular stimuli into the cell via coupling to intra-cellular heterotrimeric G-proteins. Deciphering which G-proteins couple to each of the hundreds of GPCRs present in a typical eukaryotic organism is therefore critical to understand signalling. Here, we present PRECOG (precog.russelllab.org): a web-server for predicting GPCR coupling, which allows users to: (i) predict coupling probabilities for GPCRs to individual G-proteins instead of subfamilies; (ii) visually inspect the protein sequence and structural features that are responsible for a particular coupling; (iii) suggest mutations to rationally design artificial GPCRs with new coupling properties based on predetermined coupling features.

scholarly journals Signaling from G Protein-coupled Receptors to c-Jun Kinase Involves Subunits of Heterotrimeric G Proteins Acting on a Ras and Rac1-dependent Pathway

1996 ◽  
Vol 271 (8) ◽  
pp. 3963-3966 ◽  
Author(s):  
Omar A. Coso ◽  
Hidemi Teramoto ◽  
William F. Simonds ◽  
J. Silvio Gutkind
Keyword(s):  
G Protein ◽  
G Proteins ◽  
G Protein Coupled Receptors ◽  
Heterotrimeric G Proteins ◽  
Jun Kinase ◽  
G Protein Coupled ◽  
Dependent Pathway

scholarly journals DAPLE protein inhibits nucleotide exchange on Gαs and Gαq via the same motif that activates Gαi

2020 ◽  
Vol 295 (8) ◽  
pp. 2270-2284 ◽  
Author(s):  
Arthur Marivin ◽  
Marcin Maziarz ◽  
Jingyi Zhao ◽  
Vincent DiGiacomo ◽  
Isabel Olmos Calvo ◽  
...  
Keyword(s):  
G Protein ◽  
G Proteins ◽  
Birth Defects ◽  
High Frequency ◽  
G Protein Coupled Receptors ◽  
Heterotrimeric G Proteins ◽  
Nucleotide Exchange ◽  
Cytoplasmic Proteins ◽  
G Protein Coupled

Besides being regulated by G-protein–coupled receptors, the activity of heterotrimeric G proteins is modulated by many cytoplasmic proteins. GIV/Girdin and DAPLE (Dvl-associating protein with a high frequency of leucine) are the best-characterized members of a group of cytoplasmic regulators that contain a Gα-binding and -activating (GBA) motif and whose dysregulation underlies human diseases, including cancer and birth defects. GBA motif–containing proteins were originally reported to modulate G proteins by binding Gα subunits of the Gi/o family (Gαi) over other families (such as Gs, Gq/11, or G12/13), and promoting nucleotide exchange in vitro. However, some evidence suggests that this is not always the case, as phosphorylation of the GBA motif of GIV promotes its binding to Gαs and inhibits nucleotide exchange. The G-protein specificity of DAPLE and how it might affect nucleotide exchange on G proteins besides Gαi remain to be investigated. Here, we show that DAPLE's GBA motif, in addition to Gαi, binds efficiently to members of the Gs and Gq/11 families (Gαs and Gαq, respectively), but not of the G12/13 family (Gα12) in the absence of post-translational phosphorylation. We pinpointed Met-1669 as the residue in the GBA motif of DAPLE that diverges from that in GIV and enables better binding to Gαs and Gαq. Unlike the nucleotide-exchange acceleration observed for Gαi, DAPLE inhibited nucleotide exchange on Gαs and Gαq. These findings indicate that GBA motifs have versatility in their G-protein–modulating effect, i.e. they can bind to Gα subunits of different classes and either stimulate or inhibit nucleotide exchange depending on the G-protein subtype.

scholarly journals Conformational Transitions and the Activation of Heterotrimeric G Proteins by G Protein-Coupled Receptors

2019 ◽  
Vol 2 (4) ◽  
pp. 285-290 ◽  
Author(s):  
Christopher Draper-Joyce ◽  
Sebastian George Barton Furness
Keyword(s):  
G Protein ◽  
G Proteins ◽  
Conformational Transitions ◽  
G Protein Coupled Receptors ◽  
Heterotrimeric G Proteins ◽  
G Protein Coupled

scholarly journals Every Detail Matters. That Is, How the Interaction between Gα Proteins and Membrane Affects Their Function

Membranes ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 222
Author(s):  
Agnieszka Polit ◽  
Paweł Mystek ◽  
Ewa Błasiak
Keyword(s):  
Signal Transduction ◽  
G Protein ◽  
G Proteins ◽  
Lipid Membranes ◽  
Signaling Proteins ◽  
Heterotrimeric G Proteins ◽  
Membrane Attachment ◽  
The Individual ◽  
Multicellular Organisms ◽  
G Protein Coupled

In highly organized multicellular organisms such as humans, the functions of an individual cell are dependent on signal transduction through G protein-coupled receptors (GPCRs) and subsequently heterotrimeric G proteins. As most of the elements belonging to the signal transduction system are bound to lipid membranes, researchers are showing increasing interest in studying the accompanying protein–lipid interactions, which have been demonstrated to not only provide the environment but also regulate proper and efficient signal transduction. The mode of interaction between the cell membrane and G proteins is well known. Despite this, the recognition mechanisms at the molecular level and how the individual G protein-membrane attachment signals are interrelated in the process of the complex control of membrane targeting of G proteins remain unelucidated. This review focuses on the mechanisms by which mammalian Gα subunits of G proteins interact with lipids and the factors responsible for the specificity of membrane association. We summarize recent data on how these signaling proteins are precisely targeted to a specific site in the membrane region by introducing well-defined modifications as well as through the presence of polybasic regions within these proteins and interactions with other components of the heterocomplex.

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