The G-Protein βγ Complex

Gautam, N.; Downes, Gerald B.; Yan, Kang; Kisselev, Oleg G.

doi:10.1016/s0898-6568(98)00006-0

Cited by 172 publications

(170 citation statements)

References 133 publications

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“…The genome sequencing project has provided Ͼ90% of the genomic sequence, including a single G␤ sequence. Previous studies have shown that G␥s from the same species usually share certain level of homology (Gautam et al, 1998). When we used our G␥ cDNA to search the databases, we found multiple cDNA and genomic clones, all with the same sequence.…”

Section: Discussionmentioning

confidence: 99%

“…The structures and functions of heterotrimeric G-proteins are highly conserved from yeast to human, but the sequences of ␥-subunits are quite divergent among different species (Gautam et al, 1998). G␤s have seven WD repeats at their COOH-terminal that fold into ␤-propeller structures, containing the binding sites for G␣s and effectors (Ford et al, 1998;Li et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

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Gγ inDictyostelium: Its Role in Localization of Gβγ to the Membrane Is Required for Chemotaxis in Shallow Gradients

Zhang

Lan

Devreotes

2001

MBoC

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Monitoring Editor: Joan S. Brugge G-protein-mediated signal transduction pathways play an essential role in the developmental program of the simple eukaryotic organism Dictyostelium discoideum. Database searches have yielded 11 G␣-subunits, a single G␤-subunit, but no G␥-subunits. We report here the purification, cDNA isolation, and functional analysis of a G␥-subunit. Like G␤, the G␥ appears to be unique and hybridization studies show that G␥ and G␤ are expressed in parallel during development. Species-wide sequence comparisons of G␥-subunits and ␥-like domains of RGS proteins reveal short stretches of highly conserved residues as well as the common CXXL motif at the COOHterminal of G␥s that target G␤␥s to plasma membrane. Overexpression of a CSVL-deleted G␥ (G␥⌬) in wild-type cells shifts G␤␥ to the cytosol and selectively impairs certain G-proteinmediated signal transduction pathways. These cells are able to respond to increments in the stimulus, but are unable to sense chemoattractant gradients. They neither move directionally nor recruit PH-domains to their leading edge. Thus, a full complement of membrane-tethered G␤␥ is required for sensing shallow gradients, but is not essential for responses to increments in extracellular stimuli.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Gγ inDictyostelium: Its Role in Localization of Gβγ to the Membrane Is Required for Chemotaxis in Shallow Gradients

Zhang

Lan

Devreotes

2001

MBoC

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“…The central noradrenergic system, anatomically based in the locus coeruleus (LC) of brain stem, is responsible for noradrenergic neurotransmission in the brain and plays a pivotal role in cognitive processes (13). The actions of NE are mediated by the family of G protein-coupled receptors (GPCRs) known as the adrenoceptors (ARs) (14).…”

Section: Introductionmentioning

confidence: 99%

Beta Adrenoceptor Polymorphism and Clinical Response to Sertraline in Major Depressive Patients

et al. 2017

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-Purpose: The adrenoceptor family, as one of the main contributors in regulating the noradrenergic system, has been studied in involvement of depression and its treatment. A functional polymorphism of G1165C on beta adrenoceptor (βAR) enhances post receptor signalling and is assumed to be involved in pharmacotherapy of depression. The aim of the present study was to discern the influence of G1165C polymorphism in the β1AR gene on individual differences in response to sertraline. Methods: One hundred newly diagnosed patients completed 6 weeks of sertraline treatment. Response to treatment was defined as a 50% decrease in Hamilton Rating Scale for depression (HRSD). Results: The patients who carried CC genotype responded five times more to sertraline comparing with other variants (P=0.005; OR=5.7; 95%CI=1.4-23.9). Moreover, carriers of C allele responded three times more to sertraline than patients with the G allele (P=0.001; OR= 3.3; 95%CI= 1.72-6.50). Conclusion:In conclusion, our results support the hypothesis that genetic variation of β1AR might influence clinical response to sertraline.

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“…Receptor activation initiates the exchange of GDP for GTP in the G-protein a subunit followed by dissociation of the G-protein heterotrimer into a GTP-bound a subunit and a bg dimer. Both, Ga-GTP and Gbg are signaling molecules in their own right and activate a diverse array of e ector systems such as enzymes and ion channels (Birnbaumer et al, 1990;Clapham and Neer, 1997;Gautam et al, 1998;Hepler and Gilman, 1992). In recent years it has become evident that receptor/G protein systems play an important role in cell di erentiation, proliferation and even in transformation by engaging signal transduction pathways like MAPK cascades which are classically employed by growth factors such as EGF or PDGF (Dhanasekaran et al, , 1998Gutkind, 1998;van Biesen et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

The galanin receptor type 2 initiates multiple signaling pathways in small cell lung cancer cells by coupling to Gq, Gi and G12 proteins

et al. 2000

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Neuropeptides like galanin produced and released by small cell lung cancer (SCLC) cells are considered principal mitogens in these tumors. We identi®ed the galanin receptor type 2 (GALR2) as the only galanin receptor expressed in H69 and H510 cells. Photoa nity labeling of G proteins in H69 cell membranes revealed that GALR2 activates G proteins of three subfamilies: G q , G i , and G 12 . In H69 cells, galanin-induced Ca 2+ mobilization was pertussis toxin-insensitive. While phorbol ester-induced extracellular signal-regulated kinase (ERK) activation required protein kinase C (PKC) activity, preincubation of H69 cells with the PKCinhibitor GF109203X had no e ect on galanin-dependent ERK activity. A rise of the intracellular calcium concentration was necessary and su cient to mediate galanin-induced ERK activation. In support of G i coupling, stimulation of GALR2 expressed in HEK293 cells inhibited isoproterenol-induced cAMP accumulation and raised cAMP levels in COS-7 cells when coexpressed with a chimeric Ga S -Ga i protein. In H69 cells, galanin activated the monomeric GTPase RhoA and induced stress ®ber formation in Swiss 3T3 cells expressing GALR2. Thus, we provide the ®rst direct evidence that in SCLC the mitogenic neuropeptide galanin, interacting with GALR2, simultaneously activates multiple classes of G proteins and signals through the G q phospholipase C/calcium sequence and a G 12 /Rho pathway. Oncogene (2000) 19, 4199 ± 4209.

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The G-Protein βγ Complex

Cited by 172 publications

References 133 publications

Gγ inDictyostelium: Its Role in Localization of Gβγ to the Membrane Is Required for Chemotaxis in Shallow Gradients

Gγ inDictyostelium: Its Role in Localization of Gβγ to the Membrane Is Required for Chemotaxis in Shallow Gradients

Beta Adrenoceptor Polymorphism and Clinical Response to Sertraline in Major Depressive Patients

The galanin receptor type 2 initiates multiple signaling pathways in small cell lung cancer cells by coupling to Gq, Gi and G12 proteins

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