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Data, including data from studies using transgenic/knockout mice, suggest that Ppp1ca (show PPP1CA Proteins) and Gnb1 interact in quiescent platelets; then, Ppp1ca (show PPP1CA Proteins) and Plcb3 (show PLCB3 Proteins) interact during platelet aggregation; thus, Gnb1 enlists Ppp1ca (show PPP1CA Proteins) to modulate G protein-coupled receptor (show GPR34 Proteins) signaling. (Ppp1ca (show PPP1CA Proteins) = protein phosphatase 1 (show PPP1CB Proteins), catalytic subunit alpha; Gnb1 = guanine nucleotide-binding protein (show TRIM23 Proteins), subunit beta-1; Plcb3 (show PLCB3 Proteins) = phospholipase C (show PLC Proteins), subunit beta-3)
It was concluded that GIRK2 (show KCNJ6 Proteins), through its dual responsiveness to G protein beta (show GNB3 Proteins)-gamma and Na+, mediates a form of neuronal inhibition that is amplifiable in the setting of excess electrical activity.
During corticogenesis, a cilium-transduced, noncanonical IGF-1R (show IGF1R Proteins)-Gbetagamma-phospho(T94)Tctex-1 (show DYNLT1 Proteins) signaling pathway promotes the proliferation of neural progenitors through modulation of ciliary resorption and G1 length.
ectopically expressed cTalpha 1) forms a heterotrimeric complex with rod Gbeta(1)gamma(1), and substitutes equally for rTalpha in generating photoresponses initiated by either rhodopsin or S-cone opsin
Results suggest a model in which the Gbetagamma dimer that is released as a result of the dissociation from Galpha(o (show GNAO1 Proteins)) upon activation of mGluR6 (show GRM6 Proteins) closes the TRPM1 (show TRPM1 Proteins) channel, perhaps via a direct interaction.
WDR26 (show WDR26 Proteins) is a novel Gbetagamma-binding protein that is required for the efficacy of Gbetagamma signaling and leukocyte migration
Our data suggest that the G-protein beta(1)gamma(2) dimer may play an important regulatory role in skeletal muscle excitation-contraction coupling.
G protein subunits beta1 and beta2 have different roles in neutrophil function, as revealed by gene expression silencing in primary mouse neutrophils
G betagamma binds HDAC5 (show HDAC5 Proteins) and inhibits its transcriptional co-repression activity
G protein betagamma subunits stimulate type V and VI adenylyl cyclases
Through analysis of the genomic and proteomic profiles of resistant cells, we identified an acquired mutation in the GNB1 gene, K89M, as the most likely cause of the resistance
Germline De Novo Mutations in GNB1 Cause Severe Neurodevelopmental Disability, Hypotonia, and Seizures.
we demonstrate a pathogenic role of de novo and autosomal dominant mutations in GNB1 as a cause of Global developmental delay and provide insights how perturbation in heterotrimeric G protein function contributes to the disease
PhLP1 binding stabilizes the Gbeta (show SUCLG2 Proteins) fold, disrupting interactions with CCT (show FLVCR2 Proteins) and releasing a PhLP1-Gbeta (show SUCLG2 Proteins) dimer for assembly with Ggamma.
GNB1 and GNB2 alterations confer transformed and resistance phenotypes across a range of human tumors and may be targetable with inhibitors of G protein signaling.
Data indicate that endogenous mTOR (show FRAP1 Proteins) interacts with Gbetagamma.
GNB1 plays an important role in the mTOR (show FRAP1 Proteins)-related anti-apoptosis pathway and can potentially be targeted in the treatment of human breast cancer.
Findings suggest a wide-ranging mechanism by which direct interaction of Gbetagamma with specific chromatin bound transcription factors regulates functional gene networks in response to GPCR (show NMUR1 Proteins) activation in cells including the angiotensin II type 1 receptor (show AGTR1 Proteins).
This study provided evidence that GNB1 gene polymorphisms are related to rapid virological response in HCV-1 and HCV-2 (show BMPER Proteins) infected patients. GNB1 may play an important role in activating the antiviral response prior to treatment.
Gbeta1gamma2-mediated epithelial sodium channel (ENaC) inhibition involves activation of phospholipase C-beta and its enzymatic products that induce protein kinase C and ERK1/2 signaling pathways.
Data suggest that a hetero-multimer complex forms between light-activated rhodopsin and light-activated heterotrimeric transducin (show GNAT1 Proteins) (T-alpha-1, Gnb1, Gngt1 (show GNGT1 Proteins)); the stoichiometry is 1:1 rhodopsin:transducin. The complex appears to form on native rod outer segment membranes upon light activation.
The PIP2-induced orientation of the GRK2 (show ADRBK1 Proteins)-Gbeta1gamma2 complex is therefore most likely caused by specific interactions between PIP2 and the GRK2 (show ADRBK1 Proteins) PH domain.
determined the crystallographic structure of GRK2 in complex with G protein beta1gamma2 subunits
conclude that GNB1 constitutes over 99% of the GNbeta expressed in bovine rod outer segments and displays structural heterogeneity that is due to post-translational modification, some of which is due to phosphorylation of GNB1.
Heterotrimeric guanine nucleotide-binding proteins (G proteins), which integrate signals between receptors and effector proteins, are composed of an alpha, a beta, and a gamma subunit. These subunits are encoded by families of related genes. This gene encodes a beta subunit. Beta subunits are important regulators of alpha subunits, as well as of certain signal transduction receptors and effectors. This gene uses alternative polyadenylation signals.
guanine nucleotide binding protein, beta 1
, guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
, transducin beta chain 1
, G protein, beta-1 subunit
, beta subunit, signal-transducing proteins GS/GI
, guanine nucleotide-binding protein G(I)/G(S)/G(T) beta subunit 1
, Guanine nucleotide-binding protein beta 1
, guanine nucleotide binding protein (G protein), beta 1
, guanine nucleotide-binding protein, beta-1 subunit
, rod transducin
, beta 1 subunit of heterotrimeric GTP-binding protein