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[PMID]:28880079
[Au] Autor:Yim YY; McDonald WH; Hyde K; Cruz-Rodríguez O; Tesmer JJG; Hamm HE
[Ad] Endereço:Department of Pharmacology, Vanderbilt University , Nashville, Tennessee 37232-6600, United States.
[Ti] Título:Quantitative Multiple-Reaction Monitoring Proteomic Analysis of Gß and Gγ Subunits in C57Bl6/J Brain Synaptosomes.
[So] Source:Biochemistry;56(40):5405-5416, 2017 Oct 10.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Gßγ dimers are one of the essential signaling units of activated G protein-coupled receptors (GPCRs). There are five Gß and 12 Gγ subunits in humans; numerous studies have demonstrated that different Gß and Gγ subunits selectively interact to form unique Gßγ dimers, which in turn may target specific receptors and effectors. Perturbation of Gßγ signaling can lead to impaired physiological responses. Moreover, previous targeted multiple-reaction monitoring (MRM) studies of Gß and Gγ subunits have shown distinct regional and subcellular localization patterns in four brain regions. Nevertheless, no studies have quantified or compared their individual protein levels. In this study, we have developed a quantitative MRM method not only to quantify but also to compare the protein abundance of neuronal Gß and Gγ subunits. In whole and fractionated crude synaptosomes, we were able to identify the most abundant neuronal Gß and Gγ subunits and their subcellular localizations. For example, Gß was mostly localized at the membrane while Gß was evenly distributed throughout synaptosomal fractions. The protein expression levels and subcellular localizations of Gß and Gγ subunits may affect the Gßγ dimerization and Gßγ-effector interactions. This study offers not only a new tool for quantifying and comparing Gß and Gγ subunits but also new insights into the in vivo distribution of Gß and Gγ subunits, and Gßγ dimer assembly in normal brain function.
[Mh] Termos MeSH primário: Encéfalo/citologia
Subunidades beta da Proteína de Ligação ao GTP/metabolismo
Subunidades gama da Proteína de Ligação ao GTP/metabolismo
Proteômica
Sinaptossomos/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Subunidades beta da Proteína de Ligação ao GTP/química
Subunidades gama da Proteína de Ligação ao GTP/química
Camundongos
Camundongos Endogâmicos C57BL
Multimerização Proteica
Estrutura Quaternária de Proteína
Transporte Proteico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GTP-Binding Protein beta Subunits); 0 (GTP-Binding Protein gamma Subunits)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170908
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00433


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[PMID]:28864771
[Au] Autor:Siripurapu P; Kankanamge D; Ratnayake K; Senarath K; Karunarathne A
[Ad] Endereço:From the Department of Chemistry and Biochemistry, University of Toledo, Toledo, Ohio 43606.
[Ti] Título:Two independent but synchronized Gßγ subunit-controlled pathways are essential for trailing-edge retraction during macrophage migration.
[So] Source:J Biol Chem;292(42):17482-17495, 2017 Oct 20.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chemokine-induced directional cell migration is a universal cellular mechanism and plays crucial roles in numerous biological processes, including embryonic development, immune system function, and tissue remodeling and regeneration. During the migration of a stationary cell, the cell polarizes, forms lamellipodia at the leading edge (LE), and triggers the concurrent retraction of the trailing edge (TE). During cell migration governed by inhibitory G protein (G )-coupled receptors (GPCRs), G protein ßγ (Gßγ) subunits control the LE signaling. Interestingly, TE retraction has been linked to the activation of the small GTPase Ras homolog family member A (RhoA) by the Gα pathway. However, it is not clear how the activation of G -coupled GPCRs at the LE orchestrates the TE retraction in RAW264.7 macrophages. Here, using an optogenetic approach involving an opsin to activate the G pathway in defined subcellular regions of RAW cells, we show that in addition to their LE activities, free Gßγ subunits also govern TE retraction by operating two independent, yet synchronized, pathways. The first pathway involves RhoA activation, which prevents dephosphorylation of the myosin light chain, allowing actomyosin contractility to proceed. The second pathway activates phospholipase Cß and induces myosin light chain phosphorylation to enhance actomyosin contractility through increasing cytosolic calcium. We further show that both of these pathways are essential, and inhibition of either one is sufficient to abolish the G -coupled GPCR-governed TE retraction and subsequent migration of RAW cells.
[Mh] Termos MeSH primário: Movimento Celular
Subunidades beta da Proteína de Ligação ao GTP/metabolismo
Subunidades gama da Proteína de Ligação ao GTP/metabolismo
Macrófagos/metabolismo
[Mh] Termos MeSH secundário: Actomiosina/genética
Actomiosina/metabolismo
Animais
Cálcio/metabolismo
Subunidades beta da Proteína de Ligação ao GTP/genética
Subunidades gama da Proteína de Ligação ao GTP/genética
Células HeLa
Seres Humanos
Camundongos
Fosfolipase C beta/genética
Fosfolipase C beta/metabolismo
Células RAW 264.7
Proteínas rho de Ligação ao GTP/genética
Proteínas rho de Ligação ao GTP/metabolismo
Proteína rhoA de Ligação ao GTP/genética
Proteína rhoA de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GTP-Binding Protein beta Subunits); 0 (GTP-Binding Protein gamma Subunits); 124671-05-2 (RHOA protein, human); 9013-26-7 (Actomyosin); EC 3.1.4.11 (Phospholipase C beta); EC 3.6.5.2 (RhoA protein, mouse); EC 3.6.5.2 (rho GTP-Binding Proteins); EC 3.6.5.2 (rhoA GTP-Binding Protein); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170903
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.787838


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[PMID]:28842475
[Au] Autor:Dessauer CW
[Ad] Endereço:From the Department of Integrative Biology and Pharmacology, McGovern Medical School, University of Texas Health Science Center, Houston, Texas 77030 carmen.w.dessauer@uth.tmc.edu.
[Ti] Título:Shining a light on GPCR complexes.
[So] Source:J Biol Chem;292(34):14290-14291, 2017 Aug 25.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The G protein-coupled receptor (GPCR) signaling pathways mediating information exchange across the cell membrane are central to a variety of biological processes and therapeutic strategies, but visualizing the molecular-level details of this exchange has been difficult for all but a few GPCR-G protein complexes. A study by Gao now reports new strategies and tools to obtain receptor complexes in a near-native state, revealing insights into the gross conformational features of rhodopsin-transducin interactions and setting the stage for future studies.
[Mh] Termos MeSH primário: Proteínas do Olho/metabolismo
Subunidades beta da Proteína de Ligação ao GTP/metabolismo
Subunidades gama da Proteína de Ligação ao GTP/metabolismo
Modelos Moleculares
Rodopsina/metabolismo
Transducina/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas do Olho/química
Subunidades beta da Proteína de Ligação ao GTP/química
Subunidades gama da Proteína de Ligação ao GTP/química
Seres Humanos
Domínios e Motivos de Interação entre Proteínas/efeitos da radiação
Multimerização Proteica/efeitos da radiação
Rodopsina/química
Segmento Externo da Célula Bastonete/enzimologia
Segmento Externo da Célula Bastonete/metabolismo
Segmento Externo da Célula Bastonete/efeitos da radiação
Transducina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Eye Proteins); 0 (GTP-Binding Protein beta Subunits); 0 (GTP-Binding Protein gamma Subunits); 9009-81-8 (Rhodopsin); EC 3.6.5.1 (Transducin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170827
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.H117.797100


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[PMID]:28801319
[Au] Autor:Gao Q; Binns DD; Kinch LN; Grishin NV; Ortiz N; Chen X; Goodman JM
[Ad] Endereço:Department of Pharmacology, University of Texas Southwestern Medical School, Dallas, TX.
[Ti] Título:Pet10p is a yeast perilipin that stabilizes lipid droplets and promotes their assembly.
[So] Source:J Cell Biol;216(10):3199-3217, 2017 Oct 02.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pet10p is a yeast lipid droplet protein of unknown function. We show that it binds specifically to and is stabilized by droplets containing triacylglycerol (TG). Droplets isolated from cells with a deletion strongly aggregate, appear fragile, and fuse in vivo when cells are cultured in oleic acid. Pet10p binds early to nascent droplets, and their rate of appearance is decreased in Moreover, Pet10p functionally interacts with the endoplasmic reticulum droplet assembly factors seipin and Fit2 to maintain proper droplet morphology. The activity of Dga1p, a diacylglycerol acyltransferase, and TG accumulation were both 30-35% lower in the absence of Pet10p. Pet10p contains a PAT domain, a defining property of perilipins, which was not previously known to exist in yeast. We propose that the core functions of Pet10p and other perilipins extend beyond protection from lipases and include the preservation of droplet integrity as well as collaboration with seipin and Fit2 in droplet assembly and maintenance.
[Mh] Termos MeSH primário: Proteínas de Transporte de Cátions/metabolismo
Subunidades gama da Proteína de Ligação ao GTP/metabolismo
Glicoproteínas/metabolismo
Gotículas Lipídicas/metabolismo
Perilipina-1/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Transporte de Cátions/genética
Subunidades gama da Proteína de Ligação ao GTP/genética
Glicoproteínas/genética
Perilipina-1/genética
Domínios Proteicos
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cation Transport Proteins); 0 (FIT2 protein, S cerevisiae); 0 (GTP-Binding Protein gamma Subunits); 0 (Glycoproteins); 0 (Perilipin-1); 0 (Saccharomyces cerevisiae Proteins); 0 (seipin protein, S cerevisiae)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171007
[Lr] Data última revisão:
171007
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170813
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201610013


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[PMID]:28655769
[Au] Autor:Gao Y; Westfield G; Erickson JW; Cerione RA; Skiniotis G; Ramachandran S
[Ad] Endereço:From the Department of Chemistry and Chemical Biology, Baker Laboratory, and.
[Ti] Título:Isolation and structure-function characterization of a signaling-active rhodopsin-G protein complex.
[So] Source:J Biol Chem;292(34):14280-14289, 2017 Aug 25.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The visual photo-transduction cascade is a prototypical G protein-coupled receptor (GPCR) signaling system, in which light-activated rhodopsin (Rho*) is the GPCR catalyzing the exchange of GDP for GTP on the heterotrimeric G protein transducin (G ). This results in the dissociation of G into its component α -GTP and ß Î³ subunit complex. Structural information for the Rho*-G complex will be essential for understanding the molecular mechanism of visual photo-transduction. Moreover, it will shed light on how GPCRs selectively couple to and activate their G protein signaling partners. Here, we report on the preparation of a stable detergent-solubilized complex between Rho* and a heterotrimer (G *) comprising a Gα /Gα chimera (α *) and ß Î³ The complex was formed on native rod outer segment membranes upon light activation, solubilized in lauryl maltose neopentyl glycol, and purified with a combination of affinity and size-exclusion chromatography. We found that the complex is fully functional and that the stoichiometry of Rho* to Gα * is 1:1. The molecular weight of the complex was calculated from small-angle X-ray scattering data and was in good agreement with a model consisting of one Rho* and one G *. The complex was visualized by negative-stain electron microscopy, which revealed an architecture similar to that of the ß -adrenergic receptor-G complex, including a flexible α * helical domain. The stability and high yield of the purified complex should allow for further efforts toward obtaining a high-resolution structure of this important signaling complex.
[Mh] Termos MeSH primário: Proteínas do Olho/metabolismo
Subunidades beta da Proteína de Ligação ao GTP/metabolismo
Subunidades gama da Proteína de Ligação ao GTP/metabolismo
Modelos Moleculares
Rodopsina/metabolismo
Transducina/metabolismo
[Mh] Termos MeSH secundário: Animais
Bovinos
Cristalografia por Raios X
Detergentes/química
Proteínas do Olho/química
Proteínas do Olho/genética
Proteínas do Olho/isolamento & purificação
Subunidades beta da Proteína de Ligação ao GTP/química
Subunidades beta da Proteína de Ligação ao GTP/isolamento & purificação
Subunidades gama da Proteína de Ligação ao GTP/química
Subunidades gama da Proteína de Ligação ao GTP/isolamento & purificação
Luz
Microscopia Eletrônica
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/isolamento & purificação
Fragmentos de Peptídeos/metabolismo
Conformação Proteica/efeitos da radiação
Multimerização Proteica/efeitos da radiação
Estabilidade Proteica/efeitos da radiação
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/isolamento & purificação
Proteínas Recombinantes de Fusão/metabolismo
Retina/enzimologia
Retina/metabolismo
Retina/efeitos da radiação
Rodopsina/química
Rodopsina/isolamento & purificação
Segmento Externo da Célula Bastonete/enzimologia
Segmento Externo da Célula Bastonete/metabolismo
Segmento Externo da Célula Bastonete/efeitos da radiação
Espalhamento a Baixo Ângulo
Solubilidade
Transducina/química
Transducina/genética
Transducina/isolamento & purificação
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Detergents); 0 (Eye Proteins); 0 (GTP-Binding Protein beta Subunits); 0 (GTP-Binding Protein gamma Subunits); 0 (Peptide Fragments); 0 (Recombinant Fusion Proteins); 9009-81-8 (Rhodopsin); EC 3.6.5.1 (Transducin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170629
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.797100


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[PMID]:28515322
[Au] Autor:Zurawski Z; Page B; Chicka MC; Brindley RL; Wells CA; Preininger AM; Hyde K; Gilbert JA; Cruz-Rodriguez O; Currie KPM; Chapman ER; Alford S; Hamm HE
[Ad] Endereço:From the Department of Pharmacology, Vanderbilt University, Nashville, Tennessee 37232-6600.
[Ti] Título:Gßγ directly modulates vesicle fusion by competing with synaptotagmin for binding to neuronal SNARE proteins embedded in membranes.
[So] Source:J Biol Chem;292(29):12165-12177, 2017 Jul 21.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:G -coupled G protein-coupled receptors can inhibit neurotransmitter release at synapses via multiple mechanisms. In addition to Gßγ-mediated modulation of voltage-gated calcium channels (VGCC), inhibition can also be mediated through the direct interaction of Gßγ subunits with the soluble -ethylmaleimide attachment protein receptor (SNARE) complex of the vesicle fusion apparatus. Binding studies with soluble SNARE complexes have shown that Gßγ binds to both ternary SNARE complexes, t-SNARE heterodimers, and monomeric SNAREs, competing with synaptotagmin 1(syt1) for binding sites on t-SNARE. However, in secretory cells, Gßγ, SNAREs, and synaptotagmin interact in the lipid environment of a vesicle at the plasma membrane. To approximate this environment, we show that fluorescently labeled Gßγ interacts specifically with lipid-embedded t-SNAREs consisting of full-length syntaxin 1 and SNAP-25B at the membrane, as measured by fluorescence polarization. Fluorescently labeled syt1 undergoes competition with Gßγ for SNARE-binding sites in lipid environments. Mutant Gßγ subunits that were previously shown to be more efficacious at inhibiting Ca -triggered exocytotic release than wild-type Gßγ were also shown to bind SNAREs at a higher affinity than wild type in a lipid environment. These mutant Gßγ subunits were unable to inhibit VGCC currents. Specific peptides corresponding to regions on Gß and Gγ shown to be important for the interaction disrupt the interaction in a concentration-dependent manner. In fusion assays using full-length t- and v-SNAREs embedded in liposomes, Gßγ inhibited Ca /synaptotagmin-dependent fusion. Together, these studies demonstrate the importance of these regions for the Gßγ-SNARE interaction and show that the target of Gßγ, downstream of VGCC, is the membrane-embedded SNARE complex.
[Mh] Termos MeSH primário: Subunidades beta da Proteína de Ligação ao GTP/metabolismo
Subunidades gama da Proteína de Ligação ao GTP/metabolismo
Bicamadas Lipídicas
Modelos Moleculares
Proteína 25 Associada a Sinaptossoma/metabolismo
Sinaptotagmina I/metabolismo
Sintaxina 1/metabolismo
[Mh] Termos MeSH secundário: Animais
Ligação Competitiva
Sinalização do Cálcio
Bovinos
Linhagem Celular
Subunidades beta da Proteína de Ligação ao GTP/química
Subunidades beta da Proteína de Ligação ao GTP/genética
Subunidades gama da Proteína de Ligação ao GTP/química
Subunidades gama da Proteína de Ligação ao GTP/genética
Seres Humanos
Lipossomos
Fusão de Membrana
Mutação
Proteínas do Tecido Nervoso/química
Proteínas do Tecido Nervoso/metabolismo
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Ratos
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Proteína 25 Associada a Sinaptossoma/química
Sinaptotagmina I/química
Sinaptotagmina I/genética
Sintaxina 1/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GTP-Binding Protein beta Subunits); 0 (GTP-Binding Protein gamma Subunits); 0 (Lipid Bilayers); 0 (Liposomes); 0 (Nerve Tissue Proteins); 0 (Peptide Fragments); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 0 (Snap25 protein, rat); 0 (Stx1a protein, rat); 0 (Synaptosomal-Associated Protein 25); 0 (Synaptotagmin I); 0 (Syntaxin 1); 0 (Syt1 protein, rat)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170519
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.773523


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[PMID]:28424266
[Au] Autor:Kishore A; Hall RA
[Ad] Endereço:From the Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia 30322.
[Ti] Título:Disease-associated extracellular loop mutations in the adhesion G protein-coupled receptor G1 (ADGRG1; GPR56) differentially regulate downstream signaling.
[So] Source:J Biol Chem;292(23):9711-9720, 2017 Jun 09.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutations to the adhesion G protein-coupled receptor ADGRG1 (G1; also known as GPR56) underlie the neurological disorder bilateral frontoparietal polymicrogyria. Disease-associated mutations in G1 studied to date are believed to induce complete loss of receptor function through disruption of either receptor trafficking or signaling activity. Given that N-terminal truncation of G1 and other adhesion G protein-coupled receptors has been shown to significantly increase the receptors' constitutive signaling, we examined two different bilateral frontoparietal polymicrogyria-inducing extracellular loop mutations (R565W and L640R) in the context of both full-length and N-terminally truncated (ΔNT) G1. Interestingly, we found that these mutations reduced surface expression of full-length G1 but not G1-ΔNT in HEK-293 cells. Moreover, the mutations ablated receptor-mediated activation of serum response factor luciferase, a classic measure of Gα -mediated signaling, but had no effect on G1-mediated signaling to nuclear factor of activated T cells (NFAT) luciferase. Given these differential signaling results, we sought to further elucidate the pathway by which G1 can activate NFAT luciferase. We found no evidence that ΔNT activation of NFAT is dependent on Gα -mediated or ß-arrestin-mediated signaling but rather involves liberation of Gßγ subunits and activation of calcium channels. These findings reveal that disease-associated mutations to the extracellular loops of G1 differentially alter receptor trafficking, depending on the presence of the N terminus, and differentially alter signaling to distinct downstream pathways.
[Mh] Termos MeSH primário: Malformações do Desenvolvimento Cortical/metabolismo
Mutação de Sentido Incorreto
Receptores Acoplados a Proteínas-G/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Linhagem Celular
Subunidades alfa G12-G13 de Proteínas de Ligação ao GTP/genética
Subunidades alfa G12-G13 de Proteínas de Ligação ao GTP/metabolismo
Subunidades beta da Proteína de Ligação ao GTP/genética
Subunidades beta da Proteína de Ligação ao GTP/metabolismo
Subunidades gama da Proteína de Ligação ao GTP/genética
Subunidades gama da Proteína de Ligação ao GTP/metabolismo
Seres Humanos
Malformações do Desenvolvimento Cortical/genética
Malformações do Desenvolvimento Cortical/patologia
Estrutura Secundária de Proteína
Transporte Proteico/genética
Receptores Acoplados a Proteínas-G/genética
beta-Arrestina 1/genética
beta-Arrestina 1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ARRB1 protein, human); 0 (GPR56 protein, human); 0 (GTP-Binding Protein beta Subunits); 0 (GTP-Binding Protein gamma Subunits); 0 (Receptors, G-Protein-Coupled); 0 (beta-Arrestin 1); EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, G12-G13)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170421
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.780551


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[PMID]:28380310
[Au] Autor:Takauji Y; Kudo I; En A; Matsuo R; Hossain MN; Nakabayashi K; Miki K; Fujii M; Ayusawa D
[Ad] Endereço:a Graduate School of Nanobioscience, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama, Kanagawa 236-0027, Japan.
[Ti] Título:GNG11 (G-protein subunit γ 11) suppresses cell growth with induction of reactive oxygen species and abnormal nuclear morphology in human SUSM-1 cells.
[So] Source:Biochem Cell Biol;95(4):517-523, 2017 Aug.
[Is] ISSN:1208-6002
[Cp] País de publicação:Canada
[La] Idioma:eng
[Ab] Resumo:Enforced expression of GNG11, G-protein subunit γ 11, induces cellular senescence in normal human diploid fibroblasts. We here examined the effect of the expression of GNG11 on the growth of immortalized human cell lines, and found that it suppressed the growth of SUSM-1 cells, but not of HeLa cells. We then compared these two cell lines to understand the molecular basis for the action of GNG11. We found that expression of GNG11 induced the generation of reactive oxygen species (ROS) and abnormal nuclear morphology in SUSM-1 cells but not in HeLa cells. Increased ROS generation by GNG11 would likely be caused by the down-regulation of the antioxidant enzymes in SUSM-1 cells. We also found that SUSM-1 cells, even under normal culture conditions, showed higher levels of ROS and higher incidence of abnormal nuclear morphology than HeLa cells, and that abnormal nuclear morphology was relevant to the increased ROS generation in SUSM-1 cells. Thus, SUSM-1 and HeLa cells showed differences in the regulation of ROS and nuclear morphology, which might account for their different responses to the expression of GNG11. Thus, SUSM-1 cells may provide a unique system to study the regulatory relationship between ROS generation, nuclear morphology, and G-protein signaling.
[Mh] Termos MeSH primário: Núcleo Celular/metabolismo
Núcleo Celular/patologia
Subunidades gama da Proteína de Ligação ao GTP/metabolismo
Espécies Reativas de Oxigênio/metabolismo
[Mh] Termos MeSH secundário: Proliferação Celular
Células Cultivadas
Células HeLa
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GTP-Binding Protein gamma Subunits); 0 (Reactive Oxygen Species)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170406
[St] Status:MEDLINE
[do] DOI:10.1139/bcb-2016-0248


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[PMID]:28363980
[Au] Autor:Van Hook MJ; Babai N; Zurawski Z; Yim YY; Hamm HE; Thoreson WB
[Ad] Endereço:Truhlsen Eye Institute, Department of Ophthalmology and Visual Sciences, University of Nebraska Medical Center, Omaha, Nebraska 68198, matt.vanhook@unmc.edu.
[Ti] Título:A Presynaptic Group III mGluR Recruits Gßγ/SNARE Interactions to Inhibit Synaptic Transmission by Cone Photoreceptors in the Vertebrate Retina.
[So] Source:J Neurosci;37(17):4618-4634, 2017 Apr 26.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:G-protein ßγ subunits (Gßγ) interact with presynaptic proteins and regulate neurotransmitter release downstream of Ca influx. To accomplish their roles in sensory signaling, photoreceptor synapses use specialized presynaptic proteins that support neurotransmission at active zone structures known as ribbons. While several G-protein coupled receptors (GPCRs) influence synaptic transmission at ribbon synapses of cones and other retinal neurons, it is unknown whether Gßγ contributes to these effects. We tested whether activation of one particular GPCR, a metabotropic glutamate receptor (mGluR), can reduce cone synaptic transmission via Gßγ in tiger salamander retinas. In recordings from horizontal cells, we found that an mGluR agonist (L-AP4) reduced cone-driven light responses and mEPSC frequency. In paired recordings of cones and horizontal cells, L-AP4 slightly reduced cone I (∼10%) and caused a larger reduction in cone-driven EPSCs (∼30%). Proximity ligation assay revealed direct interactions between SNAP-25 and Gßγ subunits in retinal synaptic layers. Pretreatment with the SNAP-25 cleaving protease BoNT/A inhibited L-AP4 effects on synaptic transmission, as did introduction of a peptide derived from the SNAP-25 C terminus. Introducing Gßγ subunits directly into cones reduced EPSC amplitude. This effect was inhibited by BoNT/A, supporting a role for Gßγ/SNAP-25 interactions. However, the mGluR-dependent reduction in I was not mimicked by Gßγ, indicating that this effect was independent of Gßγ. The finding that synaptic transmission at cone ribbon synapses is regulated by Gßγ/SNAP-25 interactions indicates that these mechanisms are shared by conventional and ribbon-type synapses. Gßγ liberated from other photoreceptor GPCRs is also likely to regulate synaptic transmission. Dynamic regulation of synaptic transmission by presynaptic G-protein coupled receptors shapes information flow through neural circuits. At the first synapse in the visual system, presynaptic metabotropic glutamate receptors (mGluRs) regulate cone photoreceptor synaptic transmission, although the mechanisms and functional impact of this are unclear. We show that mGluRs regulate light response encoding across the cone synapse, accomplished in part by triggering G-protein ßγ subunits (Gßγ) interactions with SNAP-25, a core component of the synaptic vesicle fusion machinery. In addition to revealing a role in visual processing, this provides the first demonstration that Gßγ/SNAP-25 interactions regulate synaptic function at a ribbon-type synapse, contributing to an emerging picture of the ubiquity of Gßγ/SNARE interactions in regulating synaptic transmission throughout the nervous system.
[Mh] Termos MeSH primário: Ambystoma/fisiologia
Subunidades beta da Proteína de Ligação ao GTP/metabolismo
Subunidades gama da Proteína de Ligação ao GTP/metabolismo
Receptores de Glutamato Metabotrópico/metabolismo
Células Fotorreceptoras Retinianas Cones/fisiologia
Proteínas SNARE/metabolismo
Sinapses/fisiologia
Transmissão Sináptica/fisiologia
[Mh] Termos MeSH secundário: Animais
Potenciais Pós-Sinápticos Excitadores/fisiologia
Feminino
Masculino
Receptores de Glutamato Metabotrópico/efeitos dos fármacos
Células Horizontais da Retina/metabolismo
Células Horizontais da Retina/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (G-protein Beta gamma); 0 (GTP-Binding Protein beta Subunits); 0 (GTP-Binding Protein gamma Subunits); 0 (Receptors, Metabotropic Glutamate); 0 (SNARE Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170402
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.2948-16.2017


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[PMID]:28235469
[Au] Autor:Noguera-Salvà MA; Guardiola-Serrano F; Martin ML; Marcilla-Etxenike A; Bergo MO; Busquets X; Escribá PV
[Ad] Endereço:Laboratory of Molecular Cell Biomedicine, Department of Biology, University of the Balearic Islands, E-07122 Palma, Balearic Islands, Spain.
[Ti] Título:Role of the C-terminal basic amino acids and the lipid anchor of the Gγ protein in membrane interactions and cell localization.
[So] Source:Biochim Biophys Acta;1859(9 Pt B):1536-1547, 2017 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Heterotrimeric G proteins are peripheral membrane proteins that frequently localize to the plasma membrane where their presence in molar excess over G protein coupled receptors permits signal amplification. Their distribution is regulated by protein-lipid interactions, which has a clear influence on their activity. Gßγ dimer drives the interaction between G protein heterotrimers with cell membranes. We focused our study on the role of the C-terminal region of the Gγ protein in G protein interactions with cell membranes. The Gγ subunit is modified at cysteine (Cys) 68 by the addition of an isoprenyl lipid, which is followed by the proteolytic removal of the last three residues that leaves an isoprenylated and carboxyl methylated Cys-68 as the terminal amino acid. The role of Cys isoprenylation of the CAAX box has been defined for other proteins, yet the importance of proteolysis and carboxyl methylation of isoprenylated proteins is less clear. Here, we showed that not only geranylgeranylation but also proteolysis and carboxyl methylation are essential for the correct localization of Gγ in the plasma membrane. Moreover, we showed the importance of electrostatic interactions between the inner leaflet of the plasma membrane and the positively charged C-terminal domain of the Gγ subunit (amino acids Arg-62, Lys-64 and Lys-65) as a second signal to reach the plasma membrane. Indeed, single or multiple point mutations at Gγ C-terminal amino acids have a significant effect on Gγ protein-plasma membrane interactions and its localization to charged Ld (liquid disordered) membrane microdomains. This article is part of a Special Issue entitled: Membrane Lipid Therapy: Drugs Targeting Biomembranes edited by Pablo V. Escribá.
[Mh] Termos MeSH primário: Membrana Celular/química
Subunidades gama da Proteína de Ligação ao GTP/química
Lipídeos de Membrana/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Linhagem Celular Tumoral
Diterpenos/metabolismo
Subunidades gama da Proteína de Ligação ao GTP/análise
Seres Humanos
Ligação Proteica
Prenilação de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Diterpenes); 0 (GTP-Binding Protein gamma Subunits); 0 (Membrane Lipids); 83807-40-3 (geranylgeranic acid)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170226
[St] Status:MEDLINE



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