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  • Mercury-induced dark-state instability and photobleaching alterations of the visual G-protein coupled receptor rhodopsin

     Morillo Cazorla, Margarita; Toledo Gonzalez, Darwin; Perez Gonzalez, Juan Jesus; Ramon Portés, Eva; Garriga Sole, Pere
    Chemical research in toxicology
    Vol. 27, num. 7, p. 1219-1226
    DOI: 10.1021/tx500114s
    Date of publication: 2014-07-01
    Journal article

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    Mercuric compounds were previously shown to affect the visual phototransduction cascade, and this could result in vision impairment. We have analyzed the effect of mercuric chloride on the structure and stability of the dim light vision photoreceptor rhodopsin. For this purpose, we have used both native rhodopsin imrnunopurified from bovine retinas and a recombinant mutant rhodopsin carrying several Cys to Ser substitutions in order to investigate the potential binding site of mercury on the receptor. Our results show that mercuric chloride dramatically reduces the stability of dark-state rhodopsin and alters the molecular features of the photoactived conformation obtained upon illumination by eliciting the formation of an altered photointermediate. The thermal bleaching kinetics of native and mutant rhodopsin is markedly accelerated by mercury in a concentration-dependent manner, and its chromophore regeneration ability is severely reduced without significantly affecting its G-protein activation capacity. Furthermore, fluorescence spectroscopic measurements on the retinal release process, ensuing illumination, suggest that mercury impairs complete retinal release from the receptor binding pocket. Our results provide further support for the capacity of mercury as a hazardous metal ion with reported deleterious effect on vision and provide a molecular explanation for such an effect at the rhodopsin photoreceptor level. We suggest that mercury could alter vision by acting in a specific manner on the molecular components of the retinoid cycle, particularly by modifying the ability of the visual photoreceptor protein rhodopsin to be regenerated and to be normally photoactivated by light.

  • Access to the full text
    Hsp90 inhibition protects against inherited retinal degeneration  Open access

     Aguilà Cerdà, Mònica; Bevilacqua, Dalila; McCulley, Caroline; Schwarz, Nele; Athanasiou, Dimitra; Kanuga, Naheed; Novoselov, Sergey S.; Lange, Clemens A.K.; Ali, Robin R.; Bainbridge, James W.; Gias, Carlos; Coffey, Peter J.; Garriga Sole, Pere; Cheetham, Michael E
    Human molecular genetics
    Vol. 23, num. 8, p. 2164-2175
    DOI: 10.1093/hmg/ddt613
    Date of publication: 2014-04-15
    Journal article

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    The molecular chaperone Hsp90 is important for the functional maturation of many client proteins, and inhibitors are in clinical trials for multiple indications in cancer. Hsp90 inhibition activates the heat shock response and can improve viability in a cell model of the P23H misfolding mutation in rhodopsin that causes autosomal dominant retinitis pigmentosa (adRP). Here, we show that a single low dose of the Hsp90 inhibitor HSP990 enhanced visual function and delayed photoreceptor degeneration in a P23H transgenic rat model. This was associated with the induction of heat shock protein expression and reduced rhodopsin aggregation. We then investigated the effect of Hsp90 inhibition on a different type of rod opsin mutant, R135L, which is hyperphosphorylated, binds arrestin and disrupts vesicular traffic. Hsp90 inhibition with 17-AAG reduced the intracellular accumulation of R135L and abolished arrestin binding in cells. Hsf-1(/) cells revealed that the effect of 17-AAG on P23H aggregation was dependent on HSF-1, whereas the effect on R135L was HSF-1 independent. Instead, the effect on R135L was mediated by a requirement of Hsp90 for rhodopsin kinase (GRK1) maturation and function. Importantly, Hsp90 inhibition restored R135L rod opsin localization to wild-type (WT) phenotype in vivo in rat retina. Prolonged Hsp90 inhibition with HSP990 in vivo led to a posttranslational reduction in GRK1 and phosphodiesterase (PDE6) protein levels, identifying them as Hsp90 clients. These data suggest that Hsp90 represents a potential therapeutic target for different types of rhodopsin adRP through distinct mechanisms, but also indicate that sustained Hsp90 inhibition might adversely affect visual function.

  • Binding specificity of retinal analogs to photoactivated visual pigments suggest mechanism for fine-tuning GPCR-ligand interactions

     Srinivasan, Sundaramoorthy; Ramon Portés, Eva; Cordomi, Arnau; Garriga Sole, Pere
    Chemistry and biology
    Vol. 21, num. 3, p. 369-378
    DOI: 10.1016/j.chembiol.2014.01.006
    Date of publication: 2014-03-20
    Journal article

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    11-cis-retinal acts as an inverse agonist stabilizing the inactive conformation of visual pigments, and upon photoactivation, it isomerizes to all-trans-retinal, initiating signal transduction. We have analyzed opsin regeneration with retinal analogs for rhodopsin and red cone opsin. We find differential binding of the analogs to the receptors after photobleaching and a dependence of the binding kinetics on the oligomerization state of the protein. The results outline the sensitivity of retinal entry to the binding pocket of visual receptors to the specific conformation adopted by the receptor and by the molecular architecture defined by specific amino acids in the binding pocket and the retinal entry site, as well as the topology of the retinal analog. Overall, our findings highlight the specificity of the ligand-opsin interactions, a feature that can be shared by other G-protein-coupled receptors.

  • G-protein-coupled receptors oligomerization: emerging signaling units and new opportunities for drug design

     Tena Campos, Merce; Ramon Portés, Eva; Rivera Rodriguez, Diana Marcela; Borroto Escuela, Dasiel Óscar; Romero Fernandez, Wilber; Fuxe, Kjell; Garriga Sole, Pere
    Current protein and peptide science
    Vol. 15, num. 7, p. 648-658
    DOI: 10.2174/1389203715666140901094248
    Date of publication: 2014-01-01
    Journal article

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    G-protein-coupled receptors (GPCRs) are a widespread family of transmembrane receptors with different physiologically relevant functions. Alterations in the structure and function of these receptors at different levels (ligand binding, signaling and trafficking) may result in a number of pathological conditions which represent a major health problem. Mutations in these receptors are also linked to different inherited diseases for which there is no cure to date. Rationale design, based on receptor structural knowledge, is needed for the discovery of novel drugs with higher selectivity and less side effects. In fact, about 50% of the drugs currently under development target this kind of receptors. Oligomerization among GPCRs has been clearly established from experimental, particularly in vitro, studies. Moreover, homo and heterodimerization provide new unexpected clues for explaining the molecular mechanisms underlying some diseases in which GPCRs signaling might be affected. In this review we will analyze GPCRs structure and function for a better understanding of the dimerization process and the experimental approaches currently used to detect such interactions. Furthermore, how drugs targeting heteromers can represent new opportunities to tackle novel and safer treatments of some pathologies will be described. Recent results, in this regard, will be reported as encouraging examples in the field. Finally, the newest technologies available for developing drugs targeting heteromers will also be reviewed highlighting the importance of bivalent ligands that emerge as very powerful molecules interacting with heteromers.

  • Differential uptake and release kinetics of photoactivated rhodopsin and red cone opsin

     Srinivasan, Sundaramoorthy; Ramon Portés, Eva; Morillo Cazorla, Margarita; Garriga Sole, Pere
    Congreso de la Sociedad Española de Bioquímica y Biología Molecular
    Presentation's date: 2013-09-04
    Presentation of work at congresses

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    Rhodopsin and cone opsins, the visual pigments of the vertebrate retina are a distinct group of G-protein-coupled receptors which are covalently bound to their ligand, the chromophoric 11-cis-retinal in the resting inactive state. The retinal binding site of these receptors is very dynamic allowing their conformational stabilization and functional activation. Though various retinal analogs were reported to behave as chromophores for retinal receptors, their specific physical properties and activation ability varies among them. We have carried out a study of the dynamics of the retinal binding site of rhodopsin and cone opsins after photo-activation which had not been previously analyzed. In order to do that, the photoreceptor genes inserted into the pMT4 vector were transiently transfected in COS-1 cells. Opsins regenerated with 11-cis-retinal were immunopurified by using rho-1D4 antibody. Fluorescence spectroscopy was employed to monitor conformational changes upon ligand binding to the receptor with retinal analogs 11-cis-retinal and 9-cis-retinal and their functional behavior was measured using a G-protein activation assay. We found that, after photo-activation, both retinals can access the binding pocket of red cone opsin but only 9-cis-retinal can occupy the retinal binding site of rhodopsin. The binding kinetics of 9-cis-retinal to photo-activated rhodopsin showed a faster entry into the retinal binding site followed by a binding process with t1/2 of ~1 min. Furthermore, the G-protein activation profile of post-bleached red cone and rhodopsin reveal differences which may account for the different rod and cone sensitivities. In summary, the present study suggests that the rhodopsin retinal binding site is less conformationally flexible than the red cone binding pocket which may be more open to permit the entry of both retinal analogs.

  • GalR1 interactions with 5HT1A, galanin and its N(1-15) terminal fragment

     Tena Campos, Merce; Borroto Escuela, Dasiel Óscar; Romero Fernandez, Wilber; Rivera Rodriguez, Diana Marcela; Lupala Lupala, Cecylia Severin; Perez Gonzalez, Juan Jesus; Fuxe, Kjell; Garriga Sole, Pere
    Congreso de la Sociedad Española de Bioquímica y Biología Molecular
    Presentation's date: 2013-09-04
    Presentation of work at congresses

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    Galanin receptor 1 (GalR1) is a G-protein coupled receptor (GPCR) widely distributed in the brain which elicits a wide range of biological effects via interactions with its cognate ligand galanin. Galanin is a 30-mer neuropeptide with an N-terminal region comprising about 15 highly conserved residues, which acts as the crucial region for agonist-receptor binding. Moreover, it has been recently shown that GalR1 could be involved in other brain processes due to its interactions with other GPCR via heterodimerization. The 5-HT1A serotonin receptor heterodimerizes with GalR1 receptor, and this interaction may modulate the molecular mechanism of depression in which this serotonin receptor is involved. We have explored how galanin ligand binding affects GalR1 heterodimerization with 5-HT1A, specially the difference between the native peptide and the N(1-15) terminal peptide, by means of FRET spectroscopy in HEK293 transiently transfected cells. We have also used synthetic peptides with sequential L-Ala substitutions of individual amino acids in the human galanin sequence and examined their effect on heterodimerization, especially for amino acids at positions (1-4) and (9-14) which seem to be essential for binding and functional coupling of the receptor. By using a construct where the 1D4 antigenic region has been fused to GalR1 using tailed PCR, we have been able to immunopurify this receptor from HEK293 cells, in order to analyze structural changes induced by the binding of the different galanin L-Ala variants using fluorescence spectroscopy. Finally, we have also probed GalR1-GalR2 heterodimerization by means of FRET.

  • Molecular insights into sector retinitis pigmentosa retinal disease

     Ramon Portés, Eva; Toledo Gonzalez, Darwin; Aguilà Cerdà, Mònica; Moore, A.T.; Webster, A.R.; Cheetham, Michael E; Garriga Sole, Pere
    International Union of Biochemistry and Molecular Biology Congress
    p. 429-
    Presentation's date: 2013-09-04
    Presentation of work at congresses

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  • Point mutations in visual photoreceptors: new insights into rhodopsin photoactivation

     Garriga Sole, Pere
    European Meeting on Phototransduction
    Presentation's date: 2013-06-20
    Presentation of work at congresses

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  • Improved Conformational Stability of the Visual G Protein-Coupled Receptor Rhodopsin by Specific Interaction with Docosahexaenoic Acid Phospholipid

     Sanchez Martin, Maria Jesús; Ramon Portés, Eva; Torrent Burgues, Juan; Garriga Sole, Pere
    Chembiochem
    Vol. 14, num. 5, p. 639-644
    DOI: 10.1002/cbic.201200687
    Date of publication: 2013-03
    Journal article

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    Rhodopsin is the photoreceptor located in the rod cells of the retina. It has seven transmembrane helices and is a prototypic member of the G protein-coupled receptor superfamily. The structures and functions of these receptors are clearly affected by the lipid composition of the cell membrane, and their study in a purified recombinant form is usually performed in detergent solution. There is a need to study these receptors in a physiologically relevant environment because the lipid environment is known to have an important effect on their function. In this work, rhodopsin reconstituted in docosahexaenoic acid (DHA) liposomes is shown to have more thermal stability than when it is solubilised with the neutral detergent dodecyl maltoside. Moreover, the specific interaction between rhodopsin and DHA was followed by means of Langmuir experiments with insertion of rhodopsin into lipid monolayers; this showed high affinity for the lipid-receptor interaction...

  • G protein-coupled receptor heterodimerization in the brain

     Borroto Escuela, Dasiel Óscar; Romero Fernandez, Wilber; Garriga Sole, Pere; Ciruela, Francisco; Narvaez, Manuel; Tarakanov, O.V.; Palkovits, Miklós; Agnati, Luigi F.; Fuxe, Kjell
    Methods in enzymology
    Vol. 521, p. 281-294
    DOI: 10.1016/B978-0-12-391862-8.00015-6
    Date of publication: 2013
    Journal article

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    G protein-coupled receptors (GPCRs) play critical roles in cellular processes and signaling and have been shown to form heteromers with diverge biochemical and/or pharmacological activities that are different from those of the corresponding monomers or homomers. However, despite extensive experimental results supporting the formation of GPCR heteromers in heterologous systems, the existence of such receptor heterocomplexes in the brain remains largely unknown, mostly because of the lack of appropriate methodology. Herein, we describe the in situ proximity ligation assay procedure underlining its high selectivity and sensitivity to image GPCR heteromers with confocal microscopy in brain sections. We describe here how the assay is performed and discuss advantages and disadvantages of this method compared with other available techniques.

  • Fluorescence studies of DHA liposomes ability to stabilize the G-protein-coupled receptor rhodopsin

     Sánchez Martín, Maria Jesús; Ramon Portés, Eva; Garriga Sole, Pere
    Luminescence
    Vol. 27, p. 551-552
    DOI: 10.1002/bio.2432
    Date of publication: 2012-12-19
    Journal article

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  • On the existence and function of galanin receptor heteromers in the central nervous system

     Fuxe, Kjell; Borroto Escuela, Dasiel Óscar; Romero Fernandez, Wilber; Tarakanov, O.V.; Calvo, Feliciano; Garriga Sole, Pere; Tena Campos, Merce; Narvaez, Manuel; Millón, Carmelo; Parrado, Concepción; Ciruela, Francisco; Agnati, Luigi F.; Narvaez, José Antonio; Díaz Cabiale, Zaida
    Frontiers in Endocrinology
    Vol. 3, num. 127, p. 1-12
    DOI: 10.3389/fendo.2012.00127
    Date of publication: 2012-10-26
    Journal article

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  • Cone opsin regeneration by retinal analogs

     Ramon Portés, Eva; Srinivasan, Sundaramoorthy; Sánchez Martín, Maria Jesús; Garriga Sole, Pere
    International Conference on Retinal Proteins
    Presentation's date: 2012-10-02
    Presentation of work at congresses

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  • Visual phototransduction: from visual pigments mutations to retinal disease

     Ramon Portés, Eva; Garriga Sole, Pere
    European Meeting on Phototransduction
    Presentation's date: 2012-09-29
    Presentation of work at congresses

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  • Improving the stability of the visual G-protein-coupled receptor rhodopsin in DHA liposomes

     Sánchez Martín, Maria Jesús; Ramon Portés, Eva; Garriga Sole, Pere
    International Union of Biochemistry and Molecular Biology Congress
    p. 471-
    Presentation's date: 2012-09-05
    Presentation of work at congresses

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  • Improving the stability of the visual G-protein-coupled receptor rhodopsin in DHA liposomes

     Sanchez Martin, Maria Jesús; Ramon Portés, Eva; Garriga Sole, Pere
    The FEBS journal
    Vol. 279, num. SI., p. 471
    Date of publication: 2012-09
    Journal article

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  • Extrasynaptic neurotransmission in the modulation of brain function. Focus on the striatal neuronal-glial networks

     Fuxe, Kjell; Borroto Escuela, Dasiel Óscar; Romero Fernandez, Wilber; Díaz Cabiale, Zaida; Rivera, Alicia; Ferraro, L.; Tanganelli, S.; Tarakanov, O.V.; Garriga Sole, Pere; Narvaez, Manuel; Ciruela, Francisco; Guescini, M.; Agnati, Luigi F.
    Frontiers in Physiology
    Vol. 3, num. 136
    DOI: 10.3389/fphys.2012.00136
    Date of publication: 2012-06
    Journal article

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  • Fluorescence studies of DHA liposomesability to stabilize the activeconformation of rhodopsin

     Sánchez Martín, Maria Jesús; Ramon Portés, Eva; Garriga Sole, Pere
    International Symposium on Luminiscence Spectrometry
    p. 17
    Presentation's date: 2012-05-02
    Presentation of work at congresses

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  • Molecular modeling of the M3 acetylcholine muscarinic receptor and its binding site

     Martinez Archundia, Marlet; Cordomí Montoya, Arnau; Garriga Sole, Pere; Perez Gonzalez, Juan Jesus
    Journal of biomedicine and biotechnology
    Vol. 2012, num. 789741
    DOI: 10.1155/2012/789741
    Date of publication: 2012
    Journal article

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  • ADDED VALUE FROM HIGH PROTEIN AND HIGH OIL INDUSTRIAL CO-STREAMS

     Torrent Burgues, Juan; Morillo Cazorla, Margarita; Macedo Fernandes, Margarida Maria; Garriga Sole, Pere; Rivera Rodriguez, Diana Marcela; Tzanov, Tzanko
    Competitive project

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  • NOVEL APPROACHES FOR PREVENTION AND DEGENERATION OF PATHOGENIC BACTERIA BIOFILMS FORMED ON MEDICAL DEVICES E.G.CATHETERS

     Ivanova, Kristina Dimitrova; Diaz Blanco, Carlos; Morillo Cazorla, Margarita; Torrent Burgues, Juan; Macedo Fernandes, Margarida Maria; Garriga Sole, Pere; Tzanov, Tzanko
    Competitive project

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  • ALTERACIONES PROCESOS ACTIVACION Y TRANSDUCCION DE SEÑAL DE RECEPTORES ACOPLADOS A PROTEINAS G

     Torrent Burgues, Juan; Hoyo Perez, Javier; Ramon Portés, Eva; Gotzens Garcia, Guadalupe; Guaus Guerrero, Ester; Morillo Cazorla, Margarita; Urtubia Vicario, Cesar; Roset Calzada, M. Lourdes; Garriga Sole, Pere
    Competitive project

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  • Comparative study of rhodopsin

     Srinivasan, Sundaramoorthy; Ramon Portés, Eva; Garriga Sole, Pere
    International Congress of the Spanish Biophysical Society
    Presentation of work at congresses

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    Rhodopsin and cone opsins, the photosensitive pigments of the vertebrate retina are a distinct group of G-protein-coupled receptors which are covalently bound to a chromophore, 11-cis-retinal. These receptors play a central role in the visual phototransduction process mediating dim-light vision and colour vision respectively. The kinetics of the response of the rod photoreceptor rhodopsin and its related cone opsins is very different suggesting important differences in both inter and intramolecular interactions. Photoactivation of these receptors leads to G-protein binding and activation and eventual retinal release from its binding pocket which causes structural rearrangements on the opsin apoproteins. Although the effect of various retinal analogs were reported to mimic -at least partially- the action of 11-cisretinal with opsins, the effect of retinal analogs on rhodopsin and cone opsins after photoactivation -at the post-bleaching level- has not been characterized in detail. This process is important for the regeneration of the fully-functional receptors after chromophore binding, and it is central to the desensitization mechanism of the photoreceptor cells. Rhodopsin and cone opsin genes -cloned into pMT4 plasmidwere transiently transfected and expressed in eukaryotic COS-1cells. Opsins were regenerated with 11-cis-retinal and purified by immunoaffinity chromatography using the Rho-1D4 monoclonal antibody coupled to a Sepharose matrix in dodecyl maltoside detergent solution. The rates of receptor reconstitution with 11-cis-retinal, and the retinal analog 9-cis-retinal, with rhodopsin and red cone opsin respectively, after bleaching, were analyzed by means of fluorescence spectroscopy. The results showed that, after bleaching, 9-cis-retinal can access the binding pocket of rhodopsin but 11-cis-retinal cannot. In contrast, both retinals can access the red cone opsin binding pocket of the photobleached receptor even long time after bleaching. We conclude that post-bleaching retinal reconstitution of opsins (rhodopsin and red cone opsin) reflects a variable degree of conformational flexibility that allows to preferentially accommodate certain retinal analogs. Studies are underway to incorporate these receptors into liposomes and to determine their ability to activate their corresponding G-proteins.

  • In vitro influence of Hg(II) on rhodopsin structure and function

     Morillo Cazorla, Margarita; Toledo Gonzalez, Darwin; Ramon Portés, Eva; Garriga Sole, Pere
    International Congress of the Spanish Biophysical Society
    p. 66-
    Presentation's date: 2012
    Presentation of work at congresses

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  • Salt effects on the conformational stability of the visual G-protein-coupled receptor rhodopsin

     Reyes Alcaraz, Arfaxad; Martinez Archundia, Marlet; Ramon Portés, Eva; Garriga Sole, Pere
    Biophysical journal
    Vol. 101, num. 11, p. 2798-2806
    DOI: 10.1016/j.bpj.2011.09.049
    Date of publication: 2011-12-07
    Journal article

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  • Altered trafficking and unfolded protein response induction as a result of M3 muscarinic receptor impaired N-glycosylation

     Romero Fernandez, Wilber; Borroto Escuela, Dasiel Óscar; Perez Alea, M.; Garcia Mesa, Y; Garriga Sole, Pere
    Glycobiology
    Vol. 21, num. 12, p. 1663-1672
    DOI: 10.1093/glycob/cwr105
    Date of publication: 2011-12
    Journal article

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  • Molecular mechanisms of disease for mutations at Gly-90 in rhodopsin

     Toledo Gonzalez, Darwin; Ramon Portés, Eva; Aguilà Cerdà, Mònica; Cordomí Montoya, Arnau; Perez Gonzalez, Juan Jesus; Mendes, H.F.; Cheetham, Michael E; Garriga Sole, Pere
    Journal of biological chemistry
    Vol. 286, num. 46, p. 39993-40001
    DOI: 10.1074/jbc.M110.201517
    Date of publication: 2011-11-18
    Journal article

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  • La química i la societat

     Grau Vilalta, Maria Dolors; Font Soldevila, Jose; Sanz Balague, Joaquim; Guaus Guerrero, Ester; Calvet Tarragona, Aurelio; Salán Ballesteros, Mª Núria; Martínez Martínez, María R.; Farran Marsa, Adriana; Gorchs Altarriba, Roser; Alvarez Del Castillo, M. Dolores; Garrido Soriano, Nuria; Morillo Cazorla, Margarita; Almajano Pablos, Maria Pilar; Cardona Planes, Anna Maria; Macanás de Benito, Jorge; Bonsfills Pedros, Ana; Gamisans Noguera, Javier; Dorado Castaño, Antonio David; Lao Luque, Concepcion; Torrent Burgues, Juan; Molins Duran, Gemma; Colom Fajula, Xavier; Carrillo Navarrete, Fernando; Ramon Portés, Eva; Garriga Sole, Pere; Sole Sardans, M. Montserrat; Ardanuy Raso, Monica; Pares Sabates, Ferran; Roncero Vivero, Maria Blanca; Cusola Aumedes, Oriol
    Collaboration in exhibitions

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  • Differential expression of muscarinic acetylcholine receptor subtypes in Jurkat cells and their signaling

     Alea, M.P.; Borroto Escuela, Dasiel Óscar; Romero Fernandez, Wilber; Fuxe, Kjell; Garriga Sole, Pere
    Journal of neuroimmunology
    Vol. 237, num. 1-2, p. 13-22
    DOI: 10.1016/j.jneuroim.2011.05.010
    Date of publication: 2011-08-15
    Journal article

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  • Structural and Stability Studies of Class A G-protein coupled receptors

     Reyes Alcaraz, Arfaxad
    Department of Chemical Engineering, Universitat Politècnica de Catalunya
    Theses

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  • Photointermediate stability changes in rhodopsin mutants associated with retinitis pigmentosa

     Ramon Portés, Eva; Bosch Presegue, Laia; Toledo Gonzalez, Darwin; Cordomí Montoya, Arnau; Garriga Sole, Pere
    Congreso de la Sociedad de Biofísica de España
    p. 140
    Presentation's date: 2011-07-01
    Presentation of work at congresses

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  • Overproduction of human M3 muscarinic acetylcholine receptor: An approach toward structural studies

     Romero Fernandez, Wilber; Garriga Sole, Pere; Borroto Escuela, Dasiel Óscar
    Biotechnology progress
    Vol. 27, num. 3, p. 838-845
    DOI: 10.1002/btpr.615
    Date of publication: 2011-06
    Journal article

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  • Alterations in the photoactivation pathway of rhodopsin mutants associated with retinitis pigmentosa

     Bosch Presegue, Laia; Ramon Portés, Eva; Toledo Gonzalez, Darwin; Cordomi Montoya, Arnau; Garriga Sole, Pere
    The FEBS journal
    Vol. 278, num. 9, p. 1493-1505
    DOI: 10.1111/j.1742-4658.2011.08066.x
    Date of publication: 2011-05
    Journal article

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    The visual photoreceptor rhodopsin undergoes a series of conformational changes upon light activation, eventually leading to the active metarhodopsin II conformation, which is able to bind and activate the G-protein, transducin. We have previously shown that mutant rhodopsins G51V and G89D, associated with retinitis pigmentosa, present photobleaching patterns characterized by the formation of altered photointermediates whose nature remained obscure. Our current detailed UV–visible spectroscopic analysis, together with functional characterization, indicate that these mutations influence the relative stability of the different metarhodopsin photointermediates by altering their equilibria and maintaining the receptor in a nonfunctional light-induced conformation that may be toxic to photoreceptor cells. We propose that G51V and G89D shift the equilibrium from metarhodopsin I towards an intermediate, recently named as metarhodopsin Ib, proposed to interact with transducin without activating it. This may be one of the causes contributing to the molecular mechanisms underlying cell death associated with some retinitis pigmentosa mutations.

  • Study of the M3 muscarinic acetylcholine receptor by molecular dynamics simulations and site-directed mutagenesis

     Martínez Archundia, Marlet Themis
    Department of Chemical Engineering, Universitat Politècnica de Catalunya
    Theses

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  • Hydrophobic amino acids at the cytoplasmic ends of helices 3 and 6 of rhodopsin conjointly modulate transducin activation

     Bosch Presegue, Laia; Iarriccio, Laura; Aguilà Cerdà, Mònica; Toledo Gonzalez, Darwin; Ramon Portés, Eva; Cordomí Montoya, Arnau; Garriga Sole, Pere
    Archives of biochemistry and biophysics
    Vol. 506, num. 2, p. 142-149
    DOI: 10.1016/j.abb.2010.11.019
    Date of publication: 2011-02-15
    Journal article

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    Rhodopsin is the visual photoreceptor responsible for dim light vision. This receptor is located in the rod cell of the retina and is a prototypical member of the G-protein-coupled receptor superfamily. The structural details underlying the molecular recognition event in transducin activation by photoactivated rhodopsin are of key interest to unravel the molecular mechanism of signal transduction in the retina. We constructed and expressed rhodopsin mutants in the second and third cytoplasmic domains of rhodopsin –where the natural amino acids were substituted by the human M3 acetylcholine muscarinic receptor homologous residues– in order to determine their potential involvement in G-protein recognition. These mutants showed normal chromophore formation and a similar photobleaching behavior than WT rhodopsin, but decreased thermal stability in the dark state. The single mutant V1383.53 and the multiple mutant containing V2275.62 and a combination of mutations at the cytoplasmic end of transmembrane helix 6 caused a reduction in transducin activation upon rhodopsin photoactivation. Furthermore, combination of mutants at the second and third cytoplasmic domains revealed a cooperative role, and partially restored transducin activation. The results indicate that hydrophobic interactions by V1383.53, V2275.62, V2506.33, V2546.37 and I2556.38 are critical for receptor activation and/or efficient rhodopsin–transducin interaction.

  • Muscarinic receptor family interacting proteins: Role in receptor function

     Borroto Escuela, Dasiel Óscar; Correia, Patricia A.; Romero Fernandez, Wilber; Narvaez, Manuel; Fuxe, Kjell; Ciruela, Francisco; Garriga Sole, Pere
    Journal of neuroscience methods
    Vol. 195, num. 2, p. 161-169
    DOI: 10.1016/j.jneumeth.2010.11.025
    Date of publication: 2011-02-15
    Journal article

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  • Dissecting the conserved NPxxY motif of the M(3) muscarinic acetylcholine receptor: Critical role of Asp-7.49 for receptor signaling and multiprotein complex formation

     Borroto Escuela, Dasiel Óscar; Romero Fernandez, Wilber; Garcia Negredo, G.; Correia, Patricia A.; Garriga Sole, Pere; Fuxe, Kjell; Ciruela, Francisco
    Cellular physiology and biochemistry
    Vol. 28, num. 5, p. 1009-1022
    DOI: 10.1159/000335788
    Date of publication: 2011
    Journal article

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  • Novel insights into galanin Nterminal fragment (1-15)- GalR1/GalR2 heteroreceptor interactions

     Perez Gonzalez, Juan Jesus; Garriga Sole, Pere
    Congreso de la Sociedad Española de Bioquímica y Biología Molecular
    p. 249
    Presentation of work at congresses

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  • Conformational Studies of the M3 Acetylcholine Muscarinic Receptor and its Binding Site

     Perez Gonzalez, Juan Jesus; Garriga Sole, Pere
    Congreso de la Sociedad de Biofísica de España
    p. 104
    Presentation of work at congresses

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  • Inorganic salt effects on the stability of the active and inactive conformations of the G-protein coupled receptor rhodopsin

     Reyes Alcaraz, Arfaxad; Martinez Archundia, Marlet; Garriga Sole, Pere
    Congreso de la Sociedad de Biofísica de España
    p. 151
    Presentation of work at congresses

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  • Efficient G-protein activation by fully-functional rhodopsin in the dark by the release of critical structural constraints

     Ramon Portés, Eva; Toledo Gonzalez, Darwin; Reyes Alcaraz, Arfaxad; Morillo Cazorla, Margarita; Garriga Sole, Pere
    Congreso de la Sociedad Española de Bioquímica y Biología Molecular
    p. 248-
    Presentation of work at congresses

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  • Molecular mechanisms for retinal diseases caused by mutations at Gly90 in the visual G protein coupled receptor, rhodopsin

     Ramon Portés, Eva; Toledo Gonzalez, Darwin; Aguilà Cerdà, Mònica; Cordomí Montoya, Arnau; Mendes, Hugo F.; Cheetham, Michael E; Garriga Sole, Pere
    Congreso de la Sociedad Española de Bioquímica y Biología Molecular
    p. 239-240
    Presentation of work at congresses

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  • New insights into the molecular mechanisms of rhodopsin retinitis pigmentosa

     Aguilà Cerdà, Mònica
    Department of Chemical Engineering, Universitat Politècnica de Catalunya
    Theses

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  • On-chip photoactivation of heterologously expressed rhodopsin allows kinetic analysis of G-protein signaling by surface plasmon resonance spectroscopy

     Komolov, Konstantin E.; Aguilà Cerdà, Mònica; Toledo Gonzalez, Darwin; Manyosa Ribatallada, Joan; Garriga Sole, Pere; Koch, Karl-Wilhelm
    Analytical and bioanalytical chemistry
    Vol. 397, num. 7, p. 2967-2976
    DOI: 10.1007/s00216-010-3876-4
    Date of publication: 2010-08
    Journal article

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  • The M-5 muscarinic acetylcholine receptor third intracellular loop regulates receptor function and oligomerization

     Borroto Escuela, Dasiel Óscar; Garcia Negredo, G.; Garriga Sole, Pere; Fuxe, Kjell; Ciruela, Francisco
    Biochimica et biophysica acta. Molecular cell research
    Vol. 1803, num. 7, p. 813-825
    DOI: 10.1016/j.bbamcr.2010.04.002
    Date of publication: 2010-07
    Journal article

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  • SUBVENCIÓ-Exp.090130 FUNDACIÓ MARATÓ TVE

     Morillo Cazorla, Margarita; Garriga Sole, Pere
    Competitive project

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  • Impaired M-3 Muscarinic Acetylcholine Receptor Signal Transduction Through Blockade of Binding of Multiple Proteins to its Third Intracellular Loop

     Borroto Escuela, Dasiel Óscar; Correia, Patricia A.; Narvaez, Manuel; Garriga Sole, Pere; Fuxe, Kjell; Ciruela, Francisco
    Cellular physiology and biochemistry
    Vol. 25, num. 4-5, p. 397-408
    DOI: 10.1159/000303044
    Date of publication: 2010
    Journal article

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  • Access to the full text
    A dual role for EDEM1 in the processing of rod opsin  Open access

     Kosmaoglou, Maria; Kanuga, Naheed; Aguilà Cerdà, Mònica; Garriga Sole, Pere; Cheetham, Michael E
    Journal of cell science
    Vol. 122, num. 24, p. 4465-4472
    DOI: 10.1242/jcs.055228
    Date of publication: 2009-12
    Journal article

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  • A PILOT LINE OF ANTIBACTERIAL AND ANTIFUGAL MEDICAL TEXTILES BASED ON A SONOCHEMICAL PROCESS

     Morillo Cazorla, Margarita; Martinez Lopez, Juan; Gibert Vives, Jose Maria; Daga Monmany, Jose Maria; Garriga Sole, Pere; Torrent Burgues, Juan; Tzanov, Tzanko
    Competitive project

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