The oligomeric state sets $ GABA_{B} $ receptor signalling efficacy
Abstract G protein‐coupled receptors (GPCRs) have key roles in cell–cell communication. Recent data suggest that these receptors can form large complexes, a possibility expected to expand the complexity of this regulatory system. Among the brain GPCRs, the heterodimeric $ GABA_{B} $ receptor is one...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Comps‐Agrar, Laëtitia [verfasserIn] Kniazeff, Julie [verfasserIn] Nørskov‐Lauritsen, Lenea [verfasserIn] Maurel, Damien [verfasserIn] Gassmann, Martin [verfasserIn] Gregor, Nathalie [verfasserIn] Prézeau, Laurent [verfasserIn] Bettler, Bernhard [verfasserIn] Durroux, Thierry [verfasserIn] Trinquet, Eric [verfasserIn] Pin, Jean‐Philippe [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2011 |
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| Schlagwörter: |
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| Anmerkung: |
© European Molecular Biology Organization 2011 |
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| Übergeordnetes Werk: |
Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 30(2011), 12 vom: 06. Mai, Seite 2336-2349 |
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| Übergeordnetes Werk: |
volume:30 ; year:2011 ; number:12 ; day:06 ; month:05 ; pages:2336-2349 |
| Links: |
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| DOI / URN: |
10.1038/emboj.2011.143 |
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| Katalog-ID: |
SPR058011277 |
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| 520 | |a Abstract G protein‐coupled receptors (GPCRs) have key roles in cell–cell communication. Recent data suggest that these receptors can form large complexes, a possibility expected to expand the complexity of this regulatory system. Among the brain GPCRs, the heterodimeric $ GABA_{B} $ receptor is one of the most abundant, being distributed in most brain regions, on either pre‐ or post‐synaptic elements. Here, using specific antibodies labelled with time‐resolved FRET compatible fluorophores, we provide evidence that the heterodimeric $ GABA_{B} $ receptor can form higher‐ordered oligomers in the brain, as suggested by the close proximity of the $ GABA_{B1} $ subunits. Destabilizing the oligomers using a competitor or a $ GABA_{B1} $ mutant revealed different G protein coupling efficiencies depending on the oligomeric state of the receptor. By examining, in heterologous system, the G protein coupling properties of such $ GABA_{B} $ receptor oligomers composed of a wild‐type and a non‐functional mutant heterodimer, we provide evidence for a negative functional cooperativity between the $ GABA_{B} $ heterodimers. | ||
| 520 | |a Abstract This paper adds to the complexity of GPCR signalling, revealing hetero‐tetramer formation for native GABAB receptors in brain tissue. An elegant mutational approach further reveals functionally relevant negative cooperativity between GABAB heterodimers. | ||
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| 700 | 1 | |a Kniazeff, Julie |e verfasserin |4 aut | |
| 700 | 1 | |a Nørskov‐Lauritsen, Lenea |e verfasserin |4 aut | |
| 700 | 1 | |a Maurel, Damien |e verfasserin |4 aut | |
| 700 | 1 | |a Gassmann, Martin |e verfasserin |4 aut | |
| 700 | 1 | |a Gregor, Nathalie |e verfasserin |4 aut | |
| 700 | 1 | |a Prézeau, Laurent |e verfasserin |4 aut | |
| 700 | 1 | |a Bettler, Bernhard |e verfasserin |4 aut | |
| 700 | 1 | |a Durroux, Thierry |e verfasserin |4 aut | |
| 700 | 1 | |a Trinquet, Eric |e verfasserin |4 aut | |
| 700 | 1 | |a Pin, Jean‐Philippe |e verfasserin |4 aut | |
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10.1038/emboj.2011.143 doi (DE-627)SPR058011277 (SPR)emboj.2011.143-e DE-627 ger DE-627 rakwb eng Comps‐Agrar, Laëtitia verfasserin aut The oligomeric state sets $ GABA_{B} $ receptor signalling efficacy 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2011 Abstract G protein‐coupled receptors (GPCRs) have key roles in cell–cell communication. Recent data suggest that these receptors can form large complexes, a possibility expected to expand the complexity of this regulatory system. Among the brain GPCRs, the heterodimeric $ GABA_{B} $ receptor is one of the most abundant, being distributed in most brain regions, on either pre‐ or post‐synaptic elements. Here, using specific antibodies labelled with time‐resolved FRET compatible fluorophores, we provide evidence that the heterodimeric $ GABA_{B} $ receptor can form higher‐ordered oligomers in the brain, as suggested by the close proximity of the $ GABA_{B1} $ subunits. Destabilizing the oligomers using a competitor or a $ GABA_{B1} $ mutant revealed different G protein coupling efficiencies depending on the oligomeric state of the receptor. By examining, in heterologous system, the G protein coupling properties of such $ GABA_{B} $ receptor oligomers composed of a wild‐type and a non‐functional mutant heterodimer, we provide evidence for a negative functional cooperativity between the $ GABA_{B} $ heterodimers. Abstract This paper adds to the complexity of GPCR signalling, revealing hetero‐tetramer formation for native GABAB receptors in brain tissue. An elegant mutational approach further reveals functionally relevant negative cooperativity between GABAB heterodimers. cooperativity (dpeaa)DE-He213 GABA (dpeaa)DE-He213 GABA (dpeaa)DE-He213 GPCR (dpeaa)DE-He213 receptor oligomer (dpeaa)DE-He213 Kniazeff, Julie verfasserin aut Nørskov‐Lauritsen, Lenea verfasserin aut Maurel, Damien verfasserin aut Gassmann, Martin verfasserin aut Gregor, Nathalie verfasserin aut Prézeau, Laurent verfasserin aut Bettler, Bernhard verfasserin aut Durroux, Thierry verfasserin aut Trinquet, Eric verfasserin aut Pin, Jean‐Philippe verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 30(2011), 12 vom: 06. Mai, Seite 2336-2349 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:30 year:2011 number:12 day:06 month:05 pages:2336-2349 https://dx.doi.org/10.1038/emboj.2011.143 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 30 2011 12 06 05 2336-2349 |
| spelling |
10.1038/emboj.2011.143 doi (DE-627)SPR058011277 (SPR)emboj.2011.143-e DE-627 ger DE-627 rakwb eng Comps‐Agrar, Laëtitia verfasserin aut The oligomeric state sets $ GABA_{B} $ receptor signalling efficacy 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2011 Abstract G protein‐coupled receptors (GPCRs) have key roles in cell–cell communication. Recent data suggest that these receptors can form large complexes, a possibility expected to expand the complexity of this regulatory system. Among the brain GPCRs, the heterodimeric $ GABA_{B} $ receptor is one of the most abundant, being distributed in most brain regions, on either pre‐ or post‐synaptic elements. Here, using specific antibodies labelled with time‐resolved FRET compatible fluorophores, we provide evidence that the heterodimeric $ GABA_{B} $ receptor can form higher‐ordered oligomers in the brain, as suggested by the close proximity of the $ GABA_{B1} $ subunits. Destabilizing the oligomers using a competitor or a $ GABA_{B1} $ mutant revealed different G protein coupling efficiencies depending on the oligomeric state of the receptor. By examining, in heterologous system, the G protein coupling properties of such $ GABA_{B} $ receptor oligomers composed of a wild‐type and a non‐functional mutant heterodimer, we provide evidence for a negative functional cooperativity between the $ GABA_{B} $ heterodimers. Abstract This paper adds to the complexity of GPCR signalling, revealing hetero‐tetramer formation for native GABAB receptors in brain tissue. An elegant mutational approach further reveals functionally relevant negative cooperativity between GABAB heterodimers. cooperativity (dpeaa)DE-He213 GABA (dpeaa)DE-He213 GABA (dpeaa)DE-He213 GPCR (dpeaa)DE-He213 receptor oligomer (dpeaa)DE-He213 Kniazeff, Julie verfasserin aut Nørskov‐Lauritsen, Lenea verfasserin aut Maurel, Damien verfasserin aut Gassmann, Martin verfasserin aut Gregor, Nathalie verfasserin aut Prézeau, Laurent verfasserin aut Bettler, Bernhard verfasserin aut Durroux, Thierry verfasserin aut Trinquet, Eric verfasserin aut Pin, Jean‐Philippe verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 30(2011), 12 vom: 06. Mai, Seite 2336-2349 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:30 year:2011 number:12 day:06 month:05 pages:2336-2349 https://dx.doi.org/10.1038/emboj.2011.143 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 30 2011 12 06 05 2336-2349 |
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10.1038/emboj.2011.143 doi (DE-627)SPR058011277 (SPR)emboj.2011.143-e DE-627 ger DE-627 rakwb eng Comps‐Agrar, Laëtitia verfasserin aut The oligomeric state sets $ GABA_{B} $ receptor signalling efficacy 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2011 Abstract G protein‐coupled receptors (GPCRs) have key roles in cell–cell communication. Recent data suggest that these receptors can form large complexes, a possibility expected to expand the complexity of this regulatory system. Among the brain GPCRs, the heterodimeric $ GABA_{B} $ receptor is one of the most abundant, being distributed in most brain regions, on either pre‐ or post‐synaptic elements. Here, using specific antibodies labelled with time‐resolved FRET compatible fluorophores, we provide evidence that the heterodimeric $ GABA_{B} $ receptor can form higher‐ordered oligomers in the brain, as suggested by the close proximity of the $ GABA_{B1} $ subunits. Destabilizing the oligomers using a competitor or a $ GABA_{B1} $ mutant revealed different G protein coupling efficiencies depending on the oligomeric state of the receptor. By examining, in heterologous system, the G protein coupling properties of such $ GABA_{B} $ receptor oligomers composed of a wild‐type and a non‐functional mutant heterodimer, we provide evidence for a negative functional cooperativity between the $ GABA_{B} $ heterodimers. Abstract This paper adds to the complexity of GPCR signalling, revealing hetero‐tetramer formation for native GABAB receptors in brain tissue. An elegant mutational approach further reveals functionally relevant negative cooperativity between GABAB heterodimers. cooperativity (dpeaa)DE-He213 GABA (dpeaa)DE-He213 GABA (dpeaa)DE-He213 GPCR (dpeaa)DE-He213 receptor oligomer (dpeaa)DE-He213 Kniazeff, Julie verfasserin aut Nørskov‐Lauritsen, Lenea verfasserin aut Maurel, Damien verfasserin aut Gassmann, Martin verfasserin aut Gregor, Nathalie verfasserin aut Prézeau, Laurent verfasserin aut Bettler, Bernhard verfasserin aut Durroux, Thierry verfasserin aut Trinquet, Eric verfasserin aut Pin, Jean‐Philippe verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 30(2011), 12 vom: 06. Mai, Seite 2336-2349 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:30 year:2011 number:12 day:06 month:05 pages:2336-2349 https://dx.doi.org/10.1038/emboj.2011.143 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 30 2011 12 06 05 2336-2349 |
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10.1038/emboj.2011.143 doi (DE-627)SPR058011277 (SPR)emboj.2011.143-e DE-627 ger DE-627 rakwb eng Comps‐Agrar, Laëtitia verfasserin aut The oligomeric state sets $ GABA_{B} $ receptor signalling efficacy 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2011 Abstract G protein‐coupled receptors (GPCRs) have key roles in cell–cell communication. Recent data suggest that these receptors can form large complexes, a possibility expected to expand the complexity of this regulatory system. Among the brain GPCRs, the heterodimeric $ GABA_{B} $ receptor is one of the most abundant, being distributed in most brain regions, on either pre‐ or post‐synaptic elements. Here, using specific antibodies labelled with time‐resolved FRET compatible fluorophores, we provide evidence that the heterodimeric $ GABA_{B} $ receptor can form higher‐ordered oligomers in the brain, as suggested by the close proximity of the $ GABA_{B1} $ subunits. Destabilizing the oligomers using a competitor or a $ GABA_{B1} $ mutant revealed different G protein coupling efficiencies depending on the oligomeric state of the receptor. By examining, in heterologous system, the G protein coupling properties of such $ GABA_{B} $ receptor oligomers composed of a wild‐type and a non‐functional mutant heterodimer, we provide evidence for a negative functional cooperativity between the $ GABA_{B} $ heterodimers. Abstract This paper adds to the complexity of GPCR signalling, revealing hetero‐tetramer formation for native GABAB receptors in brain tissue. An elegant mutational approach further reveals functionally relevant negative cooperativity between GABAB heterodimers. cooperativity (dpeaa)DE-He213 GABA (dpeaa)DE-He213 GABA (dpeaa)DE-He213 GPCR (dpeaa)DE-He213 receptor oligomer (dpeaa)DE-He213 Kniazeff, Julie verfasserin aut Nørskov‐Lauritsen, Lenea verfasserin aut Maurel, Damien verfasserin aut Gassmann, Martin verfasserin aut Gregor, Nathalie verfasserin aut Prézeau, Laurent verfasserin aut Bettler, Bernhard verfasserin aut Durroux, Thierry verfasserin aut Trinquet, Eric verfasserin aut Pin, Jean‐Philippe verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 30(2011), 12 vom: 06. Mai, Seite 2336-2349 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:30 year:2011 number:12 day:06 month:05 pages:2336-2349 https://dx.doi.org/10.1038/emboj.2011.143 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 30 2011 12 06 05 2336-2349 |
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10.1038/emboj.2011.143 doi (DE-627)SPR058011277 (SPR)emboj.2011.143-e DE-627 ger DE-627 rakwb eng Comps‐Agrar, Laëtitia verfasserin aut The oligomeric state sets $ GABA_{B} $ receptor signalling efficacy 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2011 Abstract G protein‐coupled receptors (GPCRs) have key roles in cell–cell communication. Recent data suggest that these receptors can form large complexes, a possibility expected to expand the complexity of this regulatory system. Among the brain GPCRs, the heterodimeric $ GABA_{B} $ receptor is one of the most abundant, being distributed in most brain regions, on either pre‐ or post‐synaptic elements. Here, using specific antibodies labelled with time‐resolved FRET compatible fluorophores, we provide evidence that the heterodimeric $ GABA_{B} $ receptor can form higher‐ordered oligomers in the brain, as suggested by the close proximity of the $ GABA_{B1} $ subunits. Destabilizing the oligomers using a competitor or a $ GABA_{B1} $ mutant revealed different G protein coupling efficiencies depending on the oligomeric state of the receptor. By examining, in heterologous system, the G protein coupling properties of such $ GABA_{B} $ receptor oligomers composed of a wild‐type and a non‐functional mutant heterodimer, we provide evidence for a negative functional cooperativity between the $ GABA_{B} $ heterodimers. Abstract This paper adds to the complexity of GPCR signalling, revealing hetero‐tetramer formation for native GABAB receptors in brain tissue. An elegant mutational approach further reveals functionally relevant negative cooperativity between GABAB heterodimers. cooperativity (dpeaa)DE-He213 GABA (dpeaa)DE-He213 GABA (dpeaa)DE-He213 GPCR (dpeaa)DE-He213 receptor oligomer (dpeaa)DE-He213 Kniazeff, Julie verfasserin aut Nørskov‐Lauritsen, Lenea verfasserin aut Maurel, Damien verfasserin aut Gassmann, Martin verfasserin aut Gregor, Nathalie verfasserin aut Prézeau, Laurent verfasserin aut Bettler, Bernhard verfasserin aut Durroux, Thierry verfasserin aut Trinquet, Eric verfasserin aut Pin, Jean‐Philippe verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 30(2011), 12 vom: 06. Mai, Seite 2336-2349 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:30 year:2011 number:12 day:06 month:05 pages:2336-2349 https://dx.doi.org/10.1038/emboj.2011.143 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 30 2011 12 06 05 2336-2349 |
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Comps‐Agrar, Laëtitia @@aut@@ Kniazeff, Julie @@aut@@ Nørskov‐Lauritsen, Lenea @@aut@@ Maurel, Damien @@aut@@ Gassmann, Martin @@aut@@ Gregor, Nathalie @@aut@@ Prézeau, Laurent @@aut@@ Bettler, Bernhard @@aut@@ Durroux, Thierry @@aut@@ Trinquet, Eric @@aut@@ Pin, Jean‐Philippe @@aut@@ |
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Comps‐Agrar, Laëtitia |
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The oligomeric state sets $ GABA_{B} $ receptor signalling efficacy cooperativity (dpeaa)DE-He213 GABA (dpeaa)DE-He213 GPCR (dpeaa)DE-He213 receptor oligomer (dpeaa)DE-He213 |
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Comps‐Agrar, Laëtitia Kniazeff, Julie Nørskov‐Lauritsen, Lenea Maurel, Damien Gassmann, Martin Gregor, Nathalie Prézeau, Laurent Bettler, Bernhard Durroux, Thierry Trinquet, Eric Pin, Jean‐Philippe |
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the oligomeric state sets $ gaba_{b} $ receptor signalling efficacy |
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The oligomeric state sets $ GABA_{B} $ receptor signalling efficacy |
| abstract |
Abstract G protein‐coupled receptors (GPCRs) have key roles in cell–cell communication. Recent data suggest that these receptors can form large complexes, a possibility expected to expand the complexity of this regulatory system. Among the brain GPCRs, the heterodimeric $ GABA_{B} $ receptor is one of the most abundant, being distributed in most brain regions, on either pre‐ or post‐synaptic elements. Here, using specific antibodies labelled with time‐resolved FRET compatible fluorophores, we provide evidence that the heterodimeric $ GABA_{B} $ receptor can form higher‐ordered oligomers in the brain, as suggested by the close proximity of the $ GABA_{B1} $ subunits. Destabilizing the oligomers using a competitor or a $ GABA_{B1} $ mutant revealed different G protein coupling efficiencies depending on the oligomeric state of the receptor. By examining, in heterologous system, the G protein coupling properties of such $ GABA_{B} $ receptor oligomers composed of a wild‐type and a non‐functional mutant heterodimer, we provide evidence for a negative functional cooperativity between the $ GABA_{B} $ heterodimers. Abstract This paper adds to the complexity of GPCR signalling, revealing hetero‐tetramer formation for native GABAB receptors in brain tissue. An elegant mutational approach further reveals functionally relevant negative cooperativity between GABAB heterodimers. © European Molecular Biology Organization 2011 |
| abstractGer |
Abstract G protein‐coupled receptors (GPCRs) have key roles in cell–cell communication. Recent data suggest that these receptors can form large complexes, a possibility expected to expand the complexity of this regulatory system. Among the brain GPCRs, the heterodimeric $ GABA_{B} $ receptor is one of the most abundant, being distributed in most brain regions, on either pre‐ or post‐synaptic elements. Here, using specific antibodies labelled with time‐resolved FRET compatible fluorophores, we provide evidence that the heterodimeric $ GABA_{B} $ receptor can form higher‐ordered oligomers in the brain, as suggested by the close proximity of the $ GABA_{B1} $ subunits. Destabilizing the oligomers using a competitor or a $ GABA_{B1} $ mutant revealed different G protein coupling efficiencies depending on the oligomeric state of the receptor. By examining, in heterologous system, the G protein coupling properties of such $ GABA_{B} $ receptor oligomers composed of a wild‐type and a non‐functional mutant heterodimer, we provide evidence for a negative functional cooperativity between the $ GABA_{B} $ heterodimers. Abstract This paper adds to the complexity of GPCR signalling, revealing hetero‐tetramer formation for native GABAB receptors in brain tissue. An elegant mutational approach further reveals functionally relevant negative cooperativity between GABAB heterodimers. © European Molecular Biology Organization 2011 |
| abstract_unstemmed |
Abstract G protein‐coupled receptors (GPCRs) have key roles in cell–cell communication. Recent data suggest that these receptors can form large complexes, a possibility expected to expand the complexity of this regulatory system. Among the brain GPCRs, the heterodimeric $ GABA_{B} $ receptor is one of the most abundant, being distributed in most brain regions, on either pre‐ or post‐synaptic elements. Here, using specific antibodies labelled with time‐resolved FRET compatible fluorophores, we provide evidence that the heterodimeric $ GABA_{B} $ receptor can form higher‐ordered oligomers in the brain, as suggested by the close proximity of the $ GABA_{B1} $ subunits. Destabilizing the oligomers using a competitor or a $ GABA_{B1} $ mutant revealed different G protein coupling efficiencies depending on the oligomeric state of the receptor. By examining, in heterologous system, the G protein coupling properties of such $ GABA_{B} $ receptor oligomers composed of a wild‐type and a non‐functional mutant heterodimer, we provide evidence for a negative functional cooperativity between the $ GABA_{B} $ heterodimers. Abstract This paper adds to the complexity of GPCR signalling, revealing hetero‐tetramer formation for native GABAB receptors in brain tissue. An elegant mutational approach further reveals functionally relevant negative cooperativity between GABAB heterodimers. © European Molecular Biology Organization 2011 |
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The oligomeric state sets $ GABA_{B} $ receptor signalling efficacy |
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Kniazeff, Julie Nørskov‐Lauritsen, Lenea Maurel, Damien Gassmann, Martin Gregor, Nathalie Prézeau, Laurent Bettler, Bernhard Durroux, Thierry Trinquet, Eric Pin, Jean‐Philippe |
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| score |
7.399441 |