Agonist-selective recruitment of engineered protein probes and of GRK2 by opioid receptors in living cells

G protein-coupled receptors (GPCRs) signal through allostery, and it is increasingly clear that chemically distinct agonists can produce different receptor-based effects. It has been proposed that agonists selectively promote receptors to recruit one cellular interacting partner over another, introd...
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Autor*in:	Miriam Stoeber [verfasserIn] Damien Jullié [verfasserIn] Joy Li [verfasserIn] Soumen Chakraborty [verfasserIn] Susruta Majumdar [verfasserIn] Nevin A Lambert [verfasserIn] Aashish Manglik [verfasserIn] Mark von Zastrow [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2020

Schlagwörter:	GPCR opioid biosensor receptor kinase agonist bias TIRF

Übergeordnetes Werk:	In: eLife - eLife Sciences Publications Ltd, 2013, 9(2020)
Übergeordnetes Werk:	volume:9 ; year:2020

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.7554/eLife.54208

Katalog-ID:	DOAJ032295014

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allfields	10.7554/eLife.54208 doi (DE-627)DOAJ032295014 (DE-599)DOAJ8c895244c98b40adb73cdb12ae8fea95 DE-627 ger DE-627 rakwb eng QH301-705.5 Miriam Stoeber verfasserin aut Agonist-selective recruitment of engineered protein probes and of GRK2 by opioid receptors in living cells 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier G protein-coupled receptors (GPCRs) signal through allostery, and it is increasingly clear that chemically distinct agonists can produce different receptor-based effects. It has been proposed that agonists selectively promote receptors to recruit one cellular interacting partner over another, introducing allosteric ‘bias’ into the signaling system. However, the underlying hypothesis - that different agonists drive GPCRs to engage different cytoplasmic proteins in living cells - remains untested due to the complexity of readouts through which receptor-proximal interactions are typically inferred. We describe a cell-based assay to overcome this challenge, based on GPCR-interacting biosensors that are disconnected from endogenous transduction mechanisms. Focusing on opioid receptors, we directly demonstrate differences between biosensor recruitment produced by chemically distinct opioid ligands in living cells. We then show that selective recruitment applies to GRK2, a biologically relevant GPCR regulator, through discrete interactions of GRK2 with receptors or with G protein beta-gamma subunits which are differentially promoted by agonists. GPCR opioid biosensor receptor kinase agonist bias TIRF Medicine R Science Q Biology (General) Damien Jullié verfasserin aut Joy Li verfasserin aut Soumen Chakraborty verfasserin aut Susruta Majumdar verfasserin aut Nevin A Lambert verfasserin aut Aashish Manglik verfasserin aut Mark von Zastrow verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 9(2020) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:9 year:2020 https://doi.org/10.7554/eLife.54208 kostenfrei https://doaj.org/article/8c895244c98b40adb73cdb12ae8fea95 kostenfrei https://elifesciences.org/articles/54208 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2020
spelling	10.7554/eLife.54208 doi (DE-627)DOAJ032295014 (DE-599)DOAJ8c895244c98b40adb73cdb12ae8fea95 DE-627 ger DE-627 rakwb eng QH301-705.5 Miriam Stoeber verfasserin aut Agonist-selective recruitment of engineered protein probes and of GRK2 by opioid receptors in living cells 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier G protein-coupled receptors (GPCRs) signal through allostery, and it is increasingly clear that chemically distinct agonists can produce different receptor-based effects. It has been proposed that agonists selectively promote receptors to recruit one cellular interacting partner over another, introducing allosteric ‘bias’ into the signaling system. However, the underlying hypothesis - that different agonists drive GPCRs to engage different cytoplasmic proteins in living cells - remains untested due to the complexity of readouts through which receptor-proximal interactions are typically inferred. We describe a cell-based assay to overcome this challenge, based on GPCR-interacting biosensors that are disconnected from endogenous transduction mechanisms. Focusing on opioid receptors, we directly demonstrate differences between biosensor recruitment produced by chemically distinct opioid ligands in living cells. We then show that selective recruitment applies to GRK2, a biologically relevant GPCR regulator, through discrete interactions of GRK2 with receptors or with G protein beta-gamma subunits which are differentially promoted by agonists. GPCR opioid biosensor receptor kinase agonist bias TIRF Medicine R Science Q Biology (General) Damien Jullié verfasserin aut Joy Li verfasserin aut Soumen Chakraborty verfasserin aut Susruta Majumdar verfasserin aut Nevin A Lambert verfasserin aut Aashish Manglik verfasserin aut Mark von Zastrow verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 9(2020) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:9 year:2020 https://doi.org/10.7554/eLife.54208 kostenfrei https://doaj.org/article/8c895244c98b40adb73cdb12ae8fea95 kostenfrei https://elifesciences.org/articles/54208 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2020
allfields_unstemmed	10.7554/eLife.54208 doi (DE-627)DOAJ032295014 (DE-599)DOAJ8c895244c98b40adb73cdb12ae8fea95 DE-627 ger DE-627 rakwb eng QH301-705.5 Miriam Stoeber verfasserin aut Agonist-selective recruitment of engineered protein probes and of GRK2 by opioid receptors in living cells 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier G protein-coupled receptors (GPCRs) signal through allostery, and it is increasingly clear that chemically distinct agonists can produce different receptor-based effects. It has been proposed that agonists selectively promote receptors to recruit one cellular interacting partner over another, introducing allosteric ‘bias’ into the signaling system. However, the underlying hypothesis - that different agonists drive GPCRs to engage different cytoplasmic proteins in living cells - remains untested due to the complexity of readouts through which receptor-proximal interactions are typically inferred. We describe a cell-based assay to overcome this challenge, based on GPCR-interacting biosensors that are disconnected from endogenous transduction mechanisms. Focusing on opioid receptors, we directly demonstrate differences between biosensor recruitment produced by chemically distinct opioid ligands in living cells. We then show that selective recruitment applies to GRK2, a biologically relevant GPCR regulator, through discrete interactions of GRK2 with receptors or with G protein beta-gamma subunits which are differentially promoted by agonists. GPCR opioid biosensor receptor kinase agonist bias TIRF Medicine R Science Q Biology (General) Damien Jullié verfasserin aut Joy Li verfasserin aut Soumen Chakraborty verfasserin aut Susruta Majumdar verfasserin aut Nevin A Lambert verfasserin aut Aashish Manglik verfasserin aut Mark von Zastrow verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 9(2020) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:9 year:2020 https://doi.org/10.7554/eLife.54208 kostenfrei https://doaj.org/article/8c895244c98b40adb73cdb12ae8fea95 kostenfrei https://elifesciences.org/articles/54208 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2020
allfieldsGer	10.7554/eLife.54208 doi (DE-627)DOAJ032295014 (DE-599)DOAJ8c895244c98b40adb73cdb12ae8fea95 DE-627 ger DE-627 rakwb eng QH301-705.5 Miriam Stoeber verfasserin aut Agonist-selective recruitment of engineered protein probes and of GRK2 by opioid receptors in living cells 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier G protein-coupled receptors (GPCRs) signal through allostery, and it is increasingly clear that chemically distinct agonists can produce different receptor-based effects. It has been proposed that agonists selectively promote receptors to recruit one cellular interacting partner over another, introducing allosteric ‘bias’ into the signaling system. However, the underlying hypothesis - that different agonists drive GPCRs to engage different cytoplasmic proteins in living cells - remains untested due to the complexity of readouts through which receptor-proximal interactions are typically inferred. We describe a cell-based assay to overcome this challenge, based on GPCR-interacting biosensors that are disconnected from endogenous transduction mechanisms. Focusing on opioid receptors, we directly demonstrate differences between biosensor recruitment produced by chemically distinct opioid ligands in living cells. We then show that selective recruitment applies to GRK2, a biologically relevant GPCR regulator, through discrete interactions of GRK2 with receptors or with G protein beta-gamma subunits which are differentially promoted by agonists. GPCR opioid biosensor receptor kinase agonist bias TIRF Medicine R Science Q Biology (General) Damien Jullié verfasserin aut Joy Li verfasserin aut Soumen Chakraborty verfasserin aut Susruta Majumdar verfasserin aut Nevin A Lambert verfasserin aut Aashish Manglik verfasserin aut Mark von Zastrow verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 9(2020) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:9 year:2020 https://doi.org/10.7554/eLife.54208 kostenfrei https://doaj.org/article/8c895244c98b40adb73cdb12ae8fea95 kostenfrei https://elifesciences.org/articles/54208 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2020
allfieldsSound	10.7554/eLife.54208 doi (DE-627)DOAJ032295014 (DE-599)DOAJ8c895244c98b40adb73cdb12ae8fea95 DE-627 ger DE-627 rakwb eng QH301-705.5 Miriam Stoeber verfasserin aut Agonist-selective recruitment of engineered protein probes and of GRK2 by opioid receptors in living cells 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier G protein-coupled receptors (GPCRs) signal through allostery, and it is increasingly clear that chemically distinct agonists can produce different receptor-based effects. It has been proposed that agonists selectively promote receptors to recruit one cellular interacting partner over another, introducing allosteric ‘bias’ into the signaling system. However, the underlying hypothesis - that different agonists drive GPCRs to engage different cytoplasmic proteins in living cells - remains untested due to the complexity of readouts through which receptor-proximal interactions are typically inferred. We describe a cell-based assay to overcome this challenge, based on GPCR-interacting biosensors that are disconnected from endogenous transduction mechanisms. Focusing on opioid receptors, we directly demonstrate differences between biosensor recruitment produced by chemically distinct opioid ligands in living cells. We then show that selective recruitment applies to GRK2, a biologically relevant GPCR regulator, through discrete interactions of GRK2 with receptors or with G protein beta-gamma subunits which are differentially promoted by agonists. GPCR opioid biosensor receptor kinase agonist bias TIRF Medicine R Science Q Biology (General) Damien Jullié verfasserin aut Joy Li verfasserin aut Soumen Chakraborty verfasserin aut Susruta Majumdar verfasserin aut Nevin A Lambert verfasserin aut Aashish Manglik verfasserin aut Mark von Zastrow verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 9(2020) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:9 year:2020 https://doi.org/10.7554/eLife.54208 kostenfrei https://doaj.org/article/8c895244c98b40adb73cdb12ae8fea95 kostenfrei https://elifesciences.org/articles/54208 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2020
language	English
source	In eLife 9(2020) volume:9 year:2020
sourceStr	In eLife 9(2020) volume:9 year:2020
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	GPCR opioid biosensor receptor kinase agonist bias TIRF Medicine R Science Q Biology (General)
isfreeaccess_bool	true
container_title	eLife
authorswithroles_txt_mv	Miriam Stoeber @@aut@@ Damien Jullié @@aut@@ Joy Li @@aut@@ Soumen Chakraborty @@aut@@ Susruta Majumdar @@aut@@ Nevin A Lambert @@aut@@ Aashish Manglik @@aut@@ Mark von Zastrow @@aut@@
publishDateDaySort_date	2020-01-01T00:00:00Z
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callnumber-first	Q - Science
author	Miriam Stoeber
spellingShingle	Miriam Stoeber misc QH301-705.5 misc GPCR misc opioid misc biosensor misc receptor kinase misc agonist bias misc TIRF misc Medicine misc R misc Science misc Q misc Biology (General) Agonist-selective recruitment of engineered protein probes and of GRK2 by opioid receptors in living cells
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topic_title	QH301-705.5 Agonist-selective recruitment of engineered protein probes and of GRK2 by opioid receptors in living cells GPCR opioid biosensor receptor kinase agonist bias TIRF
topic	misc QH301-705.5 misc GPCR misc opioid misc biosensor misc receptor kinase misc agonist bias misc TIRF misc Medicine misc R misc Science misc Q misc Biology (General)
topic_unstemmed	misc QH301-705.5 misc GPCR misc opioid misc biosensor misc receptor kinase misc agonist bias misc TIRF misc Medicine misc R misc Science misc Q misc Biology (General)
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title	Agonist-selective recruitment of engineered protein probes and of GRK2 by opioid receptors in living cells
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title_full	Agonist-selective recruitment of engineered protein probes and of GRK2 by opioid receptors in living cells
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title_sort	agonist-selective recruitment of engineered protein probes and of grk2 by opioid receptors in living cells
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title_auth	Agonist-selective recruitment of engineered protein probes and of GRK2 by opioid receptors in living cells
abstract	G protein-coupled receptors (GPCRs) signal through allostery, and it is increasingly clear that chemically distinct agonists can produce different receptor-based effects. It has been proposed that agonists selectively promote receptors to recruit one cellular interacting partner over another, introducing allosteric ‘bias’ into the signaling system. However, the underlying hypothesis - that different agonists drive GPCRs to engage different cytoplasmic proteins in living cells - remains untested due to the complexity of readouts through which receptor-proximal interactions are typically inferred. We describe a cell-based assay to overcome this challenge, based on GPCR-interacting biosensors that are disconnected from endogenous transduction mechanisms. Focusing on opioid receptors, we directly demonstrate differences between biosensor recruitment produced by chemically distinct opioid ligands in living cells. We then show that selective recruitment applies to GRK2, a biologically relevant GPCR regulator, through discrete interactions of GRK2 with receptors or with G protein beta-gamma subunits which are differentially promoted by agonists.
abstractGer	G protein-coupled receptors (GPCRs) signal through allostery, and it is increasingly clear that chemically distinct agonists can produce different receptor-based effects. It has been proposed that agonists selectively promote receptors to recruit one cellular interacting partner over another, introducing allosteric ‘bias’ into the signaling system. However, the underlying hypothesis - that different agonists drive GPCRs to engage different cytoplasmic proteins in living cells - remains untested due to the complexity of readouts through which receptor-proximal interactions are typically inferred. We describe a cell-based assay to overcome this challenge, based on GPCR-interacting biosensors that are disconnected from endogenous transduction mechanisms. Focusing on opioid receptors, we directly demonstrate differences between biosensor recruitment produced by chemically distinct opioid ligands in living cells. We then show that selective recruitment applies to GRK2, a biologically relevant GPCR regulator, through discrete interactions of GRK2 with receptors or with G protein beta-gamma subunits which are differentially promoted by agonists.
abstract_unstemmed	G protein-coupled receptors (GPCRs) signal through allostery, and it is increasingly clear that chemically distinct agonists can produce different receptor-based effects. It has been proposed that agonists selectively promote receptors to recruit one cellular interacting partner over another, introducing allosteric ‘bias’ into the signaling system. However, the underlying hypothesis - that different agonists drive GPCRs to engage different cytoplasmic proteins in living cells - remains untested due to the complexity of readouts through which receptor-proximal interactions are typically inferred. We describe a cell-based assay to overcome this challenge, based on GPCR-interacting biosensors that are disconnected from endogenous transduction mechanisms. Focusing on opioid receptors, we directly demonstrate differences between biosensor recruitment produced by chemically distinct opioid ligands in living cells. We then show that selective recruitment applies to GRK2, a biologically relevant GPCR regulator, through discrete interactions of GRK2 with receptors or with G protein beta-gamma subunits which are differentially promoted by agonists.
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title_short	Agonist-selective recruitment of engineered protein probes and of GRK2 by opioid receptors in living cells
url	https://doi.org/10.7554/eLife.54208 https://doaj.org/article/8c895244c98b40adb73cdb12ae8fea95 https://elifesciences.org/articles/54208 https://doaj.org/toc/2050-084X
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Agonist-selective recruitment of engineered protein probes and of GRK2 by opioid receptors in living cells

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