Visualization of arrestin recruitment by a G-protein-coupled receptor
Single-particle electron microscopy and hydrogen–deuterium exchange mass spectrometry are used to characterize the structure and dynamics of a G-protein-coupled receptor–arrestin complex. An arrestin–GPCR complex structure Much has been learned about the structure of G-protein-coupled receptors (GCP...
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| Published in | Nature (London) Vol. 512; no. 7513; pp. 218 - 222 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
14.08.2014
Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Single-particle electron microscopy and hydrogen–deuterium exchange mass spectrometry are used to characterize the structure and dynamics of a G-protein-coupled receptor–arrestin complex.
An arrestin–GPCR complex structure
Much has been learned about the structure of G-protein-coupled receptors (GCPRs) over the past seven years, but we still don't know what an activated GPCR looks like when it is bound to a β-arrestin. (Arrestins are cellular mediators with a broad range of functions, many of them involving GPCRs.) In this study the authors use single-particle electron microscopy and hydrogen–deuterium exchange mass spectrometry to characterize the structure and dynamics of a GPCR–arrestin complex. Their data support a 'biphasic' mechanism, in which the arrestin initially interacts with the phosphorylated carboxy terminus of the GPCR before re-arranging to more fully engage the membrane protein in a signalling-competent conformation.
G-protein-coupled receptors (GPCRs) are critically regulated by β-arrestins, which not only desensitize G-protein signalling but also initiate a G-protein-independent wave of signalling
1
,
2
,
3
,
4
,
5
. A recent surge of structural data on a number of GPCRs, including the β
2
adrenergic receptor (β
2
AR)–G-protein complex, has provided novel insights into the structural basis of receptor activation
6
,
7
,
8
,
9
,
10
,
11
. However, complementary information has been lacking on the recruitment of β-arrestins to activated GPCRs, primarily owing to challenges in obtaining stable receptor–β-arrestin complexes for structural studies. Here we devised a strategy for forming and purifying a functional human β
2
AR–β-arrestin-1 complex that allowed us to visualize its architecture by single-particle negative-stain electron microscopy and to characterize the interactions between β
2
AR and β-arrestin 1 using hydrogen–deuterium exchange mass spectrometry (HDX-MS) and chemical crosslinking. Electron microscopy two-dimensional averages and three-dimensional reconstructions reveal bimodal binding of β-arrestin 1 to the β
2
AR, involving two separate sets of interactions, one with the phosphorylated carboxy terminus of the receptor and the other with its seven-transmembrane core. Areas of reduced HDX together with identification of crosslinked residues suggest engagement of the finger loop of β-arrestin 1 with the seven-transmembrane core of the receptor. In contrast, focal areas of raised HDX levels indicate regions of increased dynamics in both the N and C domains of β-arrestin 1 when coupled to the β
2
AR. A molecular model of the β
2
AR–β-arrestin signalling complex was made by docking activated β-arrestin 1 and β
2
AR crystal structures into the electron microscopy map densities with constraints provided by HDX-MS and crosslinking, allowing us to obtain valuable insights into the overall architecture of a receptor–arrestin complex. The dynamic and structural information presented here provides a framework for better understanding the basis of GPCR regulation by arrestins. |
|---|---|
| AbstractList | G-protein-coupled receptors (GPCRs) are critically regulated by β-arrestins, which not only desensitize G-protein signalling but also initiate a G-protein-independent wave of signalling. A recent surge of structural data on a number of GPCRs, including the β2 adrenergic receptor (β2AR)-G-protein complex, has provided novel insights into the structural basis of receptor activation. However, complementary information has been lacking on the recruitment of β-arrestins to activated GPCRs, primarily owing to challenges in obtaining stable receptor-β-arrestin complexes for structural studies. Here we devised a strategy for forming and purifying a functional human β2AR-β-arrestin-1 complex that allowed us to visualize its architecture by single-particle negative-stain electron microscopy and to characterize the interactions between β2AR and β-arrestin 1 using hydrogen-deuterium exchange mass spectrometry (HDX-MS) and chemical crosslinking. Electron microscopy two-dimensional averages and three-dimensional reconstructions reveal bimodal binding of β-arrestin 1 to the β2AR, involving two separate sets of interactions, one with the phosphorylated carboxy terminus of the receptor and the other with its seven-transmembrane core. Areas of reduced HDX together with identification of crosslinked residues suggest engagement of the finger loop of β-arrestin 1 with the seven-transmembrane core of the receptor. In contrast, focal areas of raised HDX levels indicate regions of increased dynamics in both the N and C domains of β-arrestin 1 when coupled to the β2AR. A molecular model of the β2AR-β-arrestin signalling complex was made by docking activated β-arrestin 1 and β2AR crystal structures into the electron microscopy map densities with constraints provided by HDX-MS and crosslinking, allowing us to obtain valuable insights into the overall architecture of a receptor-arrestin complex. The dynamic and structural information presented here provides a framework for better understanding the basis of GPCR regulation by arrestins. Single-particle electron microscopy and hydrogen–deuterium exchange mass spectrometry are used to characterize the structure and dynamics of a G-protein-coupled receptor–arrestin complex. An arrestin–GPCR complex structure Much has been learned about the structure of G-protein-coupled receptors (GCPRs) over the past seven years, but we still don't know what an activated GPCR looks like when it is bound to a β-arrestin. (Arrestins are cellular mediators with a broad range of functions, many of them involving GPCRs.) In this study the authors use single-particle electron microscopy and hydrogen–deuterium exchange mass spectrometry to characterize the structure and dynamics of a GPCR–arrestin complex. Their data support a 'biphasic' mechanism, in which the arrestin initially interacts with the phosphorylated carboxy terminus of the GPCR before re-arranging to more fully engage the membrane protein in a signalling-competent conformation. G-protein-coupled receptors (GPCRs) are critically regulated by β-arrestins, which not only desensitize G-protein signalling but also initiate a G-protein-independent wave of signalling 1 , 2 , 3 , 4 , 5 . A recent surge of structural data on a number of GPCRs, including the β 2 adrenergic receptor (β 2 AR)–G-protein complex, has provided novel insights into the structural basis of receptor activation 6 , 7 , 8 , 9 , 10 , 11 . However, complementary information has been lacking on the recruitment of β-arrestins to activated GPCRs, primarily owing to challenges in obtaining stable receptor–β-arrestin complexes for structural studies. Here we devised a strategy for forming and purifying a functional human β 2 AR–β-arrestin-1 complex that allowed us to visualize its architecture by single-particle negative-stain electron microscopy and to characterize the interactions between β 2 AR and β-arrestin 1 using hydrogen–deuterium exchange mass spectrometry (HDX-MS) and chemical crosslinking. Electron microscopy two-dimensional averages and three-dimensional reconstructions reveal bimodal binding of β-arrestin 1 to the β 2 AR, involving two separate sets of interactions, one with the phosphorylated carboxy terminus of the receptor and the other with its seven-transmembrane core. Areas of reduced HDX together with identification of crosslinked residues suggest engagement of the finger loop of β-arrestin 1 with the seven-transmembrane core of the receptor. In contrast, focal areas of raised HDX levels indicate regions of increased dynamics in both the N and C domains of β-arrestin 1 when coupled to the β 2 AR. A molecular model of the β 2 AR–β-arrestin signalling complex was made by docking activated β-arrestin 1 and β 2 AR crystal structures into the electron microscopy map densities with constraints provided by HDX-MS and crosslinking, allowing us to obtain valuable insights into the overall architecture of a receptor–arrestin complex. The dynamic and structural information presented here provides a framework for better understanding the basis of GPCR regulation by arrestins. G-protein-coupled receptors (GPCRs) are critically regulated by β-arrestins, which not only desensitize G-protein signalling but also initiate a G-protein-independent wave of signalling. A recent surge of structural data on a number of GPCRs, including the β^sub 2^ adrenergic receptor (β^sub 2^AR)-G-protein complex, has provided novel insights into the structural basis of receptor activation. However, complementary information has been lacking on the recruitment of β-arrestins to activated GPCRs, primarily owing to challenges in obtaining stable receptor-β-arrestin complexes for structural studies. Here we devised a strategy for forming and purifying a functional human β^sub 2^AR-β-arrestin- 1 complex that allowed us to visualize its architecture by single-particle negative-stain electron microscopy and to characterize the interactions between β^sub 2^AR and β-arrestin 1 using hydrogen- deuterium exchange mass spectrometry (HDX-MS) and chemical crosslinking. Electron microscopy two-dimensional averages and three-dimensional reconstructions reveal bimodal binding of β-arrestin 1 to the β^sub 2^AR, involving two separate sets of interactions, one with the phosphorylated carboxy terminus of the receptor and the other with its seven-transmembrane core. Areas of reduced HDX together with identification of crosslinked residues suggest engagement of the finger loop of β-arrestin 1 with the seven-transmembrane core of the receptor. In contrast, focal areas of raised HDX levels indicate regions of increased dynamics in both the N and C domains of β-arrestin 1 when coupled to the β^sub 2^AR. A molecular model of the β^sub 2^AR-β-arrestin signalling complex was made by docking activated β-arrestin 1 and β^sub 2^AR crystal structures into the electron microscopy map densities with constraints provided by HDX-MS and crosslinking, allowing us to obtain valuable insights into the overall architecture of a receptor-arrestin complex. The dynamic and structural information presented here provides a framework for better understanding the basis of GPCR regulation by arrestins. G Protein Coupled Receptors (GPCRs) are critically regulated by β-arrestins (βarrs), which not only desensitize G protein signaling but also initiate a G protein independent wave of signaling 1 - 5 . A recent surge of structural data on a number of GPCRs, including the β 2 adrenergic receptor (β 2 AR)-G protein complex, has provided novel insights into the structural basis of receptor activation 6 - 11 . Lacking however has been complementary information on recruitment of βarrs to activated GPCRs primarily due to challenges in obtaining stable receptor-βarr complexes for structural studies. Here, we devised a strategy for forming and purifying a functional β 2 AR-βarr1 complex that allowed us to visualize its architecture by single particle negative stain electron microscopy (EM) and to characterize the interactions between β 2 AR and βarr1 using hydrogen-deuterium exchange mass spectrometry (HDXMS) and chemical cross-linking. EM 2D averages and 3D reconstructions reveal bimodal binding of βarr1 to the β 2 AR, involving two separate sets of interactions, one with the phosphorylated carboxy-terminus of the receptor and the other with its seven-transmembrane core. Areas of reduced HDX together with identification of cross-linked residues suggest engagement of the finger loop of βarr1 with the seven-transmembrane core of the receptor. In contrast, focal areas of increased HDX indicate regions of increased dynamics in both N and C domains of βarr1 when coupled to the β 2 AR. A molecular model of the β 2 AR-βarr signaling complex was made by docking activated βarr1 and β 2 AR crystal structures into the EM map densities with constraints provided by HDXMS and cross-linking, allowing us to obtain valuable insights into the overall architecture of a receptor-arrestin complex. The dynamic and structural information presented herein provides a framework for better understanding the basis of GPCR regulation by arrestins. G-protein-coupled receptors (GPCRs) are critically regulated by β- arrestins, which not only desensitize G-protein signalling but also initiate a G-protein-independent wave of signalling (1-5). A recent surge of structural data on a number of GPCRs, including the b2 adrenergic receptor ([β.sub.2]AR)-G-protein complex, has provided novel insights into the structural basis of receptor activation (6-11). However, complementary information has been lacking on the recruitment of β-arrestins to activated GPCRs, primarily owing to challenges in obtaining stable receptor-β-arrestin complexes for structural studies. Here we devised a strategy for forming and purifying a functional human [β.sub.2]AR-β- arrestin-1 complex that allowed us to visualize its architecture by single-particle negative-stain electron microscopy and to characterize the interactions between [β.sub.2]AR and β-arrestin 1 using hydrogendeuterium exchange mass spectrometry (HDX-MS) and chemical crosslinking. Electron microscopy two-dimensional averages and threedimensional reconstructions reveal bimodal binding of β-arrestin 1 to the [β.sub.2]AR, involving two separate sets of interactions, one with the phosphorylated carboxy terminus of the receptor and the other with its seven-transmembrane core. Areas of reduced HDX together with identification of crosslinked residues suggest engagement of the finger loop of β-arrestin 1 with the seven-transmembrane core of the receptor. In contrast, focal areas of raised HDX levels indicate regions of increased dynamics in both the N and C domains of barrestin 1 when coupled to the [β.sub.2]AR. A molecular model of the [β.sub.2]ARβ-arrestin signalling complex was made by docking activated β-arrestin 1 and [β.sub.2]AR crystal structures into the electron microscopy map densities with constraints provided by HDX-MS and crosslinking, allowing us to obtain valuable insights into the overall architecture of a receptor-arrestin complex. The dynamic and structural information presented here provides a framework for better understanding the basis of GPCR regulation by arrestins. |
| Audience | Academic |
| Author | Kossiakoff, Anthony A. Li, Sheng Oleskie, Austin N. Lefkowitz, Robert J. Dosey, Anne M. Kahsai, Alem W. Penczek, Pawel A. Klink, Bjoern U. Sidhu, Sachdev S. Gu, Ling-Ling Shan, Jin-Ming Choi, Minjung Kobilka, Brian K. Westfield, Gerwin H. Huang, Li-Yin Blanc, Adi Skiniotis, Georgios Liang, Cui-Rong Woods Jr, Virgil L. Hanna, Rachel Chen, Xin Xiao, Kunhong Tripathi-Shukla, Prachi Su, Min Yao, Xiao Jie Shukla, Arun K. Reis, Rosana I. Koide, Shohei Qian, Jiang |
| AuthorAffiliation | 9 Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA 1 Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710, USA 2 Life Sciences Institute and Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109, USA 5 Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, ON, Canada 6 Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois 60637, USA 3 Department of Chemistry, University of California at San Diego, La Jolla, CA 92093, USA 10 Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710, USA 7 Department of Biochemistry and Molecular Biology, The University of Texas Medical School at Houston, Houston, TX 77054, USA 8 Department of Molecular and Cellular Physiology, Stanford University School of Medicine, 279 Campus Drive, Stanford, California 94305, USA 4 School of Pharma |
| AuthorAffiliation_xml | – name: 6 Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois 60637, USA – name: 9 Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA – name: 1 Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710, USA – name: 8 Department of Molecular and Cellular Physiology, Stanford University School of Medicine, 279 Campus Drive, Stanford, California 94305, USA – name: 5 Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, ON, Canada – name: 3 Department of Chemistry, University of California at San Diego, La Jolla, CA 92093, USA – name: 2 Life Sciences Institute and Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109, USA – name: 4 School of Pharmaceutical & Life Sciences, Changzhou University, Changzhou, Jiangsu 213164, China – name: 7 Department of Biochemistry and Molecular Biology, The University of Texas Medical School at Houston, Houston, TX 77054, USA – name: 10 Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710, USA |
| Author_xml | – sequence: 1 givenname: Arun K. surname: Shukla fullname: Shukla, Arun K. organization: Department of Medicine, Duke University Medical Center, Present address: Department of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur 208016, India – sequence: 2 givenname: Gerwin H. surname: Westfield fullname: Westfield, Gerwin H. organization: Life Sciences Institute and Department of Biological Chemistry, University of Michigan Medical School – sequence: 3 givenname: Kunhong surname: Xiao fullname: Xiao, Kunhong organization: Department of Medicine, Duke University Medical Center – sequence: 4 givenname: Rosana I. surname: Reis fullname: Reis, Rosana I. organization: Department of Medicine, Duke University Medical Center – sequence: 5 givenname: Li-Yin surname: Huang fullname: Huang, Li-Yin organization: Department of Medicine, Duke University Medical Center – sequence: 6 givenname: Prachi surname: Tripathi-Shukla fullname: Tripathi-Shukla, Prachi organization: Department of Medicine, Duke University Medical Center – sequence: 7 givenname: Jiang surname: Qian fullname: Qian, Jiang organization: Department of Medicine, Duke University Medical Center – sequence: 8 givenname: Sheng surname: Li fullname: Li, Sheng organization: Department of Chemistry, University of California at San Diego – sequence: 9 givenname: Adi surname: Blanc fullname: Blanc, Adi organization: Department of Medicine, Duke University Medical Center – sequence: 10 givenname: Austin N. surname: Oleskie fullname: Oleskie, Austin N. organization: Life Sciences Institute and Department of Biological Chemistry, University of Michigan Medical School – sequence: 11 givenname: Anne M. surname: Dosey fullname: Dosey, Anne M. organization: Life Sciences Institute and Department of Biological Chemistry, University of Michigan Medical School – sequence: 12 givenname: Min surname: Su fullname: Su, Min organization: Life Sciences Institute and Department of Biological Chemistry, University of Michigan Medical School – sequence: 13 givenname: Cui-Rong surname: Liang fullname: Liang, Cui-Rong organization: School of Pharmaceutical & Life Sciences, Changzhou University, Changzhou, Jiangsu 213164, China – sequence: 14 givenname: Ling-Ling surname: Gu fullname: Gu, Ling-Ling organization: School of Pharmaceutical & Life Sciences, Changzhou University, Changzhou, Jiangsu 213164, China – sequence: 15 givenname: Jin-Ming surname: Shan fullname: Shan, Jin-Ming organization: School of Pharmaceutical & Life Sciences, Changzhou University, Changzhou, Jiangsu 213164, China – sequence: 16 givenname: Xin surname: Chen fullname: Chen, Xin organization: School of Pharmaceutical & Life Sciences, Changzhou University, Changzhou, Jiangsu 213164, China – sequence: 17 givenname: Rachel surname: Hanna fullname: Hanna, Rachel organization: Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 3E1, Canada – sequence: 18 givenname: Minjung surname: Choi fullname: Choi, Minjung organization: Department of Biochemistry, Duke University Medical Center – sequence: 19 givenname: Xiao Jie surname: Yao fullname: Yao, Xiao Jie organization: Department of Medicine, Duke University Medical Center – sequence: 20 givenname: Bjoern U. surname: Klink fullname: Klink, Bjoern U. organization: Department of Medicine, Duke University Medical Center – sequence: 21 givenname: Alem W. surname: Kahsai fullname: Kahsai, Alem W. organization: Department of Medicine, Duke University Medical Center – sequence: 22 givenname: Sachdev S. surname: Sidhu fullname: Sidhu, Sachdev S. organization: Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 3E1, Canada – sequence: 23 givenname: Shohei surname: Koide fullname: Koide, Shohei organization: Department of Biochemistry and Molecular Biology, University of Chicago – sequence: 24 givenname: Pawel A. surname: Penczek fullname: Penczek, Pawel A. organization: Department of Biochemistry and Molecular Biology, The University of Texas Medical School at Houston – sequence: 25 givenname: Anthony A. surname: Kossiakoff fullname: Kossiakoff, Anthony A. organization: Department of Biochemistry and Molecular Biology, University of Chicago – sequence: 26 givenname: Virgil L. surname: Woods Jr fullname: Woods Jr, Virgil L. organization: Department of Chemistry, University of California at San Diego – sequence: 27 givenname: Brian K. surname: Kobilka fullname: Kobilka, Brian K. email: kobilka@stanford.edu organization: Department of Molecular and Cellular Physiology, Stanford University School of Medicine, 279 Campus Drive – sequence: 28 givenname: Georgios surname: Skiniotis fullname: Skiniotis, Georgios email: skinioti@umich.edu organization: Life Sciences Institute and Department of Biological Chemistry, University of Michigan Medical School – sequence: 29 givenname: Robert J. surname: Lefkowitz fullname: Lefkowitz, Robert J. email: lefko001@receptor-biol.duke.edu organization: Department of Medicine, Duke University Medical Center, Department of Biochemistry, Duke University Medical Center, Howard Hughes Medical Institute, Duke University Medical Center |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/25043026$$D View this record in MEDLINE/PubMed |
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| Snippet | Single-particle electron microscopy and hydrogen–deuterium exchange mass spectrometry are used to characterize the structure and dynamics of a... G-protein-coupled receptors (GPCRs) are critically regulated by β-arrestins, which not only desensitize G-protein signalling but also initiate a... G-protein-coupled receptors (GPCRs) are critically regulated by β- arrestins, which not only desensitize G-protein signalling but also initiate a... G Protein Coupled Receptors (GPCRs) are critically regulated by β-arrestins (βarrs), which not only desensitize G protein signaling but also initiate a G... |
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| SubjectTerms | 631/535/1258 631/92/612/194 Animals Arrestins - chemistry Arrestins - metabolism beta-Arrestin 1 beta-Arrestins Chromatography Crosslinked polymers Crystals Deuterium Efficiency Electron microscopy G proteins GTP-Binding Proteins - chemistry GTP-Binding Proteins - metabolism Humanities and Social Sciences letter Ligands Mass spectrometry Models, Molecular multidisciplinary Protein Structure, Quaternary Proteins Receptors, Adrenergic, beta-2 - chemistry Receptors, Adrenergic, beta-2 - metabolism Receptors, G-Protein-Coupled - chemistry Receptors, G-Protein-Coupled - metabolism Science Sf9 Cells Signal transduction Structure |
| Title | Visualization of arrestin recruitment by a G-protein-coupled receptor |
| URI | https://link.springer.com/article/10.1038/nature13430 https://www.ncbi.nlm.nih.gov/pubmed/25043026 https://www.proquest.com/docview/1561134566 https://search.proquest.com/docview/1553703308 https://pubmed.ncbi.nlm.nih.gov/PMC4134437 |
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