Structural insights into the lipid and ligand regulation of serotonin receptors

Serotonin, or 5-hydroxytryptamine (5-HT), is an important neurotransmitter 1 , 2 that activates the largest subtype family of G-protein-coupled receptors 3 . Drugs that target 5-HT 1A , 5-HT 1D , 5-HT 1E and other 5-HT receptors are used to treat numerous disorders 4 . 5-HT receptors have high level...

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Published in:Nature (London) Vol. 592; no. 7854; pp. 469 - 473
Main Authors: Xu, Peiyu, Huang, Sijie, Zhang, Huibing, Mao, Chunyou, Zhou, X. Edward, Cheng, Xi, Simon, Icaro A., Shen, Dan-Dan, Yen, Hsin-Yung, Robinson, Carol V., Harpsøe, Kasper, Svensson, Bo, Guo, Jia, Jiang, Hualiang, Gloriam, David E., Melcher, Karsten, Jiang, Yi, Zhang, Yan, Xu, H. Eric
Format: Journal Article
Language:English
Published: London Nature Publishing Group UK 15.04.2021
Nature Publishing Group
Subjects:
101/1
101/28
631/154/436/2387
631/45/776
631/535/1258/1259
82
82/80
82/83
Agonists
Antipsychotic drugs
Antipsychotics
Apoproteins - chemistry
Apoproteins - metabolism
Apoproteins - ultrastructure
Aripiprazole
Aripiprazole - metabolism
Aripiprazole - pharmacology
Binding
Binding Sites
Biological control systems
Cholesterol
Cholesterol - pharmacology
Coupling (molecular)
Cryoelectron Microscopy
G protein-coupled receptors
Heterotrimeric GTP-Binding Proteins - chemistry
Heterotrimeric GTP-Binding Proteins - metabolism
Heterotrimeric GTP-Binding Proteins - ultrastructure
Humanities and Social Sciences
Humans
Ligands
Ligands (Biochemistry)
Lipids
Models, Molecular
multidisciplinary
Phenols
Phosphatidylinositol 4-phosphate
Phosphatidylinositol Phosphates - chemistry
Phosphatidylinositol Phosphates - metabolism
Phosphatidylinositol Phosphates - pharmacology
Phospholipids
Physiological aspects
Physiological research
Proteins
Receptor, Serotonin, 5-HT1A - chemistry
Receptor, Serotonin, 5-HT1A - metabolism
Receptor, Serotonin, 5-HT1A - ultrastructure
Receptors
Receptors, Serotonin, 5-HT1 - chemistry
Receptors, Serotonin, 5-HT1 - metabolism
Receptors, Serotonin, 5-HT1 - ultrastructure
Science
Science (multidisciplinary)
Serotonin
Serotonin 5-HT1 Receptor Agonists - chemistry
Serotonin 5-HT1 Receptor Agonists - metabolism
Serotonin 5-HT1 Receptor Agonists - pharmacology
Serotonin receptors
Serotonin S1 receptors
Structure
Water - chemistry
China
ISSN:0028-0836, 1476-4687, 1476-4687
Online Access:Get full text
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Abstract Serotonin, or 5-hydroxytryptamine (5-HT), is an important neurotransmitter 1 , 2 that activates the largest subtype family of G-protein-coupled receptors 3 . Drugs that target 5-HT 1A , 5-HT 1D , 5-HT 1E and other 5-HT receptors are used to treat numerous disorders 4 . 5-HT receptors have high levels of basal activity and are subject to regulation by lipids, but the structural basis for the lipid regulation and basal activation of these receptors and the pan-agonism of 5-HT remains unclear. Here we report five structures of 5-HT receptor–G-protein complexes: 5-HT 1A in the apo state, bound to 5-HT or bound to the antipsychotic drug aripiprazole; 5-HT 1D bound to 5-HT; and 5-HT 1E in complex with a 5-HT 1E - and 5-HT 1F -selective agonist, BRL-54443. Notably, the phospholipid phosphatidylinositol 4-phosphate is present at the G-protein–5-HT 1A interface, and is able to increase 5-HT 1A -mediated G-protein activity. The receptor transmembrane domain is surrounded by cholesterol molecules—particularly in the case of 5-HT 1A , in which cholesterol molecules are directly involved in shaping the ligand-binding pocket that determines the specificity for aripiprazol. Within the ligand-binding pocket of apo-5-HT 1A are structured water molecules that mimic 5-HT to activate the receptor. Together, our results address a long-standing question of how lipids and water molecules regulate G-protein-coupled receptors, reveal how 5-HT acts as a pan-agonist, and identify the determinants of drug recognition in 5-HT receptors. Cryo-electron microscopy structures of three different serotonin receptors in complex with serotonin and other agonists provide insights into the role of lipids in regulating these receptors and the structural basis of ligand recognition.
AbstractList Serotonin, or 5-hydroxytryptamine (5-HT), is an important neurotransmitter.sup.1,2 that activates the largest subtype family of G-protein-coupled receptors.sup.3. Drugs that target 5-HT.sub.1A, 5-HT.sub.1D, 5-HT.sub.1E and other 5-HT receptors are used to treat numerous disorders.sup.4. 5-HT receptors have high levels of basal activity and are subject to regulation by lipids, but the structural basis for the lipid regulation and basal activation of these receptors and the pan-agonism of 5-HT remains unclear. Here we report five structures of 5-HT receptor-G-protein complexes: 5-HT.sub.1A in the apo state, bound to 5-HT or bound to the antipsychotic drug aripiprazole; 5-HT.sub.1D bound to 5-HT; and 5-HT.sub.1E in complex with a 5-HT.sub.1E- and 5-HT.sub.1F-selective agonist, BRL-54443. Notably, the phospholipid phosphatidylinositol 4-phosphate is present at the G-protein-5-HT.sub.1A interface, and is able to increase 5-HT.sub.1A-mediated G-protein activity. The receptor transmembrane domain is surrounded by cholesterol molecules--particularly in the case of 5-HT.sub.1A, in which cholesterol molecules are directly involved in shaping the ligand-binding pocket that determines the specificity for aripiprazol. Within the ligand-binding pocket of apo-5-HT.sub.1A are structured water molecules that mimic 5-HT to activate the receptor. Together, our results address a long-standing question of how lipids and water molecules regulate G-protein-coupled receptors, reveal how 5-HT acts as a pan-agonist, and identify the determinants of drug recognition in 5-HT receptors.
Serotonin, or 5-hydroxytryptamine (5-HT), is an important neurotransmitter that activates the largest subtype family of G-protein-coupled receptors . Drugs that target 5-HT , 5-HT , 5-HT and other 5-HT receptors are used to treat numerous disorders . 5-HT receptors have high levels of basal activity and are subject to regulation by lipids, but the structural basis for the lipid regulation and basal activation of these receptors and the pan-agonism of 5-HT remains unclear. Here we report five structures of 5-HT receptor-G-protein complexes: 5-HT in the apo state, bound to 5-HT or bound to the antipsychotic drug aripiprazole; 5-HT bound to 5-HT; and 5-HT in complex with a 5-HT - and 5-HT -selective agonist, BRL-54443. Notably, the phospholipid phosphatidylinositol 4-phosphate is present at the G-protein-5-HT interface, and is able to increase 5-HT -mediated G-protein activity. The receptor transmembrane domain is surrounded by cholesterol molecules-particularly in the case of 5-HT , in which cholesterol molecules are directly involved in shaping the ligand-binding pocket that determines the specificity for aripiprazol. Within the ligand-binding pocket of apo-5-HT are structured water molecules that mimic 5-HT to activate the receptor. Together, our results address a long-standing question of how lipids and water molecules regulate G-protein-coupled receptors, reveal how 5-HT acts as a pan-agonist, and identify the determinants of drug recognition in 5-HT receptors.
Serotonin, or 5-hydroxytryptamine (5-HT), is an important neurotransmitter 1 , 2 that activates the largest subtype family of G-protein-coupled receptors 3 . Drugs that target 5-HT 1A , 5-HT 1D , 5-HT 1E and other 5-HT receptors are used to treat numerous disorders 4 . 5-HT receptors have high levels of basal activity and are subject to regulation by lipids, but the structural basis for the lipid regulation and basal activation of these receptors and the pan-agonism of 5-HT remains unclear. Here we report five structures of 5-HT receptor–G-protein complexes: 5-HT 1A in the apo state, bound to 5-HT or bound to the antipsychotic drug aripiprazole; 5-HT 1D bound to 5-HT; and 5-HT 1E in complex with a 5-HT 1E - and 5-HT 1F -selective agonist, BRL-54443. Notably, the phospholipid phosphatidylinositol 4-phosphate is present at the G-protein–5-HT 1A interface, and is able to increase 5-HT 1A -mediated G-protein activity. The receptor transmembrane domain is surrounded by cholesterol molecules—particularly in the case of 5-HT 1A , in which cholesterol molecules are directly involved in shaping the ligand-binding pocket that determines the specificity for aripiprazol. Within the ligand-binding pocket of apo-5-HT 1A are structured water molecules that mimic 5-HT to activate the receptor. Together, our results address a long-standing question of how lipids and water molecules regulate G-protein-coupled receptors, reveal how 5-HT acts as a pan-agonist, and identify the determinants of drug recognition in 5-HT receptors. Cryo-electron microscopy structures of three different serotonin receptors in complex with serotonin and other agonists provide insights into the role of lipids in regulating these receptors and the structural basis of ligand recognition.
Serotonin, or 5-hydroxytryptamine (5-HT), is an important neurotransmitter1,2 that activates the largest subtype family of G-protein-coupled receptors3. Drugs that target 5-HT1A, 5-HT1D, 5-HT1E and other 5-HT receptors are used to treat numerous disorders4. 5-HT receptors have high levels of basal activity and are subject to regulation by lipids, but the structural basis for the lipid regulation and basal activation of these receptors and the pan-agonism of 5-HT remains unclear. Here we report five structures of 5-HT receptor-G-protein complexes: 5-HT1A in the apo state, bound to 5-HT or bound to the antipsychotic drug aripiprazole; 5-HT1D bound to 5-HT; and 5-HT1E in complex with a 5-HT1E- and 5-HT1F-selective agonist, BRL-54443. Notably, the phospholipid phosphatidylinositol 4-phosphate is present at the G-protein-5-HT1A interface, and is able to increase 5-HT1A-mediated G-protein activity. The receptor transmembrane domain is surrounded by cholesterol molecules-particularly in the case of 5-HT1A, in which cholesterol molecules are directly involved in shaping the ligand-binding pocket that determines the specificity for aripiprazol. Within the ligand-binding pocket of apo-5-HT1A are structured water molecules that mimic 5-HT to activate the receptor. Together, our results address a long-standing question of how lipids and water molecules regulate G-protein-coupled receptors, reveal how 5-HT acts as a pan-agonist, and identify the determinants of drug recognition in 5-HT receptors.Serotonin, or 5-hydroxytryptamine (5-HT), is an important neurotransmitter1,2 that activates the largest subtype family of G-protein-coupled receptors3. Drugs that target 5-HT1A, 5-HT1D, 5-HT1E and other 5-HT receptors are used to treat numerous disorders4. 5-HT receptors have high levels of basal activity and are subject to regulation by lipids, but the structural basis for the lipid regulation and basal activation of these receptors and the pan-agonism of 5-HT remains unclear. Here we report five structures of 5-HT receptor-G-protein complexes: 5-HT1A in the apo state, bound to 5-HT or bound to the antipsychotic drug aripiprazole; 5-HT1D bound to 5-HT; and 5-HT1E in complex with a 5-HT1E- and 5-HT1F-selective agonist, BRL-54443. Notably, the phospholipid phosphatidylinositol 4-phosphate is present at the G-protein-5-HT1A interface, and is able to increase 5-HT1A-mediated G-protein activity. The receptor transmembrane domain is surrounded by cholesterol molecules-particularly in the case of 5-HT1A, in which cholesterol molecules are directly involved in shaping the ligand-binding pocket that determines the specificity for aripiprazol. Within the ligand-binding pocket of apo-5-HT1A are structured water molecules that mimic 5-HT to activate the receptor. Together, our results address a long-standing question of how lipids and water molecules regulate G-protein-coupled receptors, reveal how 5-HT acts as a pan-agonist, and identify the determinants of drug recognition in 5-HT receptors.
Serotonin, or 5-hydroxytryptamine (5-HT), is an important neurotransmitter1,2 that activates the largest subtype family of G-protein-coupled receptors3. Drugs that target 5-HT1A, 5-HT1D, 5-HT1e and other 5-HT receptors are used to treat numerous disorders4. 5-HT receptors have high levels of basal activity and are subject to regulation by lipids, but the structural basis for the lipid regulation and basal activation of these receptors and the pan-agonism of 5-HT remains unclear. Here we report five structures of 5-HT receptor-G-protein complexes: 5-HT1A in the apo state, bound to 5-HT or bound to the antipsychotic drug aripiprazole; 5-HT1D bound to 5-HT; and 5-HT1e in complex with a 5-HT1E- and 5-HT1F-selective agonist, BRL-54443. Notably, the phospholipid phosphatidylinositol 4-phosphate is present at the G-protein-5-HT1A interface, and is able to increase 5-HT1A-mediated G-protein activity. The receptor transmembrane domain is surrounded by cholesterol molecules-particularly in the case of 5-HT1A, in which cholesterol molecules are directly involved in shaping the ligand-binding pocket that determines the specificity for aripiprazol. Within the ligand-binding pocket of apo-5-HT1A are structured water molecules that mimic 5-HT to activate the receptor. Together, our results address a long-standing question of how lipids and water molecules regulate G-protein-coupled receptors, reveal how 5-HT acts as a pan-agonist, and identify the determinants of drug recognition in 5-HT receptors.
Serotonin, or 5-hydroxytryptamine (5-HT), is an important neurotransmitter.sup.1,2 that activates the largest subtype family of G-protein-coupled receptors.sup.3. Drugs that target 5-HT.sub.1A, 5-HT.sub.1D, 5-HT.sub.1E and other 5-HT receptors are used to treat numerous disorders.sup.4. 5-HT receptors have high levels of basal activity and are subject to regulation by lipids, but the structural basis for the lipid regulation and basal activation of these receptors and the pan-agonism of 5-HT remains unclear. Here we report five structures of 5-HT receptor-G-protein complexes: 5-HT.sub.1A in the apo state, bound to 5-HT or bound to the antipsychotic drug aripiprazole; 5-HT.sub.1D bound to 5-HT; and 5-HT.sub.1E in complex with a 5-HT.sub.1E- and 5-HT.sub.1F-selective agonist, BRL-54443. Notably, the phospholipid phosphatidylinositol 4-phosphate is present at the G-protein-5-HT.sub.1A interface, and is able to increase 5-HT.sub.1A-mediated G-protein activity. The receptor transmembrane domain is surrounded by cholesterol molecules--particularly in the case of 5-HT.sub.1A, in which cholesterol molecules are directly involved in shaping the ligand-binding pocket that determines the specificity for aripiprazol. Within the ligand-binding pocket of apo-5-HT.sub.1A are structured water molecules that mimic 5-HT to activate the receptor. Together, our results address a long-standing question of how lipids and water molecules regulate G-protein-coupled receptors, reveal how 5-HT acts as a pan-agonist, and identify the determinants of drug recognition in 5-HT receptors. Cryo-electron microscopy structures of three different serotonin receptors in complex with serotonin and other agonists provide insights into the role of lipids in regulating these receptors and the structural basis of ligand recognition.
Audience Academic
Author Zhang, Huibing
Mao, Chunyou
Zhou, X. Edward
Simon, Icaro A.
Harpsøe, Kasper
Svensson, Bo
Melcher, Karsten
Shen, Dan-Dan
Xu, H. Eric
Jiang, Yi
Xu, Peiyu
Huang, Sijie
Yen, Hsin-Yung
Cheng, Xi
Gloriam, David E.
Robinson, Carol V.
Zhang, Yan
Guo, Jia
Jiang, Hualiang
Author_xml – sequence: 1
  givenname: Peiyu
  orcidid: 0000-0003-3590-4037
  surname: Xu
  fullname: Xu, Peiyu
  organization: Department of Biophysics and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, University of Chinese Academy of Sciences
– sequence: 2
  givenname: Sijie
  orcidid: 0000-0001-5653-0260
  surname: Huang
  fullname: Huang, Sijie
  organization: CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, University of Chinese Academy of Sciences, School of Life Science and Technology, ShanghaiTech University
– sequence: 3
  givenname: Huibing
  orcidid: 0000-0003-3025-0185
  surname: Zhang
  fullname: Zhang, Huibing
  organization: Department of Biophysics and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Liangzhu Laboratory, Zhejiang University Medical Center, MOE Frontier Science Center for Brain Research and Brain-Machine Integration, Zhejiang University School of Medicine, Zheijang Provincial Key Laboratory of Immunity and Inflammatory Diseases
– sequence: 4
  givenname: Chunyou
  orcidid: 0000-0001-5349-8592
  surname: Mao
  fullname: Mao, Chunyou
  organization: Department of Biophysics and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Liangzhu Laboratory, Zhejiang University Medical Center, MOE Frontier Science Center for Brain Research and Brain-Machine Integration, Zhejiang University School of Medicine, Zheijang Provincial Key Laboratory of Immunity and Inflammatory Diseases
– sequence: 5
  givenname: X. Edward
  surname: Zhou
  fullname: Zhou, X. Edward
  organization: Department of Structural Biology, Van Andel Institute
– sequence: 6
  givenname: Xi
  orcidid: 0000-0003-3735-645X
  surname: Cheng
  fullname: Cheng, Xi
  organization: State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences
– sequence: 7
  givenname: Icaro A.
  orcidid: 0000-0003-4550-4248
  surname: Simon
  fullname: Simon, Icaro A.
  organization: Department of Drug Design and Pharmacology, University of Copenhagen, SARomics Biostructures AB, Medicon Village
– sequence: 8
  givenname: Dan-Dan
  orcidid: 0000-0001-8757-4602
  surname: Shen
  fullname: Shen, Dan-Dan
  organization: Department of Biophysics and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Liangzhu Laboratory, Zhejiang University Medical Center, MOE Frontier Science Center for Brain Research and Brain-Machine Integration, Zhejiang University School of Medicine, Zheijang Provincial Key Laboratory of Immunity and Inflammatory Diseases
– sequence: 9
  givenname: Hsin-Yung
  surname: Yen
  fullname: Yen, Hsin-Yung
  organization: Physical and Theoretical Chemistry Laboratory, University of Oxford
– sequence: 10
  givenname: Carol V.
  orcidid: 0000-0001-7829-5505
  surname: Robinson
  fullname: Robinson, Carol V.
  organization: Physical and Theoretical Chemistry Laboratory, University of Oxford
– sequence: 11
  givenname: Kasper
  orcidid: 0000-0002-9326-9644
  surname: Harpsøe
  fullname: Harpsøe, Kasper
  organization: Department of Drug Design and Pharmacology, University of Copenhagen
– sequence: 12
  givenname: Bo
  surname: Svensson
  fullname: Svensson, Bo
  organization: SARomics Biostructures AB, Medicon Village
– sequence: 13
  givenname: Jia
  surname: Guo
  fullname: Guo, Jia
  organization: CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, University of Chinese Academy of Sciences
– sequence: 14
  givenname: Hualiang
  orcidid: 0000-0003-0656-6315
  surname: Jiang
  fullname: Jiang, Hualiang
  organization: University of Chinese Academy of Sciences, School of Life Science and Technology, ShanghaiTech University, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences
– sequence: 15
  givenname: David E.
  orcidid: 0000-0002-4299-7561
  surname: Gloriam
  fullname: Gloriam, David E.
  organization: Department of Drug Design and Pharmacology, University of Copenhagen
– sequence: 16
  givenname: Karsten
  orcidid: 0000-0002-9125-4027
  surname: Melcher
  fullname: Melcher, Karsten
  organization: Department of Structural Biology, Van Andel Institute
– sequence: 17
  givenname: Yi
  orcidid: 0000-0002-0723-1413
  surname: Jiang
  fullname: Jiang, Yi
  email: yijiang@simm.ac.cn
  organization: CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, University of Chinese Academy of Sciences
– sequence: 18
  givenname: Yan
  orcidid: 0000-0003-2189-0244
  surname: Zhang
  fullname: Zhang, Yan
  email: zhang_yan@zju.edu.cn
  organization: Department of Biophysics and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Liangzhu Laboratory, Zhejiang University Medical Center, MOE Frontier Science Center for Brain Research and Brain-Machine Integration, Zhejiang University School of Medicine, Zheijang Provincial Key Laboratory of Immunity and Inflammatory Diseases
– sequence: 19
  givenname: H. Eric
  orcidid: 0000-0002-6829-8144
  surname: Xu
  fullname: Xu, H. Eric
  email: eric.xu@simm.ac.cn
  organization: CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, University of Chinese Academy of Sciences, School of Life Science and Technology, ShanghaiTech University
BackLink https://www.ncbi.nlm.nih.gov/pubmed/33762731$$D View this record in MEDLINE/PubMed
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References Hannon, Hoyer (CR3) 2008; 195
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Snippet Serotonin, or 5-hydroxytryptamine (5-HT), is an important neurotransmitter 1 , 2 that activates the largest subtype family of G-protein-coupled receptors 3 ....
Serotonin, or 5-hydroxytryptamine (5-HT), is an important neurotransmitter that activates the largest subtype family of G-protein-coupled receptors . Drugs...
Serotonin, or 5-hydroxytryptamine (5-HT), is an important neurotransmitter.sup.1,2 that activates the largest subtype family of G-protein-coupled...
Serotonin, or 5-hydroxytryptamine (5-HT), is an important neurotransmitter1,2 that activates the largest subtype family of G-protein-coupled receptors3. Drugs...
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SubjectTerms 101/1
101/28
631/154/436/2387
631/45/776
631/535/1258/1259
82
82/80
82/83
Agonists
Antipsychotic drugs
Antipsychotics
Apoproteins - chemistry
Apoproteins - metabolism
Apoproteins - ultrastructure
Aripiprazole
Aripiprazole - metabolism
Aripiprazole - pharmacology
Binding
Binding Sites
Biological control systems
Cholesterol
Cholesterol - pharmacology
Coupling (molecular)
Cryoelectron Microscopy
G protein-coupled receptors
Heterotrimeric GTP-Binding Proteins - chemistry
Heterotrimeric GTP-Binding Proteins - metabolism
Heterotrimeric GTP-Binding Proteins - ultrastructure
Humanities and Social Sciences
Humans
Ligands
Ligands (Biochemistry)
Lipids
Models, Molecular
multidisciplinary
Phenols
Phosphatidylinositol 4-phosphate
Phosphatidylinositol Phosphates - chemistry
Phosphatidylinositol Phosphates - metabolism
Phosphatidylinositol Phosphates - pharmacology
Phospholipids
Physiological aspects
Physiological research
Proteins
Receptor, Serotonin, 5-HT1A - chemistry
Receptor, Serotonin, 5-HT1A - metabolism
Receptor, Serotonin, 5-HT1A - ultrastructure
Receptors
Receptors, Serotonin, 5-HT1 - chemistry
Receptors, Serotonin, 5-HT1 - metabolism
Receptors, Serotonin, 5-HT1 - ultrastructure
Science
Science (multidisciplinary)
Serotonin
Serotonin 5-HT1 Receptor Agonists - chemistry
Serotonin 5-HT1 Receptor Agonists - metabolism
Serotonin 5-HT1 Receptor Agonists - pharmacology
Serotonin receptors
Serotonin S1 receptors
Structure
Water - chemistry
Title Structural insights into the lipid and ligand regulation of serotonin receptors
URI https://link.springer.com/article/10.1038/s41586-021-03376-8
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