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PtdIns(4,5)P2 stabilizes active states of GPCRs and enhances selectivity of G-protein coupling

Abstract:

G-protein-coupled receptors (GPCRs) are involved in many physiological processes and are therefore key drug targets1. Although detailed structural information is available for GPCRs, the effects of lipids on the receptors, and on downstream coupling of GPCRs to G proteins are largely unknown. Here we use native mass spectrometry to identify endogenous lipids bound to three class A GPCRs. We observed preferential binding of phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) over related lip...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41586-018-0325-6

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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Physical & Theoretical Chem
Role:
Author
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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Physical & Theoretical Chem
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Physical & Theoretical Chem
Role:
Author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Role:
Author
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Funding agency for:
Song, W
Grant:
Newton International Fellowship
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Funding agency for:
Robinson, C
Grant:
Investigator Award (104633/Z/14/Z)
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Funding agency for:
Sansom, M
Grant:
092970/Z/10/Z
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Publisher:
Springer Nature Publisher's website
Journal:
Nature Journal website
Volume:
559
Pages:
423–427
Publication date:
2018-07-11
Acceptance date:
2018-05-14
DOI:
ISSN:
1476-4687
Source identifiers:
891859
Pubs id:
pubs:891859
UUID:
uuid:022d4add-2d6f-43e8-901c-7330bf46d170
Local pid:
pubs:891859
Deposit date:
2018-07-31

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