The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Allosteric regulation of G protein–coupled receptor activity by phospholipids
Open accessAbstract
Lipids are emerging as key regulators of membrane protein structure and activity. Such effects can either be attributed to modification in bilayer properties (thickness, curvature and surface tension) or to binding of specific lipids to the protein surface. For G Protein-Coupled Receptors (GPCRs), the effect of phospholipids on receptor structure and activity remains poorly understood. Here we reconstituted purified β2-adrenergic receptor in High-Density-Lipoparticles to systematically characterize the effect of biologically relevant phospholipids on receptor activity. We observe that the lipid head-group type affects ligand binding (agonist and antagonist) and receptor activation. Specifically, phosphatidylgycerol markedly favors agonist binding and facilitates receptor activation while phosphatidylethanolamine favors antagonist binding and stabilizes the inactive state of the receptor. We then show that these effects can be recapitulated with detergent-solubilized lipids, demonstrating that the functional modulation occurs in the absence of a bilayer. Our data suggest that phospholipids act as direct allosteric modulators of GPCR activity.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
A RAPID METHOD OF TOTAL LIPID EXTRACTION AND PURIFICATION
Bligh, E. G., & Dyer, W. J. (1959) · Canadian Journal of Biochemistry and Physiology · doi:10.1139/o59-099 · Cited by 54,751
High-Resolution Crystal Structure of an Engineered Human β 2 -Adrenergic G Protein–Coupled Receptor
Cherezov, V., Rosenbaum, D. M., Hanson, M. A., Rasmussen, S. G. F., Thian, F. S., Kobilka, T. S., Choi, H.-J., Kuhn, P., Weis, W. I., Kobilka, B. K., et al. (2007) · Science · doi:10.1126/science.1150577 · Cited by 3,264
Self-citationCrystal structure of the β2 adrenergic receptor–Gs protein complex
Rasmussen, S. G. F., DeVree, B. T., Zou, Y., Kruse, A. C., Chung, K. Y., Kobilka, T. S., Thian, F. S., Chae, P. S., Pardon, E., Calinski, D., et al. (2011) · Nature · doi:10.1038/nature10361 · Cited by 3,009
Self-citationStructure of a nanobody-stabilized active state of the β2 adrenoceptor
Rasmussen, S. G. F., Choi, H.-J., Fung, J. J., Pardon, E., Casarosa, P., Chae, P. S., DeVree, B. T., Rosenbaum, D. M., Thian, F. S., Kobilka, T. S., et al. (2011) · Nature · doi:10.1038/nature09648 · Cited by 1,680
Self-citationAtomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment
Long, S. B., Tao, X., Campbell, E. B., & MacKinnon, R. (2007) · Nature · doi:10.1038/nature06265 · Cited by 1,411
How lipids affect the activities of integral membrane proteins
Lee, A. G. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2004.05.012 · Cited by 1,194
Chemistry and metabolism of lipids in the vertebrate retina
Fliesler, A. J., & Anderson, R. E. (1983) · Progress in Lipid Research · doi:10.1016/0163-7827(83)90004-8 · Cited by 1,052
Hanson, M. A., Cherezov, V., Griffith, M. T., Roth, C. B., Jaakola, V.-P., Chien, E. Y. T., Velasquez, J., Kuhn, P., & Stevens, R. C. (2008) · Structure · doi:10.1016/j.str.2008.05.001 · Cited by 933
The Dynamic Process of β2-Adrenergic Receptor Activation
Nygaard, R., Zou, Y., Dror, R. O., Mildorf, T. J., Arlow, D. H., Manglik, A., Pan, A. C., Liu, C. W., Fung, J. J., Bokoch, M. P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.008 · Cited by 796
Self-citationMembrane proteins bind lipids selectively to modulate their structure and function
Laganowsky, A., Reading, E., Allison, T. M., Ulmschneider, M. B., Degiacomi, M. T., Baldwin, A. J., & Robinson, C. V. (2014) · Nature · doi:10.1038/nature13419 · Cited by 781
Cited by
The Molecular Basis of G Protein–Coupled Receptor Activation
Weis, W. I., & Kobilka, B. K. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033910 · Cited by 1,227
Self-citationGPCR Dynamics: Structures in Motion
Latorraca, N. R., Venkatakrishnan, A. J., & Dror, R. O. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00177 · Cited by 835
Emerging Diversity in Lipid–Protein Interactions
Corradi, V., Sejdiu, B. I., Mesa-Galloso, H., Abdizadeh, H., Noskov, S. Y., Marrink, S. J., & Tieleman, D. P. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00451 · Cited by 459
PtdIns(4,5)P2 stabilizes active states of GPCRs and enhances selectivity of G-protein coupling
Yen, H.-Y., Hoi, K. K., Liko, I., Hedger, G., Horrell, M. R., Song, W., Wu, D., Heine, P., Warne, T., Lee, Y., et al. (2018) · Nature · doi:10.1038/s41586-018-0325-6 · Cited by 284
Nanobodies to Study G Protein–Coupled Receptor Structure and Function
Manglik, A., Kobilka, B. K., & Steyaert, J. (2017) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104710 · Cited by 257
Self-citation
Metadata
- Authors
- Dawaliby, R., Trubbia, C., Delporte, C., Masureel, M., Van Antwerpen, P., Kobilka, B. K., & Govaerts, C.
- Venue
- Nature Chemical Biology
- Published
- 2015-11-16
- Volume
- 12
- Issue
- 1
- Pages
- 35-39
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W2216747556
- Cited by
- 304
- References
- 42
- FWCI
- 11.84
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Allosteric regulation of G protein–coupled receptor activity by phospholipids. https://app.cochat.ai/papers/10.1038/nchembio.1960
- The paper
- Dawaliby, R., Trubbia, C., Delporte, C., Masureel, M., Van Antwerpen, P., Kobilka, B. K., & Govaerts, C. (2016). Allosteric regulation of G protein–coupled receptor activity by phospholipids. Nature Chemical Biology. https://doi.org/10.1038/nchembio.1960
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
