Evidence map›Paper›PMID 26488656›Full record

ArticleBiophysical journal2015

Can Specific Protein-Lipid Interactions Stabilize an Active State of the Beta 2 Adrenergic Receptor?

Chris Neale, Henry D Herce, Régis Pomès, Angel E García

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.1field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Lipid regulation of the glucagon receptor family.The Journal of endocrinology · 2024
    Review
  4. Article
  5. G Protein-Coupled Receptor Dimerization-What Next?International journal of molecular sciences · 2024
    Review
  6. Review
  7. Review
  8. CHARMM-GUIJournal of chemical theory and computation · 2023
    Review
  9. Elucidation of a dynamic interplay between a beta-2 adrenergic receptor, its agonist, and stimulatory G protein.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Allosteric Modulation of GPCRs of Class A by Cholesterol.International journal of molecular sciences · 2021
    Review
  15. Lipids and Phosphorylation Conjointly Modulate Complex Formation of βFrontiers in cell and developmental biology · 2021
    Article
  16. Review
  17. How Do Molecular Dynamics Data Complement Static Structural Data of GPCRs.International journal of molecular sciences · 2020
    Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Chris NealeDepartment of Physics, Applied Physics and Astronomy, Rensselaer Polytechnic Institute, Troy, New York.
Henry D HerceDepartment of Physics, Applied Physics and Astronomy, Rensselaer Polytechnic Institute, Troy, New York.
Régis PomèsMolecular Structure and Function, The Hospital for Sick Children, Toronto, Ontario, Canada; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
Angel E GarcíaDepartment of Physics, Applied Physics and Astronomy, Rensselaer Polytechnic Institute, Troy, New York; Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York. Electronic address: agarcia@lanl.gov.
Rensselaer Polytechnic Institute · USUniversity of Toronto · CA

Funding

Canadian Institutes of Health Research MOP-43998
6 · The paper itself

Abstract

G-protein-coupled receptors are eukaryotic membrane proteins with broad biological and pharmacological relevance. Like all membrane-embedded proteins, their location and orientation are influenced by lipids, which can also impact protein function via specific interactions. Extensive simulations totaling 0.25 ms reveal a process in which phospholipids from the membrane's cytosolic leaflet enter the empty G-protein binding site of an activated β2 adrenergic receptor and form salt-bridge interactions that inhibit ionic lock formation and prolong active-state residency. Simulations of the receptor embedded in an anionic membrane show increased lipid binding, providing a molecular mechanism for the experimental observation that anionic lipids can enhance receptor activity. Conservation of the arginine component of the ionic lock among Rhodopsin-like G-protein-coupled receptors suggests that intracellular lipid ingression between receptor helices H6 and H7 may be a general mechanism for active-state stabilization.

Indexed as

Binding SitesCarbonHumansLipid BilayersMolecular Dynamics SimulationMutationOxygenPhosphatidylcholinesPhosphatidylglycerolsProtein ConformationProtein StabilityReceptors, Adrenergic, beta-21-palmitoyl-2-oleoylglycero-3-phosphoglycerol1-palmitoyl-2-oleoylphosphatidylcholineCarbonLipid BilayersOxygenPhosphatidylcholinesPhosphatidylglycerolsReceptors, Adrenergic, beta-2

Identifiers

PMID26488656
PMCPMC4624154
OpenAlexW2120446433

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.