Evidence map›Paper›PMID 22306739›Full record

ArticleJournal of molecular biology2012

Modulation of the interaction between neurotensin receptor NTS1 and Gq protein by lipid.

Sayaka Inagaki, Rodolfo Ghirlando, Jim F White, Jelena Gvozdenovic-Jeremic, John K Northup, Reinhard Grisshammer

Abstract read
In one paragraph

Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

61 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Anionic Phospholipids Control Mechanisms of GPCR-G Protein Recognition.bioRxiv : the preprint server for biology · 2023
    Article
  7. Spectroscopic signatures of bilayer ordering in native biological membranes.Biochimica et biophysica acta. Biomembranes · 2022
    Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. DNA-Mediated Stack Formation of Nanodiscs.Molecules (Basel, Switzerland) · 2021
    Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Article
  20. Review

1 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 1 country.

Sayaka InagakiMembrane Protein Structure Function Unit, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Department of Health and Human Services, Rockville, MD 20852, USA.
Rodolfo Ghirlando
Jim F White
Jelena Gvozdenovic-Jeremic
John K Northup
Reinhard Grisshammer
National Institutes of Health · USNational Institute of Neurological Disorders and Stroke · USNational Institute on Deafness and Other Communication Disorders · US

Funding

Biophysics of Macromolecular ComplexesZIADK033007 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2024
$4.9M
Function of integral membrane proteinsZIANS003103 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI GRISSHAMMER, REINHARD · 2009 to 2015
$3.9M
Selectivity in G-protein-receptor couplingZIADC000047 · NIDCD · NATIONAL INSTITUTE ON DEAFNESS AND OTHER COMMUNICATION DISORDERS · PI NORTHUP, JOHN K · 2009 to 2012
$2.0M
Intramural NIH HHS ZIA NS003103
6 · The paper itself

Abstract

Membrane lipids have been implicated to influence the activity of G-protein-coupled receptors (GPCRs). Almost all of our knowledge on the role of lipids on GPCR and G protein function comes from work on the visual pigment rhodopsin and its G protein transducin, which reside in a highly specialized membrane environment. Thus, insight gained from rhodopsin signaling may not be simply translated to other nonvisual GPCRs. Here, we investigated the effect of lipid head group charges on the signal transduction properties of the class A GPCR neurotensin (NT) receptor 1 (NTS1) under defined experimental conditions, using self-assembled phospholipid nanodiscs prepared with the zwitter-ionic lipid 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), the negatively charged 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1'-rac-glycerol) (POPG), or a POPC/POPG mixture. A combination of dynamic light scattering and sedimentation velocity showed that NTS1 was monomeric in POPC-, POPC/POPG-, and POPG-nanodiscs. Binding of the agonist NT to NTS1 occurred with similar affinities and was essentially unaffected by the phospholipid composition. In contrast, Gq protein coupling to NTS1 in various lipid nanodiscs was significantly different, and the apparent affinity of Gαq and Gβ(1)γ(1) to activated NTS1 increased with increasing POPG content. NTS1-catalyzed GDP/GTPγS nucleotide exchange at Gαq in the presence of Gβ(1)γ(1) and NT was crucially affected by the lipid type, with exchange rates higher by 1 or 2 orders of magnitude in POPC/POPG- and POPG-nanodiscs, respectively, compared to POPC-nanodiscs. Our data demonstrate that negatively charged lipids in the immediate vicinity of a nonvisual GPCR modulate the G-protein-coupling step.

Indexed as

Signal TransductionAnimalsGTP-Binding Protein alpha Subunits, Gq-G11HumansLipid BilayersPhosphatidylcholinesPhosphatidylglycerolsRatsReceptors, G-Protein-CoupledReceptors, Neurotensin1-palmitoyl-2-oleoylglycero-3-phosphoglycerol1-palmitoyl-2-oleoylphosphatidylcholineGTP-Binding Protein alpha Subunits, Gq-G11Lipid Bilayersneurotensin type 1 receptorPhosphatidylcholinesPhosphatidylglycerolsReceptors, G-Protein-CoupledReceptors, Neurotensin

Identifiers

PMID22306739
PMCPMC3294418
OpenAlexW2103912693

What OpenQuestion holds

Textmetadata
LicenceTDM
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.