Evidence map›Paper›PMID 21876134›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Heterotrimeric G protein beta1gamma2 subunits change orientation upon complex formation with G protein-coupled receptor kinase 2 (GRK2) on a model membrane.

Andrew P Boughton, Pei Yang, Valerie M Tesmer, Bei Ding, John J G Tesmer, Zhan Chen

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

22 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
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  5. Article
  6. Article
  7. Review
  8. Article
  9. Strike a pose: Gαq complexes at the membrane.Trends in pharmacological sciences · 2014
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Dependence of Alamethicin Membrane Orientation on the Solution Concentration.The journal of physical chemistry. C, Nanomaterials and interfaces · 2013
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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 1 institution in 1 country.

Andrew P BoughtonDepartment of Chemistry, University of Michigan, 930 North University Avenue, Ann Arbor, MI 48109, USA.
Pei Yang
Valerie M Tesmer
Bei Ding
John J G Tesmer
Zhan Chen
University of Michigan–Ann Arbor · US

Funding

Structure, function, and inhibition of G protein-coupled receptor kinasesR01HL071818 · NHLBI · UNIVERSITY OF TEXAS AUSTIN · PI TESMER, JOHN · 2004 to 2023
$7.1M
Structural Studies of Galphaq and Its Complexes at the Cell MembraneR01HL086865 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TESMER, JOHN · 2007 to 2015
$3.0M
SFG Investigation of Peptide and Protein Orientations in MembranesR01GM081655 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CHEN, ZHAN · 2008 to 2012
$1.5M
NHLBI NIH HHS HL071818NHLBI NIH HHS HL086865NHLBI NIH HHS R01 HL071818NHLBI NIH HHS R01 HL086865NIGMS NIH HHS GM081655NIGMS NIH HHS R01 GM081655
6 · The paper itself

Abstract

Few experimental techniques can assess the orientation of peripheral membrane proteins in their native environment. Sum Frequency Generation (SFG) vibrational spectroscopy was applied to study the formation of the complex between G protein-coupled receptor (GPCR) kinase 2 (GRK2) and heterotrimeric G protein β(1)γ(2) subunits (Gβγ) at a lipid bilayer, without any exogenous labels. The most likely membrane orientation of the GRK2-Gβγ complex differs from that predicted from the known protein crystal structure, and positions the predicted receptor docking site of GRK2 such that it would more optimally interact with GPCRs. Gβγ also appears to change its orientation after binding to GRK2. The developed methodology is widely applicable for the study of other membrane proteins in situ.

Indexed as

Membranes, ArtificialG-Protein-Coupled Receptor Kinase 2GTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsLipid BilayersModels, MolecularPhosphatidylcholinesPhosphatidylglycerolsProtein BindingProtein ConformationSpectrum AnalysisVibration1-palmitoyl-2-oleoylglycero-3-phosphoglycerol1-palmitoyl-2-oleoylphosphatidylcholineG-Protein-Coupled Receptor Kinase 2GTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsLipid BilayersMembranes, ArtificialPhosphatidylcholinesPhosphatidylglycerols

Identifiers

PMID21876134
PMCPMC3174637
OpenAlexW2005325726

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.