Evidence map›Paper›PMID 22538369›Full record

ArticleBiochemical and biophysical research communications2012

All G protein βγ complexes are capable of translocation on receptor activation.

W K Ajith Karunarathne, Patrick R O'Neill, Pedro L Martinez-Espinosa, Vani Kalyanaraman, N Gautam

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
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

31 citing papers in PubMed.

  1. Article
  2. Opioid receptors reveal a discrete cellular mechanism of endosomal G protein activation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Molecular regulation of PLCβ signaling.Methods in enzymology · 2023
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  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

5 authors.

W K Ajith KarunarathneDepartment of Anesthesiology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Patrick R O'Neill
Pedro L Martinez-Espinosa
Vani Kalyanaraman
N Gautam

Funding

SIGNALING IN LIVING CELLSR01GM069027 · NIGMS · WASHINGTON UNIVERSITY · PI GAUTAM, NARASIMHAN · 2004 to 2016
$3.2M
AUXILIARY SUBUNITS OF CA2+ ACTIVATED K+ CHANNELSR01GM081748 · NIGMS · WASHINGTON UNIVERSITY · PI LINGLE, CHRISTOPHER J · 2008 to 2015
$3.2M
G PROTEIN SUBUNIT FUNCTIONR01GM080558 · NIGMS · WASHINGTON UNIVERSITY · PI GAUTAM, NARASIMHAN · 2008 to 2011
$1.8M
Mechanism and role of G-protein subunit translocation in cell signalingF32GM099351 · NIGMS · WASHINGTON UNIVERSITY · PI O'NEILL, PATRICK ROSS · 2011 to 2013
$155k
NIGMS NIH HHS F32 GM099351NIGMS NIH HHS GM080558NIGMS NIH HHS GM081748NIGMS NIH HHS GM69027NIGMS NIH HHS R01 GM069027NIGMS NIH HHS R01 GM080558NIGMS NIH HHS R01 GM081748
6 · The paper itself

Abstract

Heterotrimeric G proteins transduce signals sensed by transmembrane G protein coupled receptors (GPCRs). A subfamily of G protein βγ subunit types has been shown to selectively translocate from the plasma membrane to internal membranes on receptor activation. Using 4D imaging we show here that Gβγ translocation is not restricted to some subunit types but rather all 12 members of the family of mammalian γ subunits are capable of supporting βγ translocation. Translocation kinetics varies widely depending on the specific γ subunit type, with t(1/2) ranging from 10s to many minutes. Using fluorescence complementation, we show that the β and γ subunits translocate as βγ dimers with kinetics determined by the γ subunit type. The expression patterns of endogenous γ subunit types in HeLa cells, hippocampal neurons and cardiomyocytes are distinctly different. Consistent with these differences, the βγ translocation rates vary widely. βγ translocation rates exhibit the same γ subunit dependent trends regardless of the specific receptor type or cell type showing that the translocation rates are intrinsic to the γ subunit types. βγ complexes with widely different rates of translocation had differential effects on muscarinic stimulation of GIRK channel activity. These results show that G protein βγ translocation is a general response to activation of GPCRs and may play a role in regulating signaling activity.

Indexed as

Bacterial ProteinsG Protein-Coupled Inwardly-Rectifying Potassium ChannelsGreen Fluorescent ProteinsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsHeLa CellsHippocampusHumansLuminescent ProteinsMyocytes, CardiacNeuronsProtein TransportReceptors, G-Protein-CoupledReceptors, MuscarinicBacterial ProteinsG Protein-Coupled Inwardly-Rectifying Potassium ChannelsGreen Fluorescent ProteinsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsLuminescent ProteinsReceptors, G-Protein-CoupledReceptors, Muscarinicyellow fluorescent protein, Bacteria

Identifiers

PMID22538369
PMCPMC3351579

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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.