Evidence map›Paper›PMID 32634377›Full record

ArticleCell2020

Revealing the Activity of Trimeric G-proteins in Live Cells with a Versatile Biosensor Design.

Marcin Maziarz, Jong-Chan Park, Anthony Leyme, Arthur Marivin, Alberto Garcia-Lopez, Prachi P Patel, Mikel Garcia-Marcos

Abstract read
In one paragraph

Article in Cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

60 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Biased signalingActa pharmaceutica Sinica. B · 2025
    Review
  8. Article
  9. Review
  10. Discovery ofActa pharmaceutica Sinica. B · 2025
    Article
  11. Article
  12. 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
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Higher-order transient structures and the principle of dynamic connectivity in membrane signaling.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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

7 authors.

Marcin MaziarzDepartment of Biochemistry, Boston University School of Medicine, Boston, MA 02118, USA.
Jong-Chan ParkDepartment of Biochemistry, Boston University School of Medicine, Boston, MA 02118, USA.
Anthony LeymeDepartment of Biochemistry, Boston University School of Medicine, Boston, MA 02118, USA.
Arthur MarivinDepartment of Biochemistry, Boston University School of Medicine, Boston, MA 02118, USA.
Alberto Garcia-LopezDepartment of Biochemistry, Boston University School of Medicine, Boston, MA 02118, USA.
Prachi P PatelDepartment of Biochemistry, Boston University School of Medicine, Boston, MA 02118, USA.
Mikel Garcia-MarcosDepartment of Biochemistry, Boston University School of Medicine, Boston, MA 02118, USA. Electronic address: mgm1@bu.edu.

Funding

Non-canonical activation of heterotrimeric G protein signaling in vivoR01GM136132 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI GARCIA-MARCOS, MIKEL · 2019 to 2022
$1.9M
Alternative mechanisms of signaling via trimeric G proteinsR01GM108733 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI GARCIA-MARCOS, MIKEL · 2014 to 2018
$1.6M
Targeting of non-canonical G protein signaling with small moleculesR01GM130120 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI GARCIA-MARCOS, MIKEL · 2018 to 2021
$1.4M
Next generation G protein activity biosensorsR21MH118745 · NIMH · BOSTON UNIVERSITY MEDICAL CAMPUS · PI GARCIA-MARCOS, MIKEL · 2018 to 2019
$454k
NIGMS NIH HHS R01 GM108733NIGMS NIH HHS R01 GM130120NIGMS NIH HHS R01 GM136132NIMH NIH HHS R21 MH118745
6 · The paper itself

Abstract

Heterotrimeric G-proteins (Gαβγ) are the main transducers of signals from GPCRs, mediating the action of countless natural stimuli and therapeutic agents. However, there are currently no robust approaches to directly measure the activity of endogenous G-proteins in cells. Here, we describe a suite of optical biosensors that detect endogenous active G-proteins with sub-second resolution in live cells. Using a modular design principle, we developed genetically encoded, unimolecular biosensors for endogenous Gα-GTP and free Gβγ: the two active species of heterotrimeric G-proteins. This design was leveraged to generate biosensors with specificity for different heterotrimeric G-proteins or for other G-proteins, such as Rho GTPases. Versatility was further validated by implementing the biosensors in multiple contexts, from characterizing cancer-associated G-protein mutants to neurotransmitter signaling in primary neurons. Overall, the versatile biosensor design introduced here enables studying the activity of endogenous G-proteins in live cells with high fidelity, temporal resolution, and convenience.

Indexed as

Amino Acid MotifsAnimalsBioluminescence Resonance Energy Transfer TechniquesBiosensing TechniquesCells, CulturedGTP-Binding Protein alpha Subunits, Gq-G11Guanine Nucleotide Exchange FactorsGuanosine TriphosphateHEK293 CellsHeLa CellsHeterotrimeric GTP-Binding ProteinsHumansMiceMice, Inbred C57BLMutationNeoplasmsGTP-Binding Protein alpha Subunits, Gq-G11Guanine Nucleotide Exchange FactorsGuanosine TriphosphateHeterotrimeric GTP-Binding ProteinsReceptors, G-Protein-CoupledbiosensorBRETcancerGPCRG proteinGTPaseneurobiologyneurotransmitteroncogene

Identifiers

PMID32634377
PMCPMC7415655

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Registered trials

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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.