Evidence map›Paper›PMID 20959458›Full record

ArticleThe Journal of biological chemistry2010

A conserved protein interaction interface on the type 5 G protein beta subunit controls proteolytic stability and activity of R7 family regulator of G protein signaling proteins.

Morwenna Y Porter, Keqiang Xie, Edwin Pozharski, Michael R Koelle, Kirill A Martemyanov

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

14 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Activity of theeLife · 2016
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Parasite neuropeptide biology: Seeding rational drug target selection?International journal for parasitology. Drugs and drug resistance · 2012
    Review
  11. Article
  12. Article
  13. Membrane attachment is key to protecting transducin GTPase-activating complex from intracellular proteolysis in photoreceptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011
    Article
  14. 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 at 3 institutions in 1 country.

Morwenna Y PorterDepartment of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
Keqiang Xie
Edwin Pozharski
Michael R Koelle
Kirill A Martemyanov
University of Minnesota · USYale University · USUniversity of Maryland, Baltimore · US

Funding

Regulation of Signaling in the Retina by RGS ProteinsR01EY018139 · NEI · UNIVERSITY OF MINNESOTA · PI MARTEMYANOV, KIRILL A. · 2007 to 2025
$8.9M
G PROTEIN SIGNALING IN THE C ELEGANS NERVOUS SYSTEMR01NS036918 · NINDS · YALE UNIVERSITY · PI KOELLE, MICHAEL R · 1998 to 2019
$8.0M
Molecular Basis of RGS Protein Function in the StriatumR01DA021743 · NIDA · UNIVERSITY OF MINNESOTA · PI MARTEMYANOV, KIRILL A. · 2007 to 2011
$1.3M
Molecular Basis of RGS Protein Function in the StriatumK02DA026405 · NIDA · UNIVERSITY OF MINNESOTA · PI MARTEMYANOV, KIRILL A. · 2009 to 2019
$1.2M
Biochemical and genetic analysis of Regulator of G protein Signaling (RGS) proteiR21MH082201 · NIMH · YALE UNIVERSITY · PI KOELLE, MICHAEL R · 2008 to 2009
$372k
NEI NIH HHS EY018139NEI NIH HHS R01 EY018139NIDA NIH HHS DA021743NIDA NIH HHS DA026405NIDA NIH HHS K02 DA026405NIDA NIH HHS R01 DA021743NIMH NIH HHS MH082201NIMH NIH HHS R21 MH082201NINDS NIH HHS NS036918NINDS NIH HHS R01 NS036918
6 · The paper itself

Abstract

Regulators of G protein signaling (RGS) proteins of the R7 subfamily limit signaling by neurotransmitters in the brain and by light in the retina. They form obligate complexes with the Gβ5 protein that are subject to proteolysis to control their abundance and alter signaling. The mechanisms that regulate this proteolysis, however, remain unclear. We used genetic screens to find mutations in Gβ5 that selectively destabilize one of the R7 RGS proteins in Caenorhabditis elegans. These mutations cluster at the binding interface between Gβ5 and the N terminus of R7 RGS proteins. Equivalent mutations within mammalian Gβ5 allowed the interface to still bind the N-terminal DEP domain of R7 RGS proteins, and mutant Gβ5-R7 RGS complexes initially formed in cells but were then rapidly degraded by proteolysis. Molecular dynamics simulations suggest the mutations weaken the Gβ5-DEP interface, thus promoting dynamic opening of the complex to expose determinants of proteolysis known to exist on the DEP domain. We propose that conformational rearrangements at the Gβ5-DEP interface are key to controlling the stability of R7 RGS protein complexes.

Indexed as

Computer SimulationModels, MolecularAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsGTP-Binding Protein beta SubunitsHEK293 CellsHumansMultiprotein ComplexesMutationProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryRGS ProteinsCaenorhabditis elegans ProteinsGTP-Binding Protein beta SubunitsMultiprotein ComplexesRGS Proteins

Identifiers

PMID20959458
PMCPMC3003408
OpenAlexW2060148131

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.