Evidence map›Paper›PMID 9763454›Full record

ArticleMolecular biology of the cell1998

Selection of gbeta subunits with point mutations that fail to activate specific signaling pathways in vivo: dissecting cellular responses mediated by a heterotrimeric G protein in Dictyostelium discoideum.

T Jin, M Amzel, P N Devreotes, L Wu

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Function and Regulation of Heterotrimeric G Proteins during Chemotaxis.International journal of molecular sciences · 2016
    Review
  3. Article
  4. Electrical signaling in control of ocular cell behaviors.Progress in retinal and eye research · 2012
    Review
  5. Cells navigate with a local-excitation, global-inhibition-biased excitable network.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  6. The signaling mechanisms underlying cell polarity and chemotaxis.Cold Spring Harbor perspectives in biology · 2009
    Review
  7. Directional sensing in eukaryotic chemotaxis: a balanced inactivation model.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  8. Article
  9. Article
  10. Article
  11. 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

4 authors at 2 institutions in 1 country.

T JinDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
M Amzel
P N Devreotes
L Wu
Johns Hopkins University · USKalVista Pharmaceuticals (United States) · US

Funding

Temporal and Spatial Signaling in ChemotaxisR01GM034933 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI DEVREOTES, PETER N · 1987 to 2015
$8.8M
NIGMS NIH HHS GM34933NIGMS NIH HHS R01 GM034933
6 · The paper itself

Abstract

In Dictyostelium discoideum, a unique Gbeta subunit is required for a G protein-coupled receptor system that mediates a variety of cellular responses. Binding of cAMP to cAR1, the receptor linked to the G protein G2, triggers a cascade of responses, including activation of adenylyl cyclase, gene induction, actin polymerization, and chemotaxis. Null mutations of the cAR1, Galpha2, and Gbeta genes completely impair all these responses. To dissect specificity in Gbetagamma signaling to downstream effectors in living cells, we screened a randomly mutagenized library of Gbeta genes and isolated Gbeta alleles that lacked the capacity to activate some effectors but retained the ability to regulate others. These mutant Gbeta subunits were able to link cAR1 to G2, to support gene expression, and to mediate cAMP-induced actin polymerization, and some were able to mediate to chemotaxis toward cAMP. None was able to activate adenylyl cyclase, and some did not support chemotaxis. Thus, we separated in vivo functions of Gbetagamma by making point mutations on Gbeta. Using the structure of the heterotrimeric G protein displayed in the computer program CHAIN, we examined the positions and the molecular interactions of the amino acids substituted in each of the mutant Gbetas and analyzed the possible effects of each replacement. We identified several residues that are crucial for activation of the adenylyl cyclase. These residues formed an area that overlaps but is not identical to regions where bovine Gtbetagamma interacts with its regulators, Galpha and phosducin.

Indexed as

Adenylyl CyclasesAmino Acid SequenceAnimalsBinding SitesCattleChemotaxisCyclic AMPDictyosteliumGene Expression RegulationGenes, ProtozoanGTP-Binding ProteinsHumansMacromolecular SubstancesMiceModels, MolecularMolecular Sequence DataAdenylyl CyclasesCyclic AMPcyclic AMP receptor cAR1GTP-Binding ProteinsMacromolecular SubstancesProtozoan ProteinsReceptors, Cyclic AMPRecombinant Proteins

Identifiers

PMID9763454
PMCPMC25572
OpenAlexW2132033694

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.