Evidence map›Paper›PMID 34292354›Full record

ArticleCellular and molecular life sciences : CMLS2021

Residue-level determinants of RGS R4 subfamily GAP activity and specificity towards the G

Ali Asli, Sabreen Higazy-Mreih, Meirav Avital-Shacham, Mickey Kosloff

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

5 citing papers in PubMed, 11 citations in OpenAlex.

  1. GαThe FEBS journal · 2025
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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 1 institution in 1 country.

Ali Asli *The Department of Human Biology, Faculty of Natural Science, University of Haifa, 199 Aba Khoushy Ave., Mt. Carmel, 3498838, Haifa, Israel.
Sabreen Higazy-Mreih *The Department of Human Biology, Faculty of Natural Science, University of Haifa, 199 Aba Khoushy Ave., Mt. Carmel, 3498838, Haifa, Israel.
Meirav Avital-ShachamThe Department of Human Biology, Faculty of Natural Science, University of Haifa, 199 Aba Khoushy Ave., Mt. Carmel, 3498838, Haifa, Israel.
Mickey KosloffThe Department of Human Biology, Faculty of Natural Science, University of Haifa, 199 Aba Khoushy Ave., Mt. Carmel, 3498838, Haifa, Israel. kosloff@sci.haifa.ac.il.ORCID http://orcid.org/0000-0003-1807-4000
University of Haifa · IL

Funding

European Cooperation in Science and Technology CA-15126European Cooperation in Science and Technology CA-18133European Cooperation in Science and Technology CM-1207Israel Science Foundation 1454/13Israel Science Foundation 2155/15Israel Science Foundation (IL) 1959/13Israel Science Foundation (IL) 3512/19
6 · The paper itself

Abstract

The structural basis for the GTPase-accelerating activity of regulators of G protein signaling (RGS) proteins, as well as the mechanistic basis for their specificity in interacting with the heterotrimeric (αβγ) G proteins they inactivate, is not sufficiently understood at the family level. Here, we used biochemical assays to compare RGS domains across the RGS family and map those individual residues that favorably contribute to GTPase-accelerating activity, and those residues responsible for attenuating RGS domain interactions with Gα subunits. We show that conserved interactions of RGS residues with both the Gα switch I and II regions are crucial for RGS activity, while the reciprocal effects of "modulatory" and "disruptor" residues selectively modulate RGS activity. Our results quantify how specific interactions between RGS domains and Gα subunits are set by a balance between favorable RGS residue interactions with particular Gα switch regions, and unfavorable interactions with the Gα helical domain.

Indexed as

Amino Acid SequenceBinding SitesGTP-Binding Protein alpha Subunits, Gq-G11HumansMolecular Dynamics SimulationMutagenesis, Site-DirectedProtein BindingProtein Conformation, alpha-HelicalProtein DomainsProtein IsoformsProtein Structure, TertiaryProtein SubunitsRGS ProteinsSequence AlignmentThermodynamicsGTP-Binding Protein alpha Subunits, Gq-G11Protein IsoformsProtein SubunitsRGS ProteinsGTPasesProtein–protein interactionsProtein structureSignal transduction

Identifiers

PMID34292354
PMCPMC11072900
OpenAlexW3183998003

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.