Evidence map›Paper›PMID 21795707›Full record

ArticleThe Journal of biological chemistry2011

Two distinct aspects of coupling between Gα(i) protein and G protein-activated K+ channel (GIRK) revealed by fluorescently labeled Gα(i3) protein subunits.

Shai Berlin, Vladimir A Tsemakhovich, Ruth Castel, Tatiana Ivanina, Carmen W Dessauer, Tal Keren-Raifman, Nathan Dascal

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

25 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
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  8. TwoeLife · 2021
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  15. Molecular Pharmacology of δ-Opioid Receptors.Pharmacological reviews · 2016
    Review
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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

7 authors at 2 institutions in 2 countries.

Shai BerlinDepartment of Physiology and Pharmacology, Sackler School of Medicine, Tel Aviv University, Tel Aviv 69978, Israel.
Vladimir A Tsemakhovich
Ruth Castel
Tatiana Ivanina
Carmen W Dessauer
Tal Keren-Raifman
Nathan Dascal
Tel Aviv University · ILThe University of Texas Health Science Center at Houston · US

Funding

REGULATION OF ADENYLYL CYCLASE SIGNALING PATHWAYSR01GM060419 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DESSAUER, CARMEN W. · 2000 to 2021
$6.9M
NIGMS NIH HHS GM60419NIGMS NIH HHS R01 GM060419
6 · The paper itself

Abstract

G protein-activated K(+) channels (Kir3 or GIRK) are activated by direct interaction with Gβγ. Gα is essential for specific signaling and regulates basal activity of GIRK (I(basal)) and kinetics of the response elicited by activation by G protein-coupled receptors (I(evoked)). These regulations are believed to occur within a GIRK-Gα-Gβγ signaling complex. Fluorescent energy resonance transfer (FRET) studies showed strong GIRK-Gβγ interactions but yielded controversial results regarding the GIRK-Gα(i/o) interaction. We investigated the mechanisms of regulation of GIRK by Gα(i/o) using wild-type Gα(i3) (Gα(i3)WT) and Gα(i3) labeled at three different positions with fluorescent proteins, CFP or YFP (xFP). Gα(i3)xFP proteins bound the cytosolic domain of GIRK1 and interacted with Gβγ in a guanine nucleotide-dependent manner. However, only an N-terminally labeled, myristoylated Gα(i3)xFP (Gα(i3)NT) closely mimicked all aspects of Gα(i3)WT regulation except for a weaker regulation of I(basal). Gα(i3) labeled with YFP within the Gα helical domain preserved regulation of I(basal) but failed to restore fast I(evoked). Titrated expression of Gα(i3)NT and Gα(i3)WT confirmed that regulation of I(basal) and of the kinetics of I(evoked) of GIRK1/2 are independent functions of Gα(i). FRET and direct biochemical measurements indicated much stronger interaction between GIRK1 and Gβγ than between GIRK1 and Gα(i3). Thus, Gα(i/o)βγ heterotrimer may be attached to GIRK primarily via Gβγ within the signaling complex. Our findings support the notion that Gα(i/o) actively regulates GIRK. Although regulation of I(basal) is a function of Gα(i)(GDP), our new findings indicate that regulation of kinetics of I(evoked) is mediated by Gα(i)(GTP).

Indexed as

AnimalsBacterial ProteinsCell MembraneFluorescence Resonance Energy TransferFluorescent DyesG Protein-Coupled Inwardly-Rectifying Potassium ChannelsGreen Fluorescent ProteinsGTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsHumansLuminescent ProteinsMicePertussis ToxinProtein BindingProtein SubunitsBacterial ProteinsCyan Fluorescent ProteinFluorescent DyesGNAI3 protein, humanG Protein-Coupled Inwardly-Rectifying Potassium ChannelsGreen Fluorescent ProteinsGTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsLuminescent ProteinsPertussis ToxinProtein Subunitsyellow fluorescent protein, Bacteria

Identifiers

PMID21795707
PMCPMC3190912
OpenAlexW2060012277

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.