Evidence map›Paper›PMID 22846993›Full record

ArticleThe Journal of biological chemistry2012

The acid-sensitive, anesthetic-activated potassium leak channel, KCNK3, is regulated by 14-3-3β-dependent, protein kinase C (PKC)-mediated endocytic trafficking.

Luke Gabriel, Anatoli Lvov, Demetra Orthodoxou, Ann R Rittenhouse, William R Kobertz, Haley E Melikian

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
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  4. Frontiers in cell and developmental biology · 2020
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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

6 authors at 2 institutions in 1 country.

Luke GabrielGraduate Program in Neuroscience, University of Massachusetts Medical School, Worcester, Massachusetts 01604, USA.
Anatoli Lvov
Demetra Orthodoxou
Ann R Rittenhouse
William R Kobertz
Haley E Melikian
University of Massachusetts Chan Medical School · USNeuropsychiatric Research Institute · US

Funding

K+ channel complexes: assembly, trafficking and functionR01GM070650 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI KOBERTZ, WILLIAM R · 2005 to 2022
$5.7M
Trafficking and Regulation of Monoamine TransportersR01DA015169 · NIDA · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI MELIKIAN, HALEY E · 2002 to 2017
$5.2M
NIDA NIH HHS DA15169NIDA NIH HHS R01 DA015169NIGMS NIH HHS GM070650NIGMS NIH HHS R01 GM070650
6 · The paper itself

Abstract

The acid-sensitive neuronal potassium leak channel, KCNK3, is vital for setting the resting membrane potential and is the primary target for volatile anesthetics. Recent reports demonstrate that KCNK3 activity is down-regulated by PKC; however, the mechanisms responsible for PKC-induced KCNK3 down-regulation are undefined. Here, we report that endocytic trafficking dynamically regulates KCNK3 activity. Phorbol esters and Group I metabotropic glutamate receptor (mGluR) activation acutely decreased both native and recombinant KCNK3 currents with concomitant KCNK3 surface losses in cerebellar granule neurons and cell lines. PKC-mediated KCNK3 internalization required the presence of both 14-3-3β and a novel potassium channel endocytic motif, because depleting either 14-3-3β protein levels or ablating the endocytic motif completely abrogated PKC-regulated KCNK3 trafficking. These results demonstrate that neuronal potassium leak channels are not static membrane residents but are subject to 14-3-3β-dependent regulated trafficking, providing a straightforward mechanism to modulate neuronal excitability and synaptic plasticity by Group I mGluRs.

Indexed as

14-3-3 ProteinsAmino Acid MotifsAnimalsCerebellumEndocytosisHEK293 CellsHumansNerve Tissue ProteinsNeuronsPotassium Channels, Tandem Pore DomainProtein Kinase CProtein TransportRats, Sprague-DawleyReceptors, Metabotropic Glutamate14-3-3 Proteinsmetabotropic glutamate receptor type 1Nerve Tissue ProteinsPotassium Channels, Tandem Pore Domainpotassium channel subfamily K member 3Protein Kinase CReceptors, Metabotropic Glutamate

Identifiers

PMID22846993
PMCPMC3463364
OpenAlexW2084722877

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.