Evidence map›Paper›PMID 25413469›Full record

ReviewPflugers Archiv : European journal of physiology2015

Endocytosis as a mode to regulate functional expression of two-pore domain potassium (K₂p) channels.

Ita O'Kelly

Open access · hybridAbstract readReview
In one paragraph

Review in Pflugers Archiv : European journal of physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed, 11 citations in OpenAlex.

  1. Extracellular histones promote TWIK2-dependent potassium efflux and associated NLRP3 activation in alveolar macrophages during sepsis-induced lung injury.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2024
    Article
  2. Article
  3. Article
  4. Non-NMDA Mechanisms of Analgesia in Ketamine Analogs.Frontiers in pain research (Lausanne, Switzerland) · 2022
    Article
  5. TASK channels: channelopathies, trafficking, and receptor-mediated inhibition.Pflugers Archiv : European journal of physiology · 2020
    Review
  6. Article
  7. Much more than a leak: structure and function of K₂p-channels.Pflugers Archiv : European journal of physiology · 2015
    Review
  8. Review
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

1 author at 1 institution in 1 country.

Ita O'KellyHuman Development and Health, Centre for Human Development, Stem Cells and Regeneration, Faculty of Medicine, University of Southampton, Southampton, SO16 6YD, UK, I.M.O'Kelly@southampton.ac.uk.
University of Southampton · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J008168/1
6 · The paper itself

Abstract

Two-pore domain potassium (K2P) channels are implicated in an array of physiological and pathophysiological roles. As a result of their biophysical properties, these channels produce a background leak K(+) current which has a direct effect on cellular membrane potential and activity. The regulation of potassium leak from cells through K2P channels is of critical importance to cell function, development and survival. Controlling the cell surface expression of these channels is one mode to regulate their function and is achieved through a balance between regulated channel delivery to and retrieval from the cell surface. Here, we explore the modes of retrieval of K2P channels from the plasma membrane and observe that K2P channels are endocytosed in both a clathrin-mediated and clathrin-independent manner. K2P channels use a variety of pathways and show altered internalisation and sorting in response to external cues. These pathways working in concert, equip the cell with a range of approaches to maintain steady state levels of channels and to respond rapidly should changes in channel density be required.

Indexed as

AnimalsCell MembraneEndocytosisHumansMetabolic Networks and PathwaysPotassiumPotassium Channels, Tandem Pore DomainProtein TransportPotassiumPotassium Channels, Tandem Pore Domain

Identifiers

PMID25413469
PMCPMC4428836
OpenAlexW2139849763

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.