Evidence map›Paper›PMID 26152716›Full record

ArticleThe Journal of biological chemistry2015

Rab11-dependent Recycling of the Human Ether-a-go-go-related Gene (hERG) Channel.

Jeffery Chen, Jun Guo, Tonghua Yang, Wentao Li, Shawn M Lamothe, Yudi Kang, John A Szendrey, Shetuan Zhang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 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
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

8 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Subcellular trafficking and endocytic recycling of KAmerican journal of physiology. Cell physiology · 2022
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. hERG quality control and the long QT syndrome.The Journal of physiology · 2016
    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

8 authors at 1 institution in 1 country.

Jeffery ChenDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario K7L 3N6, Canada.
Jun GuoDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario K7L 3N6, Canada.
Tonghua YangDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario K7L 3N6, Canada.
Wentao LiDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario K7L 3N6, Canada.
Shawn M LamotheDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario K7L 3N6, Canada.
Yudi KangDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario K7L 3N6, Canada.
John A SzendreyDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario K7L 3N6, Canada.
Shetuan ZhangDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario K7L 3N6, Canada. Electronic address: shetuan.zhang@queensu.ca.
Queen's University · CA

Funding

Canadian Institutes of Health Research MOP 72911
6 · The paper itself

Abstract

The human ether-a-go-go-related gene (hERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel (IKr). A reduction in the hERG current causes long QT syndrome, which predisposes affected individuals to ventricular arrhythmias and sudden death. We reported previously that hERG channels in the plasma membrane undergo vigorous internalization under low K(+) conditions. In the present study, we addressed whether hERG internalization occurs under normal K(+) conditions and whether/how internalized channels are recycled back to the plasma membrane. Using patch clamp, Western blot, and confocal imaging analyses, we demonstrated that internalized hERG channels can effectively recycle back to the plasma membrane. Low K(+)-enhanced hERG internalization is accompanied by an increased rate of hERG recovery in the plasma membrane upon reculture following proteinase K-mediated clearance of cell-surface proteins. The increased recovery rate is not due to enhanced protein synthesis, as hERG mRNA expression was not altered by low K(+) exposure, and the increased recovery was observed in the presence of the protein biosynthesis inhibitor cycloheximide. GTPase Rab11, but not Rab4, is involved in the recycling of hERG channels. Interfering with Rab11 function not only delayed hERG recovery in cells after exposure to low K(+) medium but also decreased hERG expression and function in cells under normal culture conditions. We concluded that the recycling pathway plays an important role in the homeostasis of plasma membrane-bound hERG channels.

Indexed as

Amino Acid SequenceCell MembraneCycloheximideEndopeptidase KERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsGene ExpressionHEK293 CellsHumansIon TransportMolecular Sequence DataPatch-Clamp TechniquesPotassiumProtein Transportrab11 GTP-Binding Proteinsrab4 GTP-Binding ProteinsCycloheximideEndopeptidase KERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsKCNH2 protein, humanPotassiumrab11 GTP-Binding Proteinsrab4 GTP-Binding Proteinsrab GTP-Binding ProteinsRNA, Messengercell-surface proteinelectrophysiologyhERGpatch clamppotassium channeltrafficking

Identifiers

PMID26152716
PMCPMC4543667
OpenAlexW1853984831

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.