Evidence map›Paper›PMID 27377235›Full record

ArticleThe Journal of physiology2016

N-linked glycosylation of Kv1.2 voltage-gated potassium channel facilitates cell surface expression and enhances the stability of internalized channels.

Desiree A Thayer, Shi-Bing Yang, Yuh Nung Jan, Lily Y Jan

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.7field-weighted citation impact, top 26% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Sialylation in the nervous system: Functions and mechanisms.The Journal of biological chemistry · 2026
    Review
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  9. An epilepsy-associated KProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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  11. Glycosylation of β1 subunit plays a pivotal role in the toxin sensitivity and activation of BK channels.The journal of venomous animals and toxins including tropical diseases · 2021
    Article
  12. 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

4 authors at 3 institutions in 2 countries.

Desiree A ThayerHoward Hughes Medical Institute, Departments of Physiology, Biochemistry and Biophysics, Kavli Institute for Fundamental Neuroscience, Weill Institute for Neurosciences, University of California-San Francisco, San Francisco, CA, USA.
Shi-Bing YangHoward Hughes Medical Institute, Departments of Physiology, Biochemistry and Biophysics, Kavli Institute for Fundamental Neuroscience, Weill Institute for Neurosciences, University of California-San Francisco, San Francisco, CA, USA.
Yuh Nung JanHoward Hughes Medical Institute, Departments of Physiology, Biochemistry and Biophysics, Kavli Institute for Fundamental Neuroscience, Weill Institute for Neurosciences, University of California-San Francisco, San Francisco, CA, USA.
Lily Y JanHoward Hughes Medical Institute, Departments of Physiology, Biochemistry and Biophysics, Kavli Institute for Fundamental Neuroscience, Weill Institute for Neurosciences, University of California-San Francisco, San Francisco, CA, USA.
Howard Hughes Medical Institute · USAmunix (United States) · USUniversity of California, San Francisco · US

Funding

Genetic Studies of the SynapseR37MH065334 · NIMH · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JAN, LILY Y · 2006 to 2015
$3.8M
NIMH NIH HHS R37 MH065334
6 · The paper itself

Abstract

key pointsKv1.2 and related voltage-gated potassium channels have a highly conserved N-linked glycosylation site in the first extracellular loop, with complex glycosylation in COS-7 cells similar to endogenous Kv1.2 glycosylation in hippocampal neurons. COS-7 cells expressing Kv1.2 show a crucial role of this N-linked glycosylation in the forward trafficking of Kv1.2 to the cell membrane. Although both wild-type and non-glycosylated mutant Kv1.2 channels that have reached the cell membrane are internalized at a comparable rate, mutant channels are degraded at a faster rate. Treatment of wild-type Kv1.2 channels on the cell surface with glycosidase to remove sialic acids also results in the faster degradation of internalized channels. Glycosylation of Kv1.2 is important with respect to facilitating trafficking to the cell membrane and enhancing the stability of channels that have reached the cell membrane. ABSTRACT: Studies in cultured hippocampal neurons and the COS-7 cell line demonstrate important roles for N-linked glycosylation of Kv1.2 channels in forward trafficking and protein degradation. Kv1.2 channels can contain complex N-linked glycans, which facilitate cell surface expression of the channels. Additionally, the protein stability of cell surface-expressed Kv1.2 channels is affected by glycosylation via differences in the degradation of internalized channels. The present study reveals the importance of N-linked complex glycosylation in boosting Kv1.2 channel density. Notably, sialic acids at the terminal sugar branches play an important role in dampening the degradation of Kv1.2 internalized from the cell membrane to promote its stability.

Indexed as

AnimalsCell LineCell MembraneChlorocebus aethiopsCOS CellsFemaleGlycosylationKv1.2 Potassium ChannelNeuronsPolysaccharidesPotassium Channels, Voltage-GatedPregnancyProtein TransportRatsRats, Sprague-DawleyKv1.2 Potassium ChannelPolysaccharidesPotassium Channels, Voltage-Gatedchannel stabilitychannel traffickingglycosylationpotassium channelvoltage-gated channels

Identifiers

PMID27377235
PMCPMC5108895
OpenAlexW2474848014

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.