Evidence map›Paper›PMID 22106938›Full record

ArticleJournal of proteome research2012

Dynamic modulation of the kv2.1 channel by SRC-dependent tyrosine phosphorylation.

Min-Young Song, Chansik Hong, Seong Han Bae, Insuk So, Kang-Sik Park

Abstract read
In one paragraph

Article in Journal of proteome research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
  2. Sites and Regulation of L-Type CaCellular and molecular neurobiology · 2022
    Article
  3. Article
  4. Tyrosine Phosphorylation of the KInternational journal of molecular sciences · 2020
    Article
  5. Article
  6. Article
  7. Article
  8. Chronic CaThe Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2017
    Article
  9. Article
  10. Article
  11. Article
  12. Observational
  13. Leptin modulates the intrinsic excitability of AgRP/NPY neurons in the arcuate nucleus of the hypothalamus.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  14. Article
  15. Review
  16. Article
  17. Distinct modifications in Kv2.1 channel via chemokine receptor CXCR4 regulate neuronal survival-death dynamics.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article
  18. Regulation of neuronal proapoptotic potassium currents by the hepatitis C virus nonstructural protein 5A.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article
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

5 authors.

Min-Young SongDepartment of Physiology and ‡Biomedical Science Institute, Kyung Hee University School of Medicine, Seoul 130-701, South Korea.
Chansik Hong
Seong Han Bae
Insuk So
Kang-Sik Park

Funding

Determinants of Dendritic Potassium Channel LocalizationR01NS042225 · NINDS · UNIVERSITY OF CALIFORNIA DAVIS · PI TRIMMER, JAMES S · 2001 to 2014
$6.3M
NINDS NIH HHS NS42225NINDS NIH HHS R01 NS042225
6 · The paper itself

Abstract

The voltage-gated K(+) channel Kv2.1 is expressed as a highly phosphorylated protein in most central neurons, where it plays a key role in regulating neuronal membrane excitability. Previous studies have shown that Kv2.1 channel activity is upregulated by Src-mediated phosphorylation through an unknown mechanism. However, a systematic analysis of the molecular mechanism of Kv2.1 channel phosphorylation by Src is lacking. Here, we show that tyrosine phosphorylation by Src plays a fundamental role in regulating Kv2.1-mediated K(+) current enhancement. We found that the level of expression of the Kv2.1 protein is increased by Src kinase. Using mass spectrometric proteomic techniques, we identified two novel phosphotyrosine sites, Y686 and Y810, in the cytoplasmic domains of Kv2.1. We found that Src-dependent phosphorylation at these sites affects Kv2.1 through distinct regulatory mechanisms. Whereas phosphorylation at Y686 regulates Kv2.1 activity similarly to the known site Y124, phosphorylation at Y810 plays a significant role in regulating the intracellular trafficking of Kv2.1 channels. Our results show that these two novel tyrosine phosphorylation sites of Kv2.1 are crucial to regulating diverse aspects of Kv2.1 channel function and provide novel insights into molecular mechanisms for the regulation of Src-dependent modulation of Kv2.1 channels.

Indexed as

Catalytic DomainHEK293 CellsHumansIon TransportMass SpectrometryPatch-Clamp TechniquesPhosphorylationShab Potassium Channelssrc-Family KinasesShab Potassium Channelssrc-Family Kinases

Identifiers

PMID22106938
PMCPMC3272096

What OpenQuestion holds

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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.