Evidence map›Paper›PMID 15215309›Full record

ArticleMolecular biology of the cell2004

Endocytosis as a mechanism for tyrosine kinase-dependent suppression of a voltage-gated potassium channel.

Edmund Nesti, Brian Everill, Anthony D Morielli

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed.

  1. Article
  2. Article
  3. Competitive modulation of KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  4. Review
  5. Insights of Endocytosis Signaling in Health and Disease.International journal of molecular sciences · 2023
    Review
  6. Review
  7. Comparison of KHandbook of experimental pharmacology · 2021
    Article
  8. Review
  9. Review
  10. Review
  11. Slc7a5 alters Kvβ-mediated regulation of Kv1.2.The Journal of general physiology · 2020
    Article
  12. KFrontiers in cellular neuroscience · 2020
    Review
  13. Article
  14. Review
  15. Article
  16. Molecular mechanism for muscarinic MThe Journal of physiology · 2017
    Article
  17. Article
  18. Article
  19. Unconventional EGF-induced ERK1/2-mediated Kv1.3 endocytosis.Cellular and molecular life sciences : CMLS · 2016
    Article
  20. 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

3 authors.

Edmund NestiThe University of Vermont College of Medicine, Burlington, VT 05405, USA.
Brian Everill
Anthony D Morielli

Funding

Proteomics Core for Neuroscience P20 RR16435P20RR016435 · NCRR · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI MARTIN-CARABALLO, MIGUEL · 2001 to 2010
$23.5M
TUMOR GROWTH AND METASTASISP30CA022435 · NCI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI FOGARTY, JOHN P · 1985 to 2007
$9.6M
NCI NIH HHS P30 CA022435NCI NIH HHS P30CA22435NCRR NIH HHS 1P20RR16435NCRR NIH HHS P20 RR016435
6 · The paper itself

Abstract

The voltage-gated potassium channel Kv1.2 undergoes tyrosine phosphorylation-dependent suppression of its ionic current. However, little is known about the physical mechanism behind that process. We have found that the Kv1.2 alpha-subunit protein undergoes endocytosis in response to the same stimuli that evoke suppression of Kv1.2 ionic current. The process is tyrosine phosphorylation-dependent because the same tyrosine to phenylalanine mutation in the N-terminus of Kv1.2 that confers resistance to channel suppression (Y132F) also confers resistance to channel endocytosis. Overexpression of a dominant negative form of dynamin blocked stimulus-induced Kv1.2 endocytosis and also blocked suppression of Kv1.2 ionic current. These data indicate that endocytosis of Kv1.2 from the cell surface is a key mechanism for channel suppression by tyrosine kinases.

Indexed as

Amino Acid SubstitutionAnimalsAntibodies, MonoclonalCarbacholCell LineDynaminsEndocytosisHumansIn Vitro TechniquesKv1.2 Potassium ChannelMutagenesis, Site-DirectedPotassium Channels, Voltage-GatedProtein-Tyrosine KinasesRatsRecombinant ProteinsTransfectionAntibodies, MonoclonalCarbacholDynaminsKCNA2 protein, humanKcna2 protein, ratKv1.2 Potassium ChannelpervanadatePotassium Channels, Voltage-GatedProtein-Tyrosine KinasesRecombinant ProteinsVanadates

Identifiers

PMID15215309
PMCPMC515342

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.