Evidence map›Paper›PMID 25739456›Full record

ArticleMolecular biology of the cell2015

The C-terminus SH3-binding domain of Kv1.3 is required for the actin-mediated immobilization of the channel via cortactin.

Peter Hajdu, Geoffrey V Martin, Ameet A Chimote, Orsolya Szilagyi, Koichi Takimoto, Laura Conforti

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. A Meta-Analysis Study to Infer Voltage-Gated KAntioxidants (Basel, Switzerland) · 2023
    Article
  7. Cortactin in Lung Cell Function and Disease.International journal of molecular sciences · 2022
    Review
  8. Article
  9. Modulation of Lymphocyte Potassium Channel KACS pharmacology & translational science · 2020
    Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. 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

6 authors at 3 institutions in 3 countries.

Peter HajduDivision of Nephrology and Hypertension, Department of Internal Medicine, University of Cincinnati, Cincinnati, OH 45267 Department of Biophysics and Cell Biology, University of Debrecen, 4032 Debrecen, Hungary.
Geoffrey V MartinDivision of Nephrology and Hypertension, Department of Internal Medicine, University of Cincinnati, Cincinnati, OH 45267.
Ameet A ChimoteDivision of Nephrology and Hypertension, Department of Internal Medicine, University of Cincinnati, Cincinnati, OH 45267.
Orsolya SzilagyiDivision of Nephrology and Hypertension, Department of Internal Medicine, University of Cincinnati, Cincinnati, OH 45267 Department of Biophysics and Cell Biology, University of Debrecen, 4032 Debrecen, Hungary.
Koichi TakimotoDepartment of Bioengineering and Bioinformatics, Nagaoka University of Technology, Nagaoka 940-2137, Japan.
Laura ConfortiDivision of Nephrology and Hypertension, Department of Internal Medicine, University of Cincinnati, Cincinnati, OH 45267 laura.conforti@uc.edu.
University of Cincinnati · USUniversity of Debrecen · HUNagaoka University of Technology · JP

Funding

Hypoxia and Potassium Channel Activity in T LymphocytesR01CA095286 · NCI · UNIVERSITY OF CINCINNATI · PI CONFORTI, LAURA · 2003 to 2019
$4.1M
NCI NIH HHS R01 CA095286
6 · The paper itself

Abstract

Kv1.3 channels play a pivotal role in the activation and migration of T-lymphocytes. These functions are accompanied by the channels' polarization, which is essential for associated downstream events. However, the mechanisms that govern the membrane movement of Kv1.3 channels remain unclear. F-actin polymerization occurs concomitantly to channel polarization, implicating the actin cytoskeleton in this process. Here we show that cortactin, a factor initiating the actin network, controls the membrane mobilization of Kv1.3 channels. FRAP with EGFP-tagged Kv1.3 channels demonstrates that knocking down cortactin decreases the actin-based immobilization of the channels. Using various deletion and mutation constructs, we show that the SH3 motif of Kv1.3 mediates the channel immobilization. Proximity ligation assays indicate that deletion or mutation of the SH3 motif also disrupts interaction of the channel with cortactin. In T-lymphocytes, the interaction between HS1 (the cortactin homologue) and Kv1.3 occurs at the immune synapse and requires the channel's C-terminal domain. These results show that actin dynamics regulates the membrane motility of Kv1.3 channels. They also provide evidence that the SH3 motif of the channel and cortactin plays key roles in this process.

Indexed as

Actin CytoskeletonAdaptor Proteins, Signal TransducingAmino Acid SequenceBinding SitesBlood ProteinsCortactinFluorescence Recovery After PhotobleachingHEK293 CellsHumansImmunological SynapsesKineticsKv1.3 Potassium ChannelMolecular Sequence DataProtein Transportsrc Homology DomainsT-LymphocytesAdaptor Proteins, Signal TransducingBlood ProteinsCortactinHCLS1 protein, humanKv1.3 Potassium Channel

Identifiers

PMID25739456
PMCPMC4436776
OpenAlexW2151691661

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.