Evidence map›Paper›PMID 19713751›Full record

ArticleChannels (Austin, Tex.)

Proteomic analyses of native brain K(V)4.2 channel complexes.

Céline Marionneau, Richard D LeDuc, Henry W Rohrs, Andrew J Link, R Reid Townsend, Jeanne M Nerbonne

Abstract read
In one paragraph

Article in Channels (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. A-type KNeuropharmacology · 2018
    Article
  7. A-Type KFrontiers in molecular neuroscience · 2018
    Review
  8. More than a pore: ion channel signaling complexes.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Inhibition of lens photodamage by UV-absorbing contact lenses.Investigative ophthalmology & visual science · 2011
    Article
  19. Review
  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

6 authors.

Céline MarionneauDepartment of Developmental Biology, Washington University, St. Louis, MO, USA.
Richard D LeDuc
Henry W Rohrs
Andrew J Link
R Reid Townsend
Jeanne M Nerbonne

Funding

YOGA LIFESTYLE INTERVENTION REDUCES BLOOD PRESSURE IN HIV-INFECTED ADULTSP41RR000954 · NCRR · WASHINGTON UNIVERSITY · PI GROSS, MICHAEL L · 1985 to 2011
$16.0M
Washington University Center for Translational NeuroscienceP30NS057105 · NINDS · WASHINGTON UNIVERSITY · PI HOLTZMAN, DAVID M. · 2006 to 2011
$8.7M
ION CHANNEL REGULATION AND MODULATION IN CARDIAC MUSCLER01HL034161 · NHLBI · WASHINGTON UNIVERSITY · PI NERBONNE, JEANNE M. · 1986 to 2015
$4.6M
Proteomic Analysis of Eukaryotic Protein SynthesisR01GM064779 · NIGMS · VANDERBILT UNIVERSITY · PI LINK, ANDREW J. · 2002 to 2010
$3.0M
NCRR NIH HHS P41 RR000954NCRR NIH HHS P41RR000954NHLBI NIH HHS R01 HL034161NHLBI NIH HHS R01-HL034161NIGMS NIH HHS R01 GM064779NIGMS NIH HHS R01-GM064779NINDS NIH HHS P30 NS057105NINDS NIH HHS P30-NS057105
6 · The paper itself

Abstract

Somatodendritic A-type (I(A)) voltage-gated K(+) (K(V)) channels are key regulators of neuronal excitability, functioning to control action potential waveforms, repetitive firing and the responses to synaptic inputs. Rapidly activating and inactivating somatodendritic I(A) channels are encoded by K(V)4 alpha subunits and accumulating evidence suggests that these channels function as components of macromolecular protein complexes. Mass spectrometry (MS)-based proteomic approaches were developed and exploited here to identify potential components and regulators of native brain K(V)4.2-encoded I(A) channel complexes. Using anti-K(V)4.2 specific antibodies, K(V)4.2 channel complexes were immunoprecipitated from adult wild type mouse brain. Parallel control experiments were performed on brain samples isolated from (K(V)4.2(-/-)) mice harboring a targeted disruption of the KCND2 (K(V)4.2) locus. Three proteomic strategies were employed: an in-gel approach, coupled to one-dimensional liquid chromatography-tandem MS (1D-LC-MS/MS), and two in-solution approaches, followed by 1D- or 2D-LC-MS/MS. The targeted in-gel 1D-LC-MS/MS analyses demonstrated the presence of the K(V)4 alpha subunits (K(V)4.2, K(V)4.3 and K(V)4.1) and the K(V)4 accessory, KChIP (KChIP1-4) and DPP (DPP6 and 10), proteins in native brain K(V)4.2 channel complexes. The more comprehensive, in-solution approach, coupled to 2D-LC-MS/MS, also called Multidimensional Protein Identification Technology (MudPIT), revealed that additional regulatory proteins, including the K(V) channel accessory subunit K(V)beta1, are also components of native brain K(V)4.2 channel complexes. Additional biochemical and functional approaches will be required to elucidate the physiological roles of these newly identified K(V)4 interacting proteins.

Indexed as

AnimalsBrain ChemistryChromatography, LiquidKv Channel-Interacting ProteinsMiceMice, Mutant StrainsProteomicsShal Potassium ChannelsTandem Mass SpectrometryKv Channel-Interacting ProteinsShal Potassium Channels

Identifiers

PMID19713751
PMCPMC2826169

What OpenQuestion holds

Textmetadata
LicenceTDM
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.