Evidence map›Paper›PMID 16123112›Full record

ArticleThe Journal of physiology2005

Multiprotein assembly of Kv4.2, KChIP3 and DPP10 produces ternary channel complexes with ISA-like properties.

Henry H Jerng, Kumud Kunjilwar, Paul J Pfaffinger

Open access · greenAbstract readComparative Study
In one paragraph

Article in The Journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

90 citing papers in PubMed, 129 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Review
  6. Competitive modulation of KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  7. Calcium-Dependent Regulation of Neuronal Excitability Is Rescued in Fragile X Syndrome by a Tat-Conjugated N-Terminal Fragment of FMRP.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  8. KCells · 2023
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Kv4.2 autism and epilepsy mutation enhances inactivation of closed channels but impairs access to inactivated state after opening.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article

30 more citing papers are in PubMed but not listed here.

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 at 2 institutions in 1 country.

Henry H JerngDepartment of Neuroscience, Baylor College of Medicine, One Baylor Plaza, S630, Houston, TX 77030, USA. hjerng@cns.bcm.tmc.edu
Kumud Kunjilwar
Paul J Pfaffinger
Baylor College of Medicine · USThe University of Texas Health Science Center at Houston · US

Funding

Regulation of Neuronal Excitability (P01)P01NS037444 · NINDS · UNIVERSITY OF TEXAS AUSTIN · PI JOHNSTON, DANIEL · 1999 to 2008
$8.4M
FUNCTIONAL DOMAINS OF POTASSIUM CHANNEL SUBUNIT PROTEINSR01NS031583 · NINDS · BAYLOR COLLEGE OF MEDICINE · PI PFAFFINGER, PAUL · 1993 to 2004
$1.8M
NINDS NIH HHS P01 NS037444NINDS NIH HHS P01 NS37444NINDS NIH HHS R01 NS031583NINDS NIH HHS R01 NS31583
6 · The paper itself

Abstract

Kv4 pore-forming subunits are the principal constituents of the voltage-gated K+ channel underlying somatodendritic subthreshold A-type currents (I(SA)) in neurones. Two structurally distinct types of Kv4 channel modulators, Kv channel-interacting proteins (KChIPs) and dipeptidyl-peptidase-like proteins (DPLs: DPP6 or DPPX, DPP10 or DPPY), enhance surface expression and modify functional properties. Since KChIP and DPL distributions overlap in the brain, we investigated the potential coassembly of Kv4.2, KChIP3 and DPL proteins, and the contribution of DPLs to ternary complex properties. Immunoprecipitation results show that KChIP3 and DPP10 associate simultaneously with Kv4.2 proteins in rat brain as well as heterologously expressing Xenopus oocytes, indicating Kv4.2 + KChIP3 + DPP10 multiprotein complexes. Consistent with ternary complex formation, coexpression of Kv4.2, KChIP3 and DPP10 in oocytes and CHO cells results in current waveforms distinct from the arithmetic sum of Kv4.2 + KChIP3 and Kv4.2 + DPP10 currents. Furthermore, the Kv4.2 + KChIP3 + DPP10 channels recover from inactivation very rapidly (tau(rec) approximately 18-26 ms), closely matching that of native I(SA) and significantly faster than the recovery of Kv4.2 + KChIP3 or Kv4.2 + DPP10 channels. For comparison, identical triple coexpression experiments were performed using DPP6 variants. While most results are similar, the Kv4.2 + KChIP3 + DPP6 channels exhibit inactivation that slows with increasing membrane potential, resulting in inactivation slower than that of Kv4.2 + KChIP3 + DPP10 channels at positive voltages. In conclusion, the native neuronal subthreshold A-type channel is probably a macromolecular complex formed from Kv4 and a combination of both KChIP and DPL proteins, with the precise composition of channel alpha and auxiliary subunits underlying tissue and regional variability in I(SA) properties.

Indexed as

AnimalsCells, CulturedCHO CellsCricetinaeCricetulusDipeptidyl-Peptidases and Tripeptidyl-PeptidasesIon Channel GatingKv Channel-Interacting ProteinsMembrane PotentialsMultiprotein ComplexesOocytesPotassiumRatsShal Potassium ChannelsXenopus laevisDipeptidyl-Peptidases and Tripeptidyl-PeptidasesDPP10 protein, humanKv Channel-Interacting ProteinsMultiprotein ComplexesPotassiumShal Potassium Channels

Identifiers

PMID16123112
PMCPMC1464192
OpenAlexW1734472624

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.