Evidence map›Paper›PMID 19361449›Full record

ArticleJournal of molecular biology2009

Pentameric assembly of potassium channel tetramerization domain-containing protein 5.

Irina S Dementieva, Valentina Tereshko, Zoe A McCrossan, Elena Solomaha, Daniel Araki, Chen Xu, Nikolaus Grigorieff, Steve A N Goldstein

Abstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing 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

47 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Structure and dynamics of a pentameric KCTD5/CUL3/Gβγ E3 ubiquitin ligase complex.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The emerging role of the KCTD proteins in cancer.Cell communication and signaling : CCS · 2021
    Review
  14. KCells · 2020
    Article
  15. Targeted protein degradation: expanding the toolbox.Nature reviews. Drug discovery · 2019
    Article
  16. Article
  17. Article
  18. Review
  19. Structural basis for auxiliary subunit KCTD16 regulation of the GABAProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. Golgi Structure and Function in Health, Stress, and Diseases.Results and problems in cell differentiation · 2019
    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

8 authors.

Irina S DementievaDepartment of Pediatrics and Institute of Molecular Pediatric Sciences, University of Chicago, Chicago, IL 60637, USA.
Valentina Tereshko
Zoe A McCrossan
Elena Solomaha
Daniel Araki
Chen Xu
Nikolaus Grigorieff
Steve A N Goldstein

Funding

A New Family of Voltage-gated Potassium Channel Regulaory SubunitsR01NS058505 · NINDS · UNIVERSITY OF CHICAGO · PI GOLDSTEIN, STEVE A N · 2007 to 2011
$2.3M
MinK-related peptides(MiRPs): structure and functionR01GM051851 · NIGMS · YALE UNIVERSITY · PI GOLDSTEIN, STEVE A N · 1996 to 2004
$2.2M
NCI NIH HHS Y1-CO-1020NIGMS NIH HHS R01 GM051851NIGMS NIH HHS Y1-GM-1104NINDS NIH HHS R01 NS058505
6 · The paper itself

Abstract

We report the X-ray crystal structure of human potassium channel tetramerization domain-containing protein 5 (KCTD5), the first member of the family to be so characterized. Four findings were unexpected. First, the structure reveals assemblies of five subunits while tetramers were anticipated; pentameric stoichiometry is observed also in solution by scanning transmission electron microscopy mass analysis and analytical ultracentrifugation. Second, the same BTB (bric-a-brac, tramtrack, broad complex) domain surface mediates the assembly of five KCTD5 and four voltage-gated K(+) (Kv) channel subunits; four amino acid differences appear crucial. Third, KCTD5 complexes have well-defined N- and C-terminal modules separated by a flexible linker that swivels by approximately 30 degrees; the C-module shows a new fold and is required to bind Golgi reassembly stacking protein 55 with approximately 1 microM affinity, as judged by surface plasmon resonance and ultracentrifugation. Fourth, despite the homology reflected in its name, KCTD5 does not impact the operation of Kv4.2, Kv3.4, Kv2.1, or Kv1.2 channels.

Indexed as

Amino Acid SequenceBiopolymersCrystallography, X-RayHumansModels, MolecularMolecular Sequence DataPotassium ChannelsProtein ConformationSequence Homology, Amino AcidStatic ElectricitySurface Plasmon ResonanceBiopolymersKCTD5 protein, humanPotassium Channels

Identifiers

PMID19361449
PMCPMC2670943

What OpenQuestion holds

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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.