Evidence map›Paper›PMID 26912790›Full record

ArticleMolecular biology of the cell2016

A prefoldin-associated WD-repeat protein (WDR92) is required for the correct architectural assembly of motile cilia.

Ramila S Patel-King, Stephen M King

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. International journal of molecular sciences · 2023
    Review
  5. Review
  6. Article
  7. Article
  8. Role of the Novel Hsp90 Co-Chaperones in Dynein Arms' Preassembly.International journal of molecular sciences · 2019
    Review
  9. Article
  10. Article
  11. Over-expression of Hsp83 in grossly depletedJournal of biosciences · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. 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

2 authors at 1 institution in 1 country.

Ramila S Patel-KingDepartment of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 06030-3305.
Stephen M KingDepartment of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 06030-3305 Institute for Systems Genomics, University of Connecticut Health Center, Farmington, CT 06030-3305 king@uchc.edu.
UConn Health · US

Funding

MOLECULAR ANALYSIS OF FLAGELLAR DYNEIN FUNCTIONR01GM051293 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI KING, STEPHEN M · 1995 to 2020
$6.9M
NIGMS NIH HHS GM051293NIGMS NIH HHS R01 GM051293
6 · The paper itself

Abstract

WDR92 is a highly conserved WD-repeat protein that has been proposed to be involved in apoptosis and also to be part of a prefoldin-like cochaperone complex. We found that WDR92 has a phylogenetic signature that is generally compatible with it playing a role in the assembly or function of specifically motile cilia. To test this hypothesis, we performed an RNAi-based knockdown of WDR92 gene expression in the planarianSchmidtea mediterraneaand were able to achieve a robust reduction in mRNA expression to levels undetectable under our standard RT-PCR conditions. We found that this treatment resulted in a dramatic reduction in the rate of organismal movement that was caused by a switch in the mode of locomotion from smooth, cilia-driven gliding to muscle-based, peristaltic contractions. Although the knockdown animals still assembled cilia of normal length and in similar numbers to controls, these structures had reduced beat frequency and did not maintain hydrodynamic coupling. By transmission electron microscopy we observed that many cilia had pleiomorphic defects in their architecture, including partial loss of dynein arms, incomplete closure of the B-tubule, and occlusion or replacement of the central pair complex by accumulated electron-dense material. These observations suggest that WDR92 is part of a previously unrecognized cytoplasmic chaperone system that is specifically required to fold key components necessary to build motile ciliary axonemes.

Indexed as

AnimalsAxonemeCiliaGene Knockdown TechniquesHelminth ProteinsMicroscopy, Electron, TransmissionMolecular ChaperonesMultiprotein ComplexesPhylogenyPlanariansRNA InterferenceHelminth ProteinsMolecular ChaperonesMultiprotein Complexesprefoldin

Identifiers

PMID26912790
PMCPMC4831875
OpenAlexW2342316560

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.