Evidence map›Paper›PMID 23427265›Full record

ArticleMolecular biology of the cell2013

The N-DRC forms a conserved biochemical complex that maintains outer doublet alignment and limits microtubule sliding in motile axonemes.

Raqual Bower, Douglas Tritschler, Kristyn Vanderwaal, Catherine A Perrone, Joshua Mueller, Laura Fox, Winfield S Sale, M E Porter

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing 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

85 citing papers in PubMed.

  1. Article
  2. Axonemal dynein contributions to flagellar beat types and waveforms.bioRxiv : the preprint server for biology · 2025
    Article
  3. Observational
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Structural determination and modeling of ciliary microtubules.Acta crystallographica. Section D, Structural biology · 2024
    Review
  11. Article
  12. Article
  13. Article
  14. International journal of molecular sciences · 2023
    Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

25 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

8 authors.

Raqual BowerDepartment of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, MN 55455, USA.
Douglas Tritschler
Kristyn Vanderwaal
Catherine A Perrone
Joshua Mueller
Laura Fox
Winfield S Sale
M E Porter

Funding

Assembly, Targeting, And Regulation Of Dynein MotorsR01GM055667 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI PORTER, MARY E. · 1997 to 2023
$5.4M
Assembly , Targeting, and Regulation of Dynein MotorsR37GM055667 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI PORTER, MARY E. · 2005 to 2014
$4.0M
Functional Substructure of Flagellar DyneinR37GM051173 · NIGMS · EMORY UNIVERSITY · PI SALE, WINFIELD S · 2002 to 2011
$4.0M
FUNCTIONAL SUBSTRUCTURE OF FLAGELLAR DYNEINR01GM051173 · NIGMS · EMORY UNIVERSITY · PI SALE, WINFIELD S · 1994 to 2020
$3.6M
NIGMS NIH HHS GM-051173NIGMS NIH HHS GM-055667NIGMS NIH HHS R01 GM051173NIGMS NIH HHS R01 GM055667NIGMS NIH HHS R37 GM051173NIGMS NIH HHS R37 GM055667
6 · The paper itself

Abstract

The nexin-dynein regulatory complex (N-DRC) is proposed to coordinate dynein arm activity and interconnect doublet microtubules. Here we identify a conserved region in DRC4 critical for assembly of the N-DRC into the axoneme. At least 10 subunits associate with DRC4 to form a discrete complex distinct from other axonemal substructures. Transformation of drc4 mutants with epitope-tagged DRC4 rescues the motility defects and restores assembly of missing DRC subunits and associated inner-arm dyneins. Four new DRC subunits contain calcium-signaling motifs and/or AAA domains and are nearly ubiquitous in species with motile cilia. However, drc mutants are motile and maintain the 9 + 2 organization of the axoneme. To evaluate the function of the N-DRC, we analyzed ATP-induced reactivation of isolated axonemes. Rather than the reactivated bending observed with wild-type axonemes, ATP addition to drc-mutant axonemes resulted in splaying of doublets in the distal region, followed by oscillatory bending between pairs of doublets. Thus the N-DRC provides some but not all of the resistance to microtubule sliding and helps to maintain optimal alignment of doublets for productive flagellar motility. These findings provide new insights into the mechanisms that regulate motility and further highlight the importance of the proximal region of the axoneme in generating flagellar bending.

Indexed as

Amino Acid SequenceAxonemal DyneinsAxonemeChlamydomonas reinhardtiiConserved SequenceDNA Transposable ElementsFlagellaMicrotubulesMolecular Sequence DataMutagenesis, InsertionalPlant ProteinsProtein Interaction MappingSequence Homology, Amino AcidSorting NexinsAxonemal DyneinsDNA Transposable ElementsPlant ProteinsSorting Nexins

Identifiers

PMID23427265
PMCPMC3623635

What OpenQuestion holds

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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.