Evidence map›Paper›PMID 16571668›Full record

ArticleMolecular biology of the cell2006

Disruption of the A-kinase anchoring domain in flagellar radial spoke protein 3 results in unregulated axonemal cAMP-dependent protein kinase activity and abnormal flagellar motility.

Anne R Gaillard, Laura A Fox, Jeanne M Rhea, Branch Craige, Winfield S Sale

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 57 citations in OpenAlex.

  1. Defective I1 dynein inmicroPublication biology · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Survey of the Ciliary Motility Machinery ofFrontiers in genetics · 2019
    Article
  6. Article
  7. Article
  8. Alcohol-induced ciliary dysfunction targets the outer dynein arm.American journal of physiology. Lung cellular and molecular physiology · 2015
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

Anne R GaillardDepartment of Cell Biology, Emory University School of Medicine, Atlanta, GA 30322, USA.
Laura A Fox
Jeanne M Rhea
Branch Craige
Winfield S Sale
Emory University · US

Funding

Training Program in Biochemistry, Cell and Molecular BiologyT32GM008367 · NIGMS · EMORY UNIVERSITY · PI BOISE, LAWRENCE H., CORBETT, ANITA H. · 1990 to 2019
$5.6M
Functional Substructure of Flagellar DyneinR37GM051173 · NIGMS · EMORY UNIVERSITY · PI SALE, WINFIELD S · 2002 to 2011
$4.0M
NIGMS NIH HHS R37 GM-051173NIGMS NIH HHS R37 GM051173NIGMS NIH HHS T32 GM-008367NIGMS NIH HHS T32 GM008367
6 · The paper itself

Abstract

Biochemical studies of Chlamydomonas flagellar axonemes revealed that radial spoke protein (RSP) 3 is an A-kinase anchoring protein (AKAP). To determine the physiological role of PKA anchoring in the axoneme, an RSP3 mutant, pf14, was transformed with an RSP3 gene containing a mutation in the PKA-binding domain. Analysis of several independent transformants revealed that the transformed cells exhibit an unusual phenotype: a fraction of the cells swim normally; the remainder of the cells twitch feebly or are paralyzed. The abnormal/paralyzed motility is not due to an obvious deficiency of radial spoke assembly, and the phenotype cosegregates with the mutant RSP3. We postulated that paralysis was due to failure in targeting and regulation of axonemal cAMP-dependent protein kinase (PKA). To test this, reactivation experiments of demembranated cells were performed in the absence or presence of PKA inhibitors. Importantly, motility in reactivated cell models mimicked the live cell phenotype with nearly equal fractions of motile and paralyzed cells. PKA inhibitors resulted in a twofold increase in the number of motile cells, rescuing paralysis. These results confirm that flagellar RSP3 is an AKAP and reveal that a mutation in the PKA binding domain results in unregulated axonemal PKA activity and inhibition of normal motility.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCell MovementChlamydomonas reinhardtiiConserved SequenceFlagellaMolecular Sequence DataPlant ProteinsProtozoan ProteinsRegenerationAdaptor Proteins, Signal TransducingPlant ProteinsProtozoan Proteinsradial spoke protein, Chlamydomonas

Identifiers

PMID16571668
PMCPMC1474798
OpenAlexW2159638118

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.