Evidence map›Paper›PMID 14871938›Full record

ArticleEukaryotic cell2004

Flagellar radial spoke protein 2 is a calmodulin binding protein required for motility in Chlamydomonas reinhardtii.

Pinfen Yang, Chun Yang, Winfield S Sale

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2004. 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
1.9field-weighted citation impact, top 16% 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, 66 citations in OpenAlex.

  1. Article
  2. Distinct architecture and composition of mouse axonemal radial spoke head revealed by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Axoneme Structure from Motile Cilia.Cold Spring Harbor perspectives in biology · 2017
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Sequential assembly of flagellar radial spokes.Cytoskeleton (Hoboken, N.J.) · 2011
    Article
  17. Article
  18. Article
  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

3 authors at 2 institutions in 1 country.

Pinfen YangDepartment of Biology, Marquette University, Milwaukee, Wisconsin 53233, USA.
Chun Yang
Winfield S Sale
Marquette University · USEmory University · US

Funding

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
REGULATION OF DYNEIN-DRIVEN FLAGELLAR MOTILITYR01GM068101 · NIGMS · MARQUETTE UNIVERSITY · PI YANG, PINFEN · 2003 to 2009
$1.3M
TARGETED ASSEMBLY OF DYNEIN ON FLAGELLAR MICROTUBULESF32GM017666 · NIGMS · EMORY UNIVERSITY · PI YANG, PINFEN · 1995 to 1997
–
NIGMS NIH HHS F32 GM017666NIGMS NIH HHS GM51173NIGMS NIH HHS GM68101NIGMS NIH HHS R01 GM051173NIGMS NIH HHS R01 GM068101NIGMS NIH HHS R37 GM051173
6 · The paper itself

Abstract

Genetic and morphological studies have revealed that the radial spokes regulate ciliary and flagellar bending. Functional and biochemical analysis and the discovery of calmodulin in the radial spokes suggest that the regulatory mechanism involves control of axonemal protein phosphorylation and calcium binding to spoke proteins. To identify potential regulatory proteins in the radial spoke, in-gel kinase assays were performed on isolated axonemes and radial spoke fractions. The results indicated that radial spoke protein 2 (RSP2) can bind ATP and transfer phosphate in vitro. RSP2 was cloned and mapped to the PF24 locus, a gene required for motility. Sequencing revealed that pf24 contains a point mutation converting the first ATG to ATA, resulting in only trace amounts of RSP2 and confirming the RSP2 mapping. Surprisingly, the sequence does not include signature domains for conventional kinases, indicating that RSP2 may not perform as a protein kinase in vivo. However, the predicted RSP2 protein sequence contains Ca2+-dependent calmodulin binding motifs and a GAF domain, a domain found in diverse signaling proteins for binding small ligands including cyclic nucleotides. As predicted from the sequence, recombinant RSP2 binds calmodulin in a calcium-dependent manner. We postulate that RSP2 is a regulatory subunit of the radial spoke involved in localization of calmodulin for control of motility.

Indexed as

Adenosine TriphosphateAmino Acid MotifsAmino Acid SequenceAnimalsBlotting, WesternCalciumCalmodulinCalmodulin-Binding ProteinsChlamydomonas reinhardtiiChromosome MappingCloning, MolecularCyclic AMPDNA, ComplementaryFlagellaLigandsModels, BiologicalAdenosine TriphosphateCalciumCalmodulinCalmodulin-Binding ProteinsCyclic AMPDNA, ComplementaryLigandsPlant ProteinsProtein IsoformsProtozoan Proteinsradial spoke protein, ChlamydomonasRecombinant Proteins

Identifiers

PMID14871938
PMCPMC329519
OpenAlexW2141020972

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.