Evidence map›Paper›PMID 22851692›Full record

ArticleMolecular and cellular biology2012

The DPY-30 domain and its flanking sequence mediate the assembly and modulation of flagellar radial spoke complexes.

Radhika Gopal, Kenneth W Foster, Pinfen Yang

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.5field-weighted citation impact, top 30% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Functional Diversity and Emerging Roles of Human NME/NDPK Group II Proteins.International journal of molecular sciences · 2026
    Review
  2. Heterogeneity of radial spoke components in Tetrahymena cilia.Cellular and molecular life sciences : CMLS · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Nme family of proteins--clues from simple animals.Naunyn-Schmiedeberg's archives of pharmacology · 2015
    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

3 authors at 2 institutions in 1 country.

Radhika GopalDepartment of Biological Sciences, Marquette University, Milwaukee, WI, USA.
Kenneth W Foster
Pinfen Yang
Marquette University · USSyracuse University · US

Funding

REGULATION OF DYNEIN-DRIVEN FLAGELLAR MOTILITYR01GM068101 · NIGMS · MARQUETTE UNIVERSITY · PI YANG, PINFEN · 2003 to 2009
$1.3M
Biomechanics of the axonemal nanomachineR15GM090162 · NIGMS · MARQUETTE UNIVERSITY · PI YANG, PINFEN · 2010 to 2010
$224k
NIGMS NIH HHS GM068101NIGMS NIH HHS GM068101-05A1NIGMS NIH HHS R01 GM068101NIGMS NIH HHS R15 GM090162
6 · The paper itself

Abstract

RIIa is known as the dimerization and docking (D/D) domain of the cyclic AMP (cAMP)-dependent protein kinase. However, numerous molecules, including radial spoke protein 2 (RSP2) in Chlamydomonas flagella, also contain an RIIa or a similar DPY-30 domain. To elucidate new roles of D/D domain-containing proteins, we investigated a panel of RSP2 mutants. An RSP2 mutant had paralyzed flagella defective in RSP2 and multiple subunits near the spokehead. New transgenic strains lacking only the DPY-30 domain in RSP2 were also paralyzed. In contrast, motility was restored in strains that lacked only RSP2's calmodulin-binding C-terminal region. These cells swam normally in dim light but could not maintain typical swimming trajectories under bright illumination. In both deletion transgenic strains, the subunits near the spokehead were restored, but their firm attachment to the spokestalk required the DPY-30 domain. We postulate that the DPY-30-helix dimer is a conserved two-prong linker, required for normal motility, organizing duplicated subunits in the radial spoke stalk and formation of a symmetrical spokehead. Further, the dispensable calmodulin-binding region appears to fine-tune the spokehead for regulation of "steering" motility in the green algae. Thus, in general, D/D domains may function to localize molecular modules for both the assembly and modulation of macromolecular complexes.

Indexed as

Amino Acid SequenceAnimalsCell MovementChlamydomonasCyclic AMP-Dependent Protein KinasesFlagellaHumansModels, MolecularMolecular Sequence DataPlant ProteinsProtein Structure, SecondaryProtein Structure, TertiarySequence AlignmentCyclic AMP-Dependent Protein KinasesPlant Proteins

Identifiers

PMID22851692
PMCPMC3457544
OpenAlexW2155449053

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.