Evidence map›Paper›PMID 15304520›Full record

ArticleMolecular biology of the cell2004

The LC7 light chains of Chlamydomonas flagellar dyneins interact with components required for both motor assembly and regulation.

Linda M DiBella, Miho Sakato, Ramila S Patel-King, Gregory J Pazour, Stephen M King

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

31 citing papers in PubMed, 63 citations in OpenAlex.

  1. Review
  2. Asymmetries in the cilia ofPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Ciliary Motility: Regulation of Axonemal Dynein Motors.Cold Spring Harbor perspectives in biology · 2017
    Review
  8. Article
  9. Article
  10. Article
  11. Cooperative binding of the outer arm-docking complex underlies the regular arrangement of outer arm dynein in the axoneme.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Integrated control of axonemal dynein AAA(+) motors.Journal of structural biology · 2012
    Review
  17. 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
  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

5 authors at 2 institutions in 1 country.

Linda M DiBellaDepartment of Biochemistry, University of Connecticut Health Center, Farmington, CT 06030-3305, USA.
Miho Sakato
Ramila S Patel-King
Gregory J Pazour
Stephen M King
UConn Health · USUniversity of Massachusetts Chan Medical School · 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 GM-51293NIGMS NIH HHS R01 GM051293
6 · The paper itself

Abstract

Members of the LC7/Roadblock family of light chains (LCs) have been found in both cytoplasmic and axonemal dyneins. LC7a was originally identified within Chlamydomonas outer arm dynein and associates with this motor's cargo-binding region. We describe here a novel member of this protein family, termed LC7b that is also present in the Chlamydomonas flagellum. Levels of LC7b are reduced approximately 20% in axonemes isolated from strains lacking inner arm I1 and are approximately 80% lower in the absence of the outer arms. When both dyneins are missing, LC7b levels are diminished to <10%. In oda9 axonemal extracts that completely lack outer arms, LC7b copurifies with inner arm I1, whereas in ida1 extracts that are devoid of I1 inner arms it associates with outer arm dynein. We also have observed that some LC7a is present in both isolated axonemes and purified 18S dynein from oda1, suggesting that it is also a component of both the outer arm and inner arm I1. Intriguingly, in axonemal extracts from the LC7a null mutant, oda15, which assembles approximately 30% of its outer arms, LC7b fails to copurify with either dynein, suggesting that it interacts with LC7a. Furthermore, both the outer arm gamma heavy chain and DC2 from the outer arm docking complex completely dissociate after salt extraction from oda15 axonemes. EDC cross-linking of purified dynein revealed that LC7b interacts with LC3, an outer dynein arm thioredoxin; DC2, an outer arm docking complex component; and also with the phosphoprotein IC138 from inner arm I1. These data suggest that LC7a stabilizes both the outer arms and inner arm I1 and that both LC7a and LC7b are involved in multiple intradynein interactions within both dyneins.

Indexed as

Amino Acid SequenceAnimalsCarrier ProteinsChlamydomonas reinhardtiiDyneinsFlagellaHumansMolecular Motor ProteinsMolecular Sequence DataPhylogenyPlant ProteinsProtein IsoformsProtozoan ProteinsRecombinant Fusion ProteinsCarrier ProteinsDyneinsLC7 protein, ChlamydomonasMolecular Motor ProteinsPlant ProteinsProtein IsoformsProtozoan ProteinsRecombinant Fusion Proteins

Identifiers

PMID15304520
PMCPMC519155
OpenAlexW2107854855

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.