Evidence map›Paper›PMID 19382199›Full record

ArticleCell motility and the cytoskeleton2009

HA-tagging of putative flagellar proteins in Chlamydomonas reinhardtii identifies a novel protein of intraflagellar transport complex B.

Karl-Ferdinand Lechtreck, Scott Luro, Junya Awata, George B Witman

Abstract read
In one paragraph

Article in Cell motility and the cytoskeleton, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

43 citing papers in PubMed, 68 citations in OpenAlex.

  1. Review
  2. Article
  3. Unraveling the intricate cargo-BBSome coupling mechanism at the ciliary tip.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Biology open · 2017
    Article
  15. Article
  16. Ciliary Motility: Regulation of Axonemal Dynein Motors.Cold Spring Harbor perspectives in biology · 2017
    Review
  17. Article
  18. Article
  19. The Intraflagellar Transport Machinery.Cold Spring Harbor perspectives in biology · 2016
    Review
  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

4 authors at 1 institution in 1 country.

Karl-Ferdinand LechtreckDepartment of Cell Biology, University of Massachusetts Medical School, Worcester, Massachusetts, USA. karl.lechtreck@umassmed.edu
Scott Luro
Junya Awata
George B Witman
University of Massachusetts Chan Medical School · US

Funding

Flagellar Motility and AssemlbyR37GM030626 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI WITMAN, GEORGE B · 2007 to 2016
$6.3M
MOLECULAR MECHANISM OF FLAGELLAR MOTILITYR01GM030626 · NIGMS · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI WITMAN, GEORGE B · 1985 to 2006
$3.0M
NIGMS NIH HHS GM30626NIGMS NIH HHS R01 GM030626NIGMS NIH HHS R37 GM030626
6 · The paper itself

Abstract

Proteomic analysis of flagella from the green alga Chlamydomonas reinhardtii has identified over 600 putative flagellar proteins. The genes encoding nine of these not previously characterized plus the previously described PACRG protein were cloned, inserted into a vector adding a triple-HA tag to the C-terminus of the gene product, and transformed into C. reinhardtii. Expression was confirmed by western blotting. Indirect immunofluorescence located all 10 fusion proteins in the flagellum; PACRG was localized to a subset of outer doublet microtubules. For some proteins, additional signal was observed in the cell body. Among the latter was FAP232-HA, which showed a spotted distribution along the flagella and an accumulation at the basal bodies. This pattern is characteristic for intraflagellar transport (IFT) proteins. FAP232-HA co-localized with the IFT protein IFT46 and co-sedimented with IFT particles in sucrose gradients. Furthermore, it co-immunoprecipitated with IFT complex B protein IFT46, but not with IFT complex A protein IFT139. We conclude that FAP232 is a novel component of IFT complex B and rename it IFT25. Homologues of IFT25 are encoded in the genomes of a subset of organisms that assemble cilia or flagella; C. reinhardtii IFT25 is 37% identical to the corresponding human protein. Genes encoding IFT25 homologues are absent from the genomes of organisms that lack cilia and flagella and, interestingly, also from those of Drosophila melanogaster and Caenorhabditis elegans, suggesting that IFT25 has a specialized role in IFT that is not required for the assembly of cilia or flagella in the worm and fly. Cell Motil. Cytoskeleton 2009. (c) 2009 Wiley-Liss, Inc.

Indexed as

Amino Acid SequenceAnimalsBlotting, WesternChlamydomonas reinhardtiiFlagellaFluorescent Antibody Technique, IndirectImmunoprecipitationModels, GeneticMolecular Sequence DataPolymerase Chain ReactionProtein BindingProtozoan ProteinsRecombinant Fusion ProteinsSequence Homology, Amino AcidProtozoan ProteinsRecombinant Fusion Proteins

Identifiers

PMID19382199
PMCPMC2922027
OpenAlexW2084945515

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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.