Evidence map›Paper›PMID 25349261›Full record

ArticleThe Journal of cell biology2014

Crystal structures of IFT70/52 and IFT52/46 provide insight into intraflagellar transport B core complex assembly.

Michael Taschner, Fruzsina Kotsis, Philipp Braeuer, E Wolfgang Kuehn, Esben Lorentzen

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
8.2field-weighted citation impact, top 2% 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

76 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
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  5. The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025
    Review
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16 more citing papers are in PubMed but not listed here.

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.

Michael TaschnerDepartment of Structural Cell Biology, Max-Planck-Institute of Biochemistry, D-82152 Martinsried, Germany.
Fruzsina KotsisRenal Division, University Hospital Freiburg, D-79106 Freiburg, Germany.
Philipp BraeuerDepartment of Structural Cell Biology, Max-Planck-Institute of Biochemistry, D-82152 Martinsried, Germany.
E Wolfgang KuehnRenal Division, University Hospital Freiburg, D-79106 Freiburg, Germany BIOSS Center for Biological Signaling Studies, Albert-Ludwig-University, 79104 Freiburg, Germany.
Esben LorentzenDepartment of Structural Cell Biology, Max-Planck-Institute of Biochemistry, D-82152 Martinsried, Germany lorentze@biochem.mpg.de.
Max Planck Institute of Biochemistry · DEUniversity Medical Center Freiburg · DE

Funding

European Research Council 310343
6 · The paper itself

Abstract

Cilia are microtubule-based organelles that assemble via intraflagellar transport (IFT) and function as signaling hubs on eukaryotic cells. IFT relies on molecular motors and IFT complexes that mediate the contacts with ciliary cargo. To elucidate the architecture of the IFT-B complex, we reconstituted and purified the nonameric IFT-B core from Chlamydomonas reinhardtii and determined the crystal structures of C. reinhardtii IFT70/52 and Tetrahymena IFT52/46 subcomplexes. The 2.5-Å resolution IFT70/52 structure shows that IFT52330-370 is buried deeply within the IFT70 tetratricopeptide repeat superhelix. Furthermore, the polycystic kidney disease protein IFT88 binds IFT52281-329 in a complex that interacts directly with IFT70/IFT52330-381 in trans. The structure of IFT52C/IFT46C was solved at 2.3 Å resolution, and we show that it is essential for IFT-B core integrity by mediating interaction between IFT88/70/52/46 and IFT81/74/27/25/22 subcomplexes. Consistent with this, overexpression of mammalian IFT52C in MDCK cells is dominant-negative and causes IFT protein mislocalization and disrupted ciliogenesis. These data further rationalize several ciliogenesis phenotypes of IFT mutant strains.

Indexed as

Amino Acid SequenceBinding SitesChlamydomonas reinhardtiiCrystallography, X-RayModels, MolecularMolecular Sequence DataPlant ProteinsProtein Structure, TertiaryProtozoan ProteinsSequence AlignmentTetrahymenaPlant ProteinsProtozoan Proteins

Identifiers

PMID25349261
PMCPMC4210449
OpenAlexW2008047816

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.