Evidence map›Paper›PMID 36932088›Full record

ArticleNature communications2023

Structural insight into the intraflagellar transport complex IFT-A and its assembly in the anterograde IFT train.

Yuanyuan Ma, Jun He, Shaobai Li, Deqiang Yao, Chenhui Huang, Jian Wu, Ming Lei

Open access · goldFull text read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
10.3field-weighted citation impact, top 1% 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

23 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
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  9. Review
  10. Article
  11. Article
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  13. Article
  14. The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025
    Review
  15. Article
  16. Article
  17. Article
  18. AlphaFold two years on: Validation and impact.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Review
  20. Structural determination and modeling of ciliary microtubules.Acta crystallographica. Section D, Structural biology · 2024
    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

7 authors at 2 institutions in 2 countries.

Yuanyuan Ma *Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200011, China.ORCID http://orcid.org/0000-0003-1949-2001
Jun He *Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200011, China.
Shaobai LiNinth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200011, China.
Deqiang YaoRenji Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200032, China.
Chenhui HuangNinth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200011, China.ORCID http://orcid.org/0000-0003-1947-9472
Jian WuNinth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200011, China. wujian@shsmu.edu.cn.ORCID http://orcid.org/0000-0002-2072-0967
Ming LeiNinth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200011, China. leim@shsmu.edu.cn.ORCID http://orcid.org/0000-0002-1153-4791
Shanghai Jiao Tong University · CNShanghai Ninth People's Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intraflagellar transport (IFT) trains, the polymers composed of two multi-subunit complexes, IFT-A and IFT-B, carry out bidirectional intracellular transport in cilia, vital for cilia biogenesis and signaling. IFT-A plays crucial roles in the ciliary import of membrane proteins and the retrograde cargo trafficking. However, the molecular architecture of IFT-A and the assembly mechanism of the IFT-A into the IFT trains in vivo remains elusive. Here, we report the cryo-electron microscopic structures of the IFT-A complex from protozoa Tetrahymena thermophila. We find that IFT-A complexes present two distinct, elongated and folded states. Remarkably, comparison with the in situ cryo-electron tomography structure of the anterograde IFT train unveils a series of adjustments of the flexible arms in apo IFT-A when incorporated into the anterograde train. Our results provide an atomic-resolution model for the IFT-A complex and valuable insights into the assembly mechanism of anterograde IFT trains.

Indexed as

CiliaSignal TransductionBiological TransportCryoelectron MicroscopyElectron Microscope TomographyFlagella

Identifiers

PMID36932088
PMCPMC10023715
OpenAlexW4327811890

What OpenQuestion holds

Textfull text, public
LicenceCC BY
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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.