Evidence map›Paper›PMID 36462505›Full record

ArticleCell2022

IFT-A structure reveals carriages for membrane protein transport into cilia.

Sophie J Hesketh, Aakash G Mukhopadhyay, Dai Nakamura, Katerina Toropova, Anthony J Roberts

Open access · hybridAbstract read
PubMed Publisher
In one paragraph

Article in Cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
14.4field-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

49 citing papers in PubMed, 80 citations in OpenAlex.

  1. Review
  2. Review
  3. Primary cilia dysfunction: A critical driver of metabolic diseases (Review).International journal of molecular medicine · 2026
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Design principles of ciliary signaling.Journal of cell science · 2025
    Review
  9. Review
  10. Review
  11. Regulation of kinesin-2 motility by its β-hairpin motif.Nature structural & molecular biology · 2025
    Article
  12. Ciliary ARL13B Is Essential for Vision and Morphogenesis of Cone Outer Segments.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
  13. Characterizing the ADPKD-Kidney international reports · 2025
    Article
  14. Article
  15. Article
  16. Intraflagellar transport trains can switch rails and move along multiple microtubules in intact primary cilia.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Article
  19. The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025
    Review
  20. Ciliary and Non-Ciliary Roles of IFT88 in Development and Diseases.International journal of molecular sciences · 2025
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Sophie J HeskethInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck University of London, London, WC1E 7HX, UK.
Aakash G MukhopadhyayInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck University of London, London, WC1E 7HX, UK.
Dai NakamuraInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck University of London, London, WC1E 7HX, UK.
Katerina ToropovaInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck University of London, London, WC1E 7HX, UK. Electronic address: e.toropova@bbk.ac.uk.
Anthony J RobertsInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck University of London, London, WC1E 7HX, UK. Electronic address: anthony.roberts@bbk.ac.uk.
Institute of Structural and Molecular Biology · GB

Funding

Biotechnology and Biological Sciences Research Council BB/S007202/1Wellcome Trust 202679/Z/16/ZWellcome Trust 206166/Z/17/ZWellcome Trust 217186/Z/19/Z
6 · The paper itself

Abstract

Intraflagellar transport (IFT) trains are massive molecular machines that traffic proteins between cilia and the cell body. Each IFT train is a dynamic polymer of two large complexes (IFT-A and -B) and motor proteins, posing a formidable challenge to mechanistic understanding. Here, we reconstituted the complete human IFT-A complex and obtained its structure using cryo-EM. Combined with AlphaFold prediction and genome-editing studies, our results illuminate how IFT-A polymerizes, interacts with IFT-B, and uses an array of β-propeller and TPR domains to create "carriages" of the IFT train that engage TULP adaptor proteins. We show that IFT-A⋅TULP carriages are essential for cilia localization of diverse membrane proteins, as well as ICK-the key kinase regulating IFT train turnaround. These data establish a structural link between IFT-A's distinct functions, provide a blueprint for IFT-A in the train, and shed light on how IFT evolved from a proto-coatomer ancestor.

Indexed as

CiliaKinesinsBiological TransportDyneinsFlagellaHumansMembrane ProteinsProtein TransportDyneinsKinesinsMembrane ProteinsAlphaFoldCiliaCOPICryo-EMG-Protein Coupled ReceptorIntraflagellar TransportMembrane ProteinMicrotubuleMotor ProteinTULP3

Identifiers

PMID36462505
OpenAlexW4310668128

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.