ArticleCell2022
Mechanism of IFT-A polymerization into trains for ciliary transport.
Article in Cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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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.
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.
Who cites it
28 citing papers in PubMed, 47 citations in OpenAlex.
- Structure Makes a Difference: IFT Complex in Ciliary Function and Ciliopathy.Cytoskeleton (Hoboken, N.J.) · 2026Review
- Primary cilia dysfunction: A critical driver of metabolic diseases (Review).International journal of molecular medicine · 2026Review
- Bridging structure and function: artificial intelligence-based modelling of kidney proteins.Nature reviews. Nephrology · 2026Review
- Efficient and Stable Subcellular Protein Labeling inPathogens (Basel, Switzerland) · 2026Article
- A microscopy-based CRISPR screening platform enables organellar functional genomics and illuminates ciliary biology.Developmental cell · 2026Article
- Advances in high-resolution imaging of centrioles and cilia.Journal of cell science · 2025Review
- IFT139 regulates Hedgehog signaling and cilia structure through ciliary protein localization.Biology open · 2025Article
- Recent progress and future challenges in structure-based protein-protein interaction prediction.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Review
- 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 · 2025Article
- Delivery of intraflagellar transport proteins to the ciliary base and assembly into trains.Science advances · 2025Article
- Mutually independent and cilia-independent assembly of IFT-A and IFT-B complexes at mother centriole.Molecular biology of the cell · 2025Article
- An amino acid-resolution interactome for motile cilia identifies the structure and function of ciliopathy protein complexes.Developmental cell · 2025Article
- The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025Review
- Ciliary and Non-Ciliary Roles of IFT88 in Development and Diseases.International journal of molecular sciences · 2025Review
- A defined tubby domain β-barrel surface region of TULP3 mediates ciliary trafficking of diverse cargoes.Molecular biology of the cell · 2025Article
- Article
- Ccrk-Mak/Ick signaling is a ciliary transport regulator essential for retinal photoreceptor survival.Life science alliance · 2024Article
- Article
- Molecular and structural perspectives on protein trafficking to the primary cilium membrane.Biochemical Society transactions · 2024Review
- Structural determination and modeling of ciliary microtubules.Acta crystallographica. Section D, Structural biology · 2024Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Intraflagellar transport (IFT) is the highly conserved process by which proteins are transported along ciliary microtubules by a train-like polymeric assembly of IFT-A and IFT-B complexes. IFT-A is sandwiched between IFT-B and the ciliary membrane, consistent with its putative role in transporting transmembrane and membrane-associated cargoes. Here, we have used single-particle analysis electron cryomicroscopy (cryo-EM) to determine structures of native IFT-A complexes. We show that subcomplex rearrangements enable IFT-A to polymerize laterally on anterograde IFT trains, revealing a cooperative assembly mechanism. Surprisingly, we discover that binding of IFT-A to IFT-B shields the preferred lipid-binding interface from the ciliary membrane but orients an interconnected network of β-propeller domains with the capacity to accommodate diverse cargoes toward the ciliary membrane. This work provides a mechanistic basis for understanding IFT-train assembly and cargo interactions.
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What OpenQuestion holds
Registered trials
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.