ArticleNature communications2018
Membrane association and remodeling by intraflagellar transport protein IFT172.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 35 citations in OpenAlex.
- Intraflagellar transport-20 guides the ciliary membrane trafficking of channelrhodopsin in Chlamydomonas reinhardtii.Molecular biology reports · 2026Article
- Research Progress on the Pathogenesis and Diagnostic and Therapeutic Potential of Ciliopathies Regulated by IFT172.Clinical genetics · 2026Review
- Article
- FGFR2 residence in primary cilia is necessary for epithelial cell signaling.The Journal of cell biology · 2025Article
- The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025Review
- Structure, function, and research progress of primary cilia in reproductive physiology and reproductive diseases.Frontiers in cell and developmental biology · 2024Review
- The molecular structure of IFT-A and IFT-B in anterograde intraflagellar transport trains.Nature structural & molecular biology · 2023Article
- Ciliogenesis membrane dynamics and organization.Seminars in cell & developmental biology · 2023Review
- Primary cilia-associated protein IFT172 in ciliopathies.Frontiers in cell and developmental biology · 2023Review
- Biochemically validated structural model of the 15-subunit intraflagellar transport complex IFT-B.The EMBO journal · 2022Article
- Composition, organization and mechanisms of the transition zone, a gate for the cilium.EMBO reports · 2022Review
- A WDR35-dependent coat protein complex transports ciliary membrane cargo vesicles to cilia.eLife · 2021Article
- Novel alterations in IFT172 and KIFAP3 may induce basal cell carcinoma.Orphanet journal of rare diseases · 2021Article
- Kinesin-2 transports Orco into the olfactory cilium of Drosophila melanogaster at specific developmental stages.PLoS genetics · 2021Article
- Intraflagellar Transport Proteins as Regulators of Primary Cilia Length.Frontiers in cell and developmental biology · 2021Review
- Recent advances in understanding assembly of the primary cilium membrane.Faculty reviews · 2021Review
- FtsZ Reorganization Facilitates Deformation of Giant Vesicles in Microfluidic Traps*.Angewandte Chemie (International ed. in English) · 2020Article
- Structural insights into the architecture and assembly of eukaryotic flagella.Microbial cell (Graz, Austria) · 2020Review
- Murine germ cell-specific disruption of Ift172 causes defects in spermiogenesis and male fertility.Reproduction (Cambridge, England) · 2020Article
- Review: Intraflagellar transport proteins in the retina.Molecular vision · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 4 countries.
Funding
Abstract
The cilium is an organelle used for motility and cellular signaling. Intraflagellar transport (IFT) is a process to move ciliary building blocks and signaling components into the cilium. How IFT controls the movement of ciliary components is currently poorly understood. IFT172 is the largest IFT subunit essential for ciliogenesis. Due to its large size, the characterization of IFT172 has been challenging. Using giant unilamellar vesicles (GUVs), we show that IFT172 is a membrane-interacting protein with the ability to remodel large membranes into small vesicles. Purified IFT172 has an architecture of two globular domains with a long rod-like protrusion, resembling the domain organization of coatomer proteins such as COPI-II or clathrin. IFT172 adopts two different conformations that can be manipulated by lipids or detergents: 1) an extended elongated conformation and 2) a globular closed architecture. Interestingly, the association of IFT172 with membranes is mutually exclusive with IFT57, implicating multiple functions for IFT172 within IFT.
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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.