ArticleProceedings of the National Academy of Sciences of the United States of America2013
Evolution of modular intraflagellar transport from a coatomer-like progenitor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.
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Who cites it
98 citing papers in PubMed, 163 citations in OpenAlex.
- Primary cilia: master conductors of cellular communication in development and disease.Nature reviews. Nephrology · 2026Review
- The photophobic response in the apusomonad Podomonas kaiyoae is mediated by coordination of cilia and actin filaments.Communications biology · 2025Article
- Nuclear genome sequencing reveals the highly intron-rich architecture of the chlorarachniophyte alga Amorphochlora amoebiformis.DNA research : an international journal for rapid publication of reports on genes and genomes · 2025Article
- Article
- Homology search confirms widespread presence of BBSome proteins in Hexapoda with implications for potential non-ciliary BBS protein functions in honey bees.Scientific reports · 2025Article
- Delivery of intraflagellar transport proteins to the ciliary base and assembly into trains.Science advances · 2025Article
- The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025Review
- Two-directional trafficking of the IFT25 protein in the developing mouse sperm flagella.Biology of reproduction · 2025Article
- Proteomic analysis reveals molecular changes following genetic engineering in Chlamydomonas reinhardtii.BMC microbiology · 2024Article
- Evolutionary trajectory for nuclear functions of ciliary transport complex proteins.Microbiology and molecular biology reviews : MMBR · 2024Review
- Matreex: Compact and Interactive Visualization for Scalable Studies of Large Gene Families.Genome biology and evolution · 2024Article
- Transport and barrier mechanisms that regulate ciliary compartmentalization and ciliopathies.Nature reviews. Nephrology · 2024Review
- Deletion of IFT20 exclusively in the RPE ablates primary cilia and leads to retinal degeneration.PLoS biology · 2023Article
- The IFT81-IFT74 complex acts as an unconventional RabL2 GTPase-activating protein during intraflagellar transport.The EMBO journal · 2023Article
- Organization, functions, and mechanisms of the BBSome in development, ciliopathies, and beyond.eLife · 2023Review
- Genome analysis of Parmales, the sister group of diatoms, reveals the evolutionary specialization of diatoms from phago-mixotrophs to photoautotrophs.Communications biology · 2023Article
- Primary cilia as dynamic and diverse signalling hubs in development and disease.Nature reviews. Genetics · 2023Review
- Radial spoke protein 9 is necessary for axoneme assembly in Plasmodium but not in trypanosomatid parasites.Journal of cell science · 2023Article
- Architecture of intraflagellar transport complexes.Nature structural & molecular biology · 2023Article
- A modERN resource: identification of Drosophila transcription factor candidate target genes using RNAi.Genetics · 2023Article
38 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 5 institutions in 4 countries.
Funding
Abstract
The intraflagellar transport (IFT) complex is an integral component of the cilium, a quintessential organelle of the eukaryotic cell. The IFT system consists of three subcomplexes [i.e., intraflagellar transport (IFT)-A, IFT-B, and the BBSome], which together transport proteins and other molecules along the cilium. IFT dysfunction results in diseases collectively called ciliopathies. It has been proposed that the IFT complexes originated from vesicle coats similar to coat protein complex (COP) I, COPII, and clathrin. Here we provide phylogenetic evidence for common ancestry of IFT subunits and α, β', and ε subunits of COPI, and trace the origins of the IFT-A, IFT-B, and the BBSome subcomplexes. We find that IFT-A and the BBSome likely arose from an IFT-B-like complex by intracomplex subunit duplication. The distribution of IFT proteins across eukaryotes identifies the BBSome as a frequently lost, modular component of the IFT. Significantly, loss of the BBSome from a taxon is a frequent precursor to complete cilium loss in related taxa. Given the inferred late origin of the BBSome in cilium evolution and its frequent loss, the IFT complex behaves as a "last-in, first-out" system. The protocoatomer origin of the IFT complex corroborates involvement of IFT components in vesicle transport. Expansion of IFT subunits by duplication and their subsequent independent loss supports the idea of modularity and structural independence of the IFT subcomplexes.
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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.