ArticleGenetics2009
Retrograde intraflagellar transport mutants identify complex A proteins with multiple genetic interactions in Chlamydomonas reinhardtii.
Article in Genetics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed, 120 citations in OpenAlex.
- Functions and trafficking mechanisms of RIC-8 inMolecular biology of the cell · 2026Article
- Cell-specific roles for the conserved Galpha chaperone RIC-8 in cilia biology.bioRxiv : the preprint server for biology · 2026Article
- Role of intraflagellar transport protein IFT140 in the formation and function of motile cilia in mammals.Cellular and molecular life sciences : CMLS · 2025Article
- Intraflagellar transport: A critical player in photoreceptor development and the pathogenesis of retinal degenerative diseases.Cytoskeleton (Hoboken, N.J.) · 2024Review
- Article
- Label-free proteomic comparison reveals ciliary and nonciliary phenotypes of IFT-A mutants.Molecular biology of the cell · 2024Article
- Cilia Structure and Function in Human Disease.Current opinion in endocrine and metabolic research · 2024Article
- Primary cilia are critical for tracheoesophageal septation.Developmental dynamics : an official publication of the American Association of Anatomists · 2024Article
- Gene dosage of independent dynein arm motor preassembly factors influences cilia assembly in Chlamydomonas reinhardtii.PLoS genetics · 2024Article
- Structure, function, and research progress of primary cilia in reproductive physiology and reproductive diseases.Frontiers in cell and developmental biology · 2024Review
- Human IFT-A complex structures provide molecular insights into ciliary transport.Cell research · 2023Article
- Structural insight into the intraflagellar transport complex IFT-A and its assembly in the anterograde IFT train.Nature communications · 2023Article
- Appearing and disappearing acts of cilia.Journal of biosciences · 2023Review
- Cilia-Localized Counterregulatory Signals as Drivers of Renal Cystogenesis.Frontiers in molecular biosciences · 2022Review
- A WDR35-dependent coat protein complex transports ciliary membrane cargo vesicles to cilia.eLife · 2021Article
- Patterns of cilia gene dysregulations in major psychiatric disorders.Progress in neuro-psychopharmacology & biological psychiatry · 2021Article
- IFT54 directly interacts with kinesin-II and IFT dynein to regulate anterograde intraflagellar transport.The EMBO journal · 2021Article
- Intraflagellar transport trains and motors: Insights from structure.Seminars in cell & developmental biology · 2020Review
- Cilia in cystic kidney and other diseases.Cellular signalling · 2020Review
- Activation of cryptic splicing in bovine WDR19 is associated with reduced semen quality and male fertility.PLoS genetics · 2020Article
18 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The intraflagellar transport machinery is required for the assembly of cilia. It has been investigated by biochemical, genetic, and computational methods that have identified at least 21 proteins that assemble into two subcomplexes. It has been hypothesized that complex A is required for retrograde transport. Temperature-sensitive mutations in FLA15 and FLA17 show defects in retrograde intraflagellar transport (IFT) in Chlamydomonas. We show that IFT144 and IFT139, two complex A proteins, are encoded by FLA15 and FLA17, respectively. The fla15 allele is a missense mutation in a conserved cysteine and the fla17 allele is an in-frame deletion of three exons. The flagellar assembly defect of each mutant is rescued by the respective transgenes. In fla15 and fla17 mutants, bulges form in the distal one-third of the flagella at the permissive temperature and this phenotype is also rescued by the transgenes. These bulges contain the complex B component IFT74/72, but not alpha-tubulin or p28, a component of an inner dynein arm, which suggests specificity with respect to the proteins that accumulate in these bulges. IFT144 and IFT139 are likely to interact with each other and other proteins on the basis of three distinct genetic tests: (1) Double mutants display synthetic flagellar assembly defects at the permissive temperature, (2) heterozygous diploid strains exhibit second-site noncomplemention, and (3) transgenes confer two-copy suppression. Since these tests show different levels of phenotypic sensitivity, we propose they illustrate different gradations of gene interaction between complex A proteins themselves and with a complex B protein (IFT172).
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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.