GO:0036159 inner dynein arm assembly: Ciliary Motility Complex, Genes, Functions and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0036159 (inner dynein arm assembly) describes the aggregation, arrangement and bonding of components that form the axonemal inner dynein arm on outer doublet microtubules of cilia and flagella.
• Inner dynein arms are multi-subunit motor complexes; in Chlamydomonas the I1 dynein (two-headed) and several single-headed inner arm dyneins (a-g) are the best-characterized examples.
• Assembly is not a single event: subunits are preassembled in the cytoplasm and then transported by intraflagellar transport (IFT) before docking onto the axoneme, as shown for the I1 dynein.
• Dedicated assembly factors such as MBO2/FAP58, FAP57/WDR65 and the preassembly machinery determine which inner arm dyneins are built and where they dock [5,6,7].
• Loss of inner dynein arm components or their assembly factors causes primary ciliary dyskinesia (PCD) with ciliary beat abnormalities; variants in CCDC39 and CCDC40 lead to axonemal absence of inner dynein arm heavy chains DNAH1, DNAH6 and DNAH7.
• CRISPR-based knockout, point-mutation, knock-in and overexpression models in Chlamydomonas, mammalian cells and animal models are key tools for dissecting inner dynein arm assembly [1,4,5].
Description
Inner dynein arm assembly (GO:0036159) is the biological process by which a set of protein components is aggregated, arranged and bonded together to form an axonemal dynein inner arm, an inner arm structure present on the outer doublet microtubules of ciliary and flagellar axonemes. Inner dynein arms are the motors that generate the asymmetric, waveform-defining forces of cilia and flagella, and their correct assembly is therefore essential for motile cilia function in processes such as mucociliary clearance and sperm motility [3,5]. The term is used by researchers who study ciliary motility, primary ciliary dyskinesia and the cell biology of axonemal dynein complexes [1,3]. Unlike the outer dynein arm, which is a relatively uniform complex, the inner dynein arm system comprises multiple distinct dynein species, including the two-headed I1 dynein and several single-headed inner arm dyneins, each with its own subunit composition and assembly requirements. Work in Chlamydomonas reinhardtii has shown that inner arm dynein subunits are preassembled in the cytoplasm and then transported into the cilium by intraflagellar transport before docking onto the axoneme, so GO:0036159 encompasses both cytoplasmic preassembly steps and axonemal docking steps. Because inner dynein arm assembly is a multi-step, factor-dependent process, it is a productive entry point for genetics and cell biology: mutations in dynein subunits or in dedicated assembly factors such as MBO2/FAP58 and FAP57/WDR65 disrupt specific inner arm dyneins and alter ciliary waveform [5,6,7]. In humans, defects in inner dynein arm assembly are linked to primary ciliary dyskinesia, and disease-causing variants in CCDC39 and CCDC40 cause axonemal absence of inner dynein arm heavy chains DNAH1, DNAH6 and DNAH7. This makes GO:0036159 directly relevant to diagnostic and mechanistic studies of motile ciliopathies [1,3].
inner dynein arm assembly At A Glance
| GO ID | GO:0036159 |
|---|---|
| GO term | inner dynein arm assembly |
| Ontology | biological_process |
| Synonym | IDA assembly |
| Definition | The aggregation, arrangement and bonding together of a set of components to form an axonemal dynein inner arm, an inner arm structure present on the outer doublet microtubules of ciliary and flagellar axonemes. |
| Major function | Builds inner dynein arm motor complexes that generate and shape ciliary and flagellar beating. |
| Location | Outer doublet microtubules of ciliary and flagellar axonemes. |
| Key example complex | I1 dynein, a two-headed inner arm dynein, plus single-headed inner arm dyneins. |
| Related disease | Primary ciliary dyskinesia (PCD) and other motile ciliopathies. |
What Is GO:0036159?
In plain terms, GO:0036159 describes the construction of the inner dynein arm, a motor structure that sits on the outer doublet microtubules inside cilia and flagella. The definition covers the aggregation, arrangement and bonding together of a set of components to form an axonemal dynein inner arm. It is a biological_process term, and its synonym is IDA assembly. The process includes both the assembly of inner arm dynein subunits into complexes and their placement on the axonemal doublet microtubules, as demonstrated for the I1 dynein, which is assembled in the cytoplasm and transported by IFT before axonemal docking.
Why Is inner dynein arm assembly Important in Cell Biology?
GO:0036159 matters because inner dynein arms are the motors that convert ATP hydrolysis into the asymmetric bending that defines ciliary and flagellar waveforms, and because failure to assemble them correctly is a direct cause of human motile ciliopathy [1,3]. The process is also mechanistically informative: it requires cytoplasmic preassembly, intraflagellar transport and axonemal docking, so it connects dynein motor biology to the broader cell biology of cilia. In addition, dedicated assembly factors such as MBO2/FAP58 and FAP57/WDR65 show that inner arm assembly is not simply self-assembly of dynein subunits but is guided by targeting factors, which makes the pathway genetically tractable and experimentally attractive [5,6,7].
• Inner dynein arms are required for normal ciliary and flagellar motility, so their assembly is essential for mucociliary clearance and sperm motility.
• Defects in inner dynein arm assembly cause primary ciliary dyskinesia, a motile ciliopathy with respiratory and reproductive consequences.
• Disease-causing variants in CCDC39 and CCDC40 cause axonemal absence of inner dynein arm heavy chains DNAH1, DNAH6 and DNAH7, linking assembly factors to dynein composition.
• The I1 dynein is assembled in the cytoplasm and transported by IFT before axonemal docking, making GO:0036159 a model for compartmentalized motor assembly.
• MBO2/FAP58 stabilizes assembly of inner arm dynein b and reveals axoneme asymmetries involved in ciliary waveform.
• FAP57/WDR65 targets assembly of a subset of inner arm dyneins and connects to regulatory hubs in cilia.
• Gene dosage of independent dynein arm motor preassembly factors influences cilia assembly, showing that assembly factor levels are rate-limiting.
• Outer arm dynein light chain LC1 is required for normal motor assembly kinetics and ciliary stability, illustrating shared principles between inner and outer arm assembly.
• Inner arm dynein composition and function have been dissected in Chlamydomonas reinhardtii, providing a reference framework for other organisms.
• CRISPR-based models allow causal testing of candidate assembly genes in ciliated cells and organisms [1,4,5].
What Happens During inner dynein arm assembly?
Cytoplasmic preassembly of inner arm dynein subunits
In simple terms: The parts of the inner dynein arm motor are first put together in the main body of the cell, not inside the cilium.
Inner dynein arm assembly begins with the preassembly of dynein subunits in the cytoplasm. For the I1 dynein, the two-headed inner arm dynein, studies in Chlamydomonas reinhardtii showed that the complex is assembled in the cytoplasm and then transported by intraflagellar transport before axonemal docking. This means GO:0036159 includes events that occur before the motor ever reaches the axoneme, and it explains why mutations in cytoplasmic preassembly factors can produce inner arm defects [4,8].
Intraflagellar transport of inner arm dynein complexes
In simple terms: Once built, the motor is carried into the cilium by a transport train.
After cytoplasmic preassembly, inner arm dynein complexes are moved into the ciliary compartment by intraflagellar transport (IFT). The I1 dynein is transported by IFT before it docks onto the axoneme, as demonstrated in Chlamydomonas. This transport step is a required part of inner dynein arm assembly because the axoneme itself does not synthesize proteins, so all inner arm components must be delivered from the cytoplasm.
Targeting and stabilization by dedicated assembly factors
In simple terms: Helper proteins decide which inner arm motors get built and make sure they stay together.
Inner dynein arm assembly is guided by dedicated factors rather than occurring by simple self-assembly. The MBO2/FAP58 heterodimer stabilizes assembly of inner arm dynein b and reveals axoneme asymmetries involved in ciliary waveform, and the ciliary MBO2 complex targets assembly of inner arm dynein b and reveals additional doublet microtubule asymmetries. FAP57/WDR65 targets assembly of a subset of inner arm dyneins and connects to regulatory hubs in cilia. These findings show that specific targeting factors determine which inner arm dyneins are assembled and where they dock [5,6,7].
Axonemal docking on outer doublet microtubules
In simple terms: The finished motor is locked onto the correct microtubule track inside the cilium.
The final stage of GO:0036159 is docking of the assembled inner dynein arm onto the outer doublet microtubules of the axoneme. The I1 dynein is assembled in the cytoplasm and transported by IFT before axonemal docking, which places docking as a distinct step after transport. Docking is also asymmetric: MBO2/FAP58 and the MBO2 complex reveal doublet microtubule asymmetries that influence where inner arm dynein b is placed [5,6]. Correct docking is required for the inner arm to generate the asymmetric forces that shape ciliary waveform [3,5].
Quality control and dosage effects in assembly
In simple terms: The cell needs the right amount of each assembly helper for cilia to form normally.
Inner dynein arm assembly is sensitive to the dosage of assembly factors. Gene dosage of independent dynein arm motor preassembly factors influences cilia assembly in Chlamydomonas reinhardtii, indicating that the levels of these factors are rate-limiting for building functional cilia. In addition, outer arm dynein light chain LC1 is required for normal motor assembly kinetics, ciliary stability and motility, showing that assembly kinetics and stability are actively controlled processes rather than passive outcomes. Together these studies indicate that GO:0036159 is a regulated, dosage-sensitive process [2,4].
Key Genes Involved in GO:0036159 inner dynein arm assembly
The genes and proteins below are experimentally implicated in inner dynein arm assembly (GO:0036159) or in the assembly of related axonemal dynein arms, based on the cited literature.
| Gene | Major Role | Research Relevance |
|---|---|---|
| DNAH1 | Inner dynein arm heavy chain; absent from axonemes when CCDC39/CCDC40 are mutated | Marker of inner arm heavy chain loss in PCD models |
| DNAH6 | Inner dynein arm heavy chain; absent from axonemes in CCDC39/CCDC40-related disease | Readout for inner arm assembly defects |
| DNAH7 | Inner dynein arm heavy chain; absent from axonemes in CCDC39/CCDC40-related disease | Readout for inner arm assembly defects |
| CCDC39 | Assembly factor required for axonemal presence of inner dynein arm heavy chains | Disease-causing variants cause PCD with inner arm loss |
| CCDC40 | Assembly factor required for axonemal presence of inner dynein arm heavy chains | Disease-causing variants cause PCD with inner arm loss |
| MBO2 | Component of the MBO2/FAP58 heterodimer that stabilizes inner arm dynein b assembly | Target for studying inner arm b assembly and waveform [5,6] |
| FAP58 | Partner of MBO2; stabilizes assembly of inner arm dynein b | Target for inner arm b assembly and doublet asymmetry |
| FAP57 | Also known as WDR65; targets assembly of a subset of inner arm dyneins | Links inner arm assembly to ciliary regulatory hubs |
| WDR65 | Alternative name for FAP57; involved in targeting inner arm dynein assembly | Candidate for inner arm subset assembly studies |
| LC1 | Outer arm dynein light chain required for normal motor assembly kinetics and ciliary stability | Model for dynein assembly kinetics shared with inner arm biology |
| I1 dynein subunits | Two-headed inner arm dynein complex assembled in cytoplasm and transported by IFT | Classic model for GO:0036159 assembly steps [3,8] |
| Single-headed inner arm dyneins | Inner arm dynein species a-g with distinct subunit compositions | Framework for inner arm composition and function |
| Dynein arm preassembly factors | Independent factors whose dosage influences cilia assembly | Gene dosage studies of cilia assembly |
| IFT machinery | Transports inner arm dynein complexes into the cilium | Required for delivery of I1 dynein before docking |
| Outer dynein arm components | Related axonemal dynein motors that share assembly principles | Comparative studies of dynein assembly |
How Is inner dynein arm assembly Regulated?
Inner dynein arm assembly is regulated at multiple levels. Gene dosage of independent dynein arm motor preassembly factors influences cilia assembly in Chlamydomonas reinhardtii, showing that the abundance of assembly factors is a regulatory parameter. Assembly kinetics and ciliary stability are also controlled, as illustrated by the outer arm dynein light chain LC1, which is required for normal motor assembly kinetics, ciliary stability and motility. In addition, targeting factors such as MBO2/FAP58 and FAP57/WDR65 impose specificity on which inner arm dyneins are assembled and where they dock, connecting inner arm assembly to regulatory hubs in cilia [5,6,7]. Finally, the requirement for cytoplasmic preassembly and IFT-dependent delivery means that assembly is coupled to the general ciliary transport machinery.
inner dynein arm assembly and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| CCDC39 | Primary ciliary dyskinesia with inner dynein arm heavy chain loss | Knockout or point-mutation in ciliated cells; patient-derived models |
| CCDC40 | Primary ciliary dyskinesia with inner dynein arm heavy chain loss | Knockout or point-mutation in ciliated cells; patient-derived models |
| DNAH1 | Inner dynein arm heavy chain loss in PCD | Tagged knock-in or knockout for axonemal localization studies |
| DNAH6 | Inner dynein arm heavy chain loss in PCD | Knockout and rescue models |
| DNAH7 | Inner dynein arm heavy chain loss in PCD | Knockout and rescue models |
| MBO2/FAP58 | Inner arm dynein b assembly and ciliary waveform | Chlamydomonas knockout and tagged knock-in [5,6] |
Primary ciliary dyskinesia and inner dynein arm loss
Primary ciliary dyskinesia (PCD) is a motile ciliopathy in which ciliary beating is defective. Disease-causing variants in CCDC39 and CCDC40 cause axonemal absence of inner dynein arm heavy chains DNAH1, DNAH6 and DNAH7, directly linking inner dynein arm assembly (GO:0036159) to human disease. This makes inner arm heavy chain composition a diagnostic and mechanistic readout in PCD research.
Ciliary waveform defects and motility disorders
Inner dynein arms shape the ciliary waveform, and their assembly is therefore tied to motility disorders. The MBO2/FAP58 heterodimer stabilizes assembly of inner arm dynein b and reveals axoneme asymmetries involved in ciliary waveform, so defects in this assembly step are expected to alter beating patterns. Similarly, FAP57/WDR65 targets assembly of a subset of inner arm dyneins and connects to regulatory hubs in cilia, providing a mechanistic route from assembly defects to abnormal ciliary function.
Broader motile ciliopathy mechanisms
Because inner dynein arm assembly requires cytoplasmic preassembly and IFT-dependent delivery, defects in these steps can contribute to motile ciliopathy phenotypes beyond dynein subunit mutations. Gene dosage effects of dynein arm preassembly factors further indicate that partial loss of assembly capacity can impair cilia assembly, which is relevant to understanding variable disease severity. Comparative work on outer arm dynein assembly, such as the requirement for light chain LC1 in motor assembly kinetics and ciliary stability, highlights shared principles that may apply to inner arm-related disease mechanisms.
From inner dynein arm assembly-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Is a candidate gene required for inner dynein arm assembly? | CRISPR knockout in Chlamydomonas or ciliated mammalian cells [1,4] |
| Does a patient variant impair inner arm assembly? | Point-mutation knock-in of the variant followed by axonemal analysis |
| Where does an assembly factor localize during assembly? | Tagged knock-in with fluorescent or epitope tag [5,6,7] |
| Does overexpression of an assembly factor alter cilia assembly? | Overexpression of preassembly factors in Chlamydomonas |
| Which inner arm dynein subsets depend on a targeting factor? | Knockout of FAP57/WDR65 or MBO2/FAP58 with dynein profiling [5,6,7] |
| How is inner arm dynein transported before docking? | IFT assays in Chlamydomonas with tagged I1 dynein |
How to Study the inner dynein arm assembly Process
| Method | What It Measures | Typical Application |
|---|---|---|
| CRISPR knockout | Requirement of a gene for inner dynein arm assembly | Testing candidate assembly genes [1,4] |
| Point-mutation knock-in | Effect of a specific patient variant | Modeling PCD-associated variants |
| Tagged knock-in | Localization and dynamics of assembly factors | Tracking MBO2/FAP58 or FAP57/WDR65 [5,6,7] |
| Axonemal protein profiling | Presence or absence of inner arm dynein subunits | Detecting DNAH1, DNAH6, DNAH7 loss |
| Motility and waveform imaging | Functional ciliary beating | Linking assembly to waveform defects [2,5,6] |
| IFT assays | Transport of inner arm dynein complexes | Studying I1 dynein delivery before docking |
| Gene dosage manipulation | Sensitivity of cilia assembly to factor levels | Overexpression or partial loss studies |
| Comparative dynein analysis | Shared principles between inner and outer arm assembly | Using LC1 as a reference for assembly kinetics |
Genetic knockout and rescue in ciliated models
CRISPR knockout of candidate assembly genes followed by rescue with wild-type or mutant constructs is a direct way to test causality in GO:0036159. Studies of CCDC39 and CCDC40 variants show how disease-causing changes can be linked to axonemal absence of inner dynein arm heavy chains DNAH1, DNAH6 and DNAH7. Gene dosage experiments in Chlamydomonas further demonstrate that manipulating preassembly factor levels changes cilia assembly outcomes.
Axonemal protein profiling and immunodetection
Because inner dynein arm assembly determines which dynein subunits are present on the axoneme, protein-level profiling of axonemes is a core method. The loss of DNAH1, DNAH6 and DNAH7 from axonemes in CCDC39/CCDC40-related disease was detected by axonemal analysis. Composition and function of ciliary inner-dynein-arm subunits have been studied systematically in Chlamydomonas reinhardtii, providing a reference for such profiling.
Live imaging and motility assays
Ciliary waveform and motility are functional readouts of inner dynein arm assembly. MBO2/FAP58 and the MBO2 complex were linked to inner arm dynein b assembly and to axoneme asymmetries involved in ciliary waveform, which requires motility and imaging-based assays [5,6]. Outer arm dynein light chain LC1 studies similarly used motility and stability measurements to connect assembly kinetics to ciliary function.
Transport and localization assays
Intraflagellar transport and localization assays are needed to resolve the preassembly, transport and docking steps of GO:0036159. The I1 dynein was shown to be assembled in the cytoplasm and transported by IFT before axonemal docking, which required tracking the complex through the ciliary compartment. Tagged knock-in approaches for factors such as FAP57/WDR65 and MBO2/FAP58 support this type of localization analysis [5,6,7].
How CRISPR Can Be Used to Study GO:0036159 inner dynein arm assembly
Knockout
CRISPR knockout is used to remove candidate inner dynein arm assembly genes and test whether their loss prevents formation of inner arm dyneins on the axoneme. This approach mirrors the observation that CCDC39 and CCDC40 defects cause axonemal absence of DNAH1, DNAH6 and DNAH7, and it can be applied to assembly factors such as MBO2/FAP58 and FAP57/WDR65 to define which inner arm dynein subsets they control [5,6,7].
Point Mutation
Point-mutation knock-in allows precise modeling of disease-associated variants in inner dynein arm assembly genes. Because disease-causing variants in CCDC39 and CCDC40 lead to loss of inner dynein arm heavy chains from axonemes, introducing the same variants into model systems can reveal whether a specific amino acid change is sufficient to disrupt assembly, transport or docking.
Knock-in
Knock-in of tags or reporters into endogenous assembly genes enables tracking of inner dynein arm assembly steps in living cells. Tagged knock-in of factors such as MBO2/FAP58 and FAP57/WDR65 supports studies of targeting, stabilization and docking of inner arm dyneins [5,6,7], while tagged I1 dynein subunits allow visualization of cytoplasmic preassembly and IFT-dependent transport.
Overexpression
Overexpression is used to test whether increasing the level of an assembly factor changes cilia assembly. Gene dosage of independent dynein arm motor preassembly factors influences cilia assembly in Chlamydomonas reinhardtii, so controlled overexpression of preassembly factors can reveal rate-limiting steps in GO:0036159 and help distinguish sufficiency from requirement.
How EDITGENE Supports inner dynein arm assembly Research
Researchers studying inner dynein arm assembly-related genes often need to determine whether a candidate gene is causally involved in building functional inner dynein arms, whether a patient variant is pathogenic, and where the encoded protein acts during preassembly, transport or axonemal docking. Answering these questions requires precise, reproducible genome engineering and functional readouts in ciliated cell models.
Contact EDITGENE today to design your custom CRISPR model for inner dynein arm assembly research.
Frequently Asked Questions About inner dynein arm assembly
What is inner dynein arm assembly (GO:0036159)?
It is the biological process in which a set of components is aggregated, arranged and bonded together to form an axonemal dynein inner arm on the outer doublet microtubules of ciliary and flagellar axonemes.
What genes are involved in inner dynein arm assembly?
Genes and proteins implicated in this process include inner dynein arm heavy chains such as DNAH1, DNAH6 and DNAH7, assembly factors such as CCDC39 and CCDC40, and targeting factors such as MBO2/FAP58 and FAP57/WDR65 [1,5,6,7].
Why is inner dynein arm assembly important for cilia?
Inner dynein arms are motors that shape ciliary and flagellar waveforms, so their correct assembly is required for normal ciliary motility [3,5].
How is the inner dynein arm assembled?
The I1 dynein is assembled in the cytoplasm and transported by intraflagellar transport before axonemal docking, and dedicated factors such as MBO2/FAP58 and FAP57/WDR65 target specific inner arm dyneins [5,6,7,8].
What diseases are linked to inner dynein arm assembly defects?
Primary ciliary dyskinesia is linked to inner dynein arm defects; disease-causing variants in CCDC39 and CCDC40 cause axonemal absence of DNAH1, DNAH6 and DNAH7.
What is the role of CCDC39 and CCDC40 in inner dynein arm assembly?
CCDC39 and CCDC40 are required for the axonemal presence of inner dynein arm heavy chains, and their mutation leads to loss of DNAH1, DNAH6 and DNAH7 from axonemes.
What is the role of MBO2 and FAP58 in inner arm dynein assembly?
The MBO2/FAP58 heterodimer stabilizes assembly of inner arm dynein b and reveals axoneme asymmetries involved in ciliary waveform [5,6].
What does FAP57/WDR65 do in cilia?
FAP57/WDR65 targets assembly of a subset of inner arm dyneins and connects to regulatory hubs in cilia.
How do researchers study inner dynein arm assembly?
Researchers use genetic knockouts, point-mutation and tagged knock-in models, axonemal protein profiling, motility imaging and intraflagellar transport assays in organisms such as Chlamydomonas reinhardtii [1,3,4,5,8].
Can CRISPR be used to study inner dynein arm assembly?
Yes; CRISPR knockout, point-mutation, knock-in and overexpression approaches can test the requirement and dosage sensitivity of inner dynein arm assembly genes and assembly factors [1,4,5].
Conclusion
GO:0036159 (inner dynein arm assembly) captures a multi-step process in which inner arm dynein subunits are preassembled in the cytoplasm, delivered by intraflagellar transport and docked onto outer doublet microtubules with the help of dedicated targeting factors [5,6,7,8]. Its importance is underscored by human disease: variants in CCDC39 and CCDC40 cause axonemal absence of inner dynein arm heavy chains DNAH1, DNAH6 and DNAH7 in primary ciliary dyskinesia. Continued work in Chlamydomonas and other ciliated models, supported by CRISPR-based knockout, point-mutation, knock-in and overexpression approaches, will clarify how assembly specificity, dosage and docking are controlled [2,3,4].
References
- 1. Wilken A et al.. 2024. Primary Ciliary Dyskinesia Associated Disease-Causing Variants in CCDC39 and CCDC40 Cause Axonemal Absence of Inner Dynein Arm Heavy Chains DNAH1, DNAH6, and DNAH7.. Cells 13(14) PMID: 39056782
- 2. Sakato-Antoku M et al.. 2023. Outer-arm dynein light chain LC1 is required for normal motor assembly kinetics, ciliary stability, and motility.. Mol Biol Cell 34(7):ar75 PMID: 37133971
- 3. Yamamoto R et al.. 2021. Composition and function of ciliary inner-dynein-arm subunits studied in Chlamydomonas reinhardtii.. Cytoskeleton (Hoboken) 78(3):77-96 PMID: 33876572
- 4. Penny GM et al.. 2024. Gene dosage of independent dynein arm motor preassembly factors influences cilia assembly in Chlamydomonas reinhardtii.. PLoS Genet 20(3):e1011038 PMID: 38498551
- 5. Fu G et al.. 2024. The MBO2/FAP58 heterodimer stabilizes assembly of inner arm dynein b and reveals axoneme asymmetries involved in ciliary waveform.. Mol Biol Cell 35(5):ar72 PMID: 38568782
- 6. Fu G et al.. 2023. The ciliary MBO2 complex targets assembly of inner arm dynein b and reveals additional doublet microtubule asymmetries.. bioRxiv PMID: 37577467
- 7. Lin J et al.. 2019. FAP57/WDR65 targets assembly of a subset of inner arm dyneins and connects to regulatory hubs in cilia.. Mol Biol Cell 30(21):2659-2680 PMID: 31483737
- 8. Viswanadha R et al.. 2014. The ciliary inner dynein arm, I1 dynein, is assembled in the cytoplasm and transported by IFT before axonemal docking.. Cytoskeleton (Hoboken) 71(10):573-86 PMID: 25252184
