Human CFAP300 variants cause respiratory-cilium motility defects with both outer and inner dynein-arm loss; patient phenotype and microscopy establish necessity but not the performed molecular step.

Tagged native Paramecium and Chlamydomonas orthologs are predominantly cytoplasmic, with a small ciliary pool; full Figure 3 fractionation places this pool in soluble membrane/matrix material. These are ortholog constructs, not a direct human assay.

IFT139/TTC21B and FLA10 perturbations alter the ciliary distribution of CFAP300 orthologs. The experiment follows the factor itself rather than directly showing it carrying a dynein complex.

Paramecium ortholog knockdown reduces dynein arms, beating and swimming. Its conserved accessory-factor role is supported, while preassembly, stabilization and delivery remain experimentally distinguishable possibilities.

During ciliogenesis the tagged model-organism factor accumulates at ciliary tips with a distribution resembling IFT46. The endpoint supports the factor’s own trafficking and does not by itself establish a dynein-cargo bridge.

Human loss-of-function variants cause outer- and inner-dynein-arm defects in respiratory cilia and sperm flagella, supporting the inherited assembly-process proposals together with the interaction evidence.

DNAAF2 association is supported by the target yeast-two-hybrid assay and tagged co-immunoprecipitation in Figure S12/Table S2. The inspected text does not resolve the exact modern CFAP300 product or co-IP host.

IFT46 and PIH1D3 yeast candidates showed autoactivation and were not recovered in the tested co-immunoprecipitations; these controls do not establish a CFAP300 bridge to IFT machinery.

Expression increases during ciliogenesis and the authors propose a preassembly role. Association and selective arm defects support assembly-factor participation, but no specific chaperone, scaffold or catalytic reaction was reconstructed.

Endogenous human nasal epithelial immunostaining and Airyscan imaging show a predominantly cytoplasmic distribution plus CFAP300 along ciliary axonemes; patient signal is strongly depleted. This supports the retained axoneme localization at the resolution of the assay.

The CFAP300 antibody recognizes residues 113–188, and the authors consider a short product as a possible source of residual patient staining. The assay does not establish isoform-specific transport or stable incorporation into an axonemal structural complex.

Patient cilia lose dynein-arm components while retaining the basic microtubule arrangement. The authors treat basal-foot disorientation as potentially secondary to immotility; neither fixed-cell localization nor this phenotype directly measures cargo carriage.

Patient respiratory-cell dynein markers have different abnormal apical distributions. These endpoints motivate distinct trafficking hypotheses but do not measure whether retained motors are preassembled or physically linked to CFAP300.

Planarian gene silencing supports a conserved ciliary role; this ortholog perturbation is separate from the human patient localization data.