Falcon deep research succeeded (IFT52-deep-research-falcon.md; first run, ~15 min). Its conclusions agree with this review: [file:human/IFT52/IFT52-deep-research-falcon.md "Direct human genetics and knockout/rescue experiments strongly establish IFT52 as an IFT-B scaffold required for ciliary assembly and anterograde transport."] It also reports (Ishida 2022, Tasaki 2025; not cached here) that IFT52 knockout in RPE1 cells abolishes mother-centriole recruitment of IFT88/IFT38 and ciliogenesis, and (Dupont 2019) a proposed extraciliary centrosome-cohesion role in mouse IMCD3 cells that remains less established; consistent with keeping centrosome/centriole rows as non-core.
IFT52 is an IFT-B1 core hub subunit PMID:28625565
- SRTD16 patient cells: PMID:27466190; PMID:27466190
- Photoreceptor ciliary base, with SANS/USH1G PMID:31637240
HPA v25: Primary cilium (Approved), Basal body (Approved); main location Microtubules. Consistent with the module role (IFT-B subunit of anterograde trains, stage 4). Only Approved-grade reliability; no GO_REF:0000052 rows exist for IFT52. Core functions agree with the module's process (intraciliary anterograde transport, cilium assembly) and complex; as for IFT88, no cargo-adaptor MF is asserted because IFT52's demonstrated role is structural bridging within IFT-B.
Every IFT-B subunit annotated from PMID:26980730 (Katoh et al. 2016, an IFT-B architecture paper) carries an IDA to GO:0030991 intraciliary transport particle A. This contradicts the paper's own content (which supports the GO:0030992 IFT-B IPI rows from the same paper) and the established biochemistry. Marked REMOVE as a genuinely contradicted claim (likely batch term-selection error), not as second-guessing assay data.