Reference - Detail
| RRC ID | 83198 |
|---|---|
| Author | Tasaki K, Satoda Y, Chiba S, Shin HW, Katoh Y, Nakayama K. |
| Title | Mutually independent and cilia-independent assembly of IFT-A and IFT-B complexes at mother centriole. |
| Journal | Mol Biol Cell |
| Abstract |
The intraflagellar transport (IFT) machinery, containing the IFT-A and IFT-B complexes and powered by dynein-2 and kinesin-2 motors, is crucial for bidirectional trafficking of ciliary proteins and their import/export across the transition zone (TZ). Stepwise assembly of anterograde IFT trains was proposed previously; that is, the IFT-B complex first forms a TZ-tethered scaffold with sequential incorporation of IFT-A, dynein-2, and finally kinesin-2. However, IFT-A and IFT-B complexes also demonstrate distinct localization to the basal body/mother centriole. We show that IFT-A, IFT-B, and dynein-2 complexes are recruited to the mother centriole independently of ciliogenesis. Furthermore, mother centriole recruitment of IFT-A and IFT-B can occur in the absence of IFT-B and IFT-A, respectively, and dynein-2 recruitment is independent of IFT-A and IFT-B. Expansion microscopy revealed that the IFT-A/IFT-B pool at the basal body is distinct from that at the TZ. We conclude that IFT-A and IFT-B are recruited to the mother centriole in a mutually independent and ciliogenesis-independent manner before IFT train assembly. |
| Volume | 36(4) |
| Pages | ar48 |
| Published | 2025-4-1 |
| DOI | 10.1091/mbc.E24-11-0509 |
| PMID | 40020180 |
| MeSH | Animals Basal Bodies / metabolism Centrioles* / metabolism Cilia* / metabolism Dyneins* / metabolism Flagella / metabolism Kinesins* / metabolism Mice Protein Transport / physiology |
| IF | 3.791 |
| Altmetric score |
オルトメトリクス指標項目
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| The most frequently cited source | X(Twitter) |
| Total number of mentions | 2 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| Human and Animal Cells | 293T(RCB2202) |