Mutually independent and cilia-independent assembly of IFT-A and IFT-B complexes at mother centriole.

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Tác giả: Shuhei Chiba, Yohei Katoh, Kazuhisa Nakayama, Yuuki Satoda, Hye-Won Shin, Koshi Tasaki

Ngôn ngữ: eng

Ký hiệu phân loại:

Thông tin xuất bản: United States : Molecular biology of the cell , 2025

Mô tả vật lý:

Bộ sưu tập: NCBI

ID: 728620

 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
  i.e., 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.
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