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Human IFT-A complex structures provide molecular insights into ciliary transport.

Meiqin Jiang1, Vivek Reddy Palicharla2, Darcie Miller1

  • 1Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.

Cell Research
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Structural insights into Intraflagellar Transport (IFT)-A complex assembly and TULP3 interaction reveal mechanisms underlying ciliopathies. This study clarifies IFT-A architecture and its role in ciliary transport.

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Area of Science:

  • Structural Biology
  • Cell Biology
  • Molecular Medicine

Background:

  • Intraflagellar transport (IFT) complexes (IFT-A and IFT-B) are crucial for cilia assembly and maintenance, moving along axonemal microtubules.
  • Dysfunctional IFT subunits cause ciliopathies, but the precise mechanisms of IFT complex assembly and cargo transport remain unclear due to limited high-resolution structural data.

Purpose of the Study:

  • To elucidate the high-resolution structure of the human IFT-A complex.
  • To investigate the interaction between IFT-A and its cargo adapter TULP3.
  • To understand the molecular basis of disease-causing mutations in ciliopathies.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to determine the structures of human IFT-A complexes.
  • Structures were resolved at resolutions ranging from 3.0 to 3.9 Å.
  • Analysis included examining IFT-A in the presence and absence of TULP3, and assessing the impact of disease mutations.

Main Results:

  • The cryo-EM structures reveal the 'lariat' architecture of the IFT-A complex, highlighting interconnected core and peripheral subunits stabilized by zinc-binding domains.
  • TULP3 binds to IFT-A via its N-terminal region, with interface mutations shown to impair cargo transport.
  • The study details the molecular effects of disease-associated mutations on IFT-A complex formation and ciliary transport dynamics.

Conclusions:

  • The determined IFT-A architecture provides fundamental insights into complex assembly and ciliary transport mechanisms.
  • The findings clarify the role of TULP3 as a cargo adapter and its interaction interface with IFT-A.
  • This structural and mechanistic understanding enables the rationalization of various ciliopathies linked to IFT subunit mutations.