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TitleMechanism of IFT-A polymerization into trains for ciliary transport.
Journal, issue, pagesCell, Vol. 185, Issue 26, Page 4986-4998.e12, Year 2022
Publish dateDec 22, 2022
AuthorsShimi Meleppattu / Haixia Zhou / Jin Dai / Miao Gui / Alan Brown /
PubMed AbstractIntraflagellar transport (IFT) is the highly conserved process by which proteins are transported along ciliary microtubules by a train-like polymeric assembly of IFT-A and IFT-B complexes. IFT-A is ...Intraflagellar transport (IFT) is the highly conserved process by which proteins are transported along ciliary microtubules by a train-like polymeric assembly of IFT-A and IFT-B complexes. IFT-A is sandwiched between IFT-B and the ciliary membrane, consistent with its putative role in transporting transmembrane and membrane-associated cargoes. Here, we have used single-particle analysis electron cryomicroscopy (cryo-EM) to determine structures of native IFT-A complexes. We show that subcomplex rearrangements enable IFT-A to polymerize laterally on anterograde IFT trains, revealing a cooperative assembly mechanism. Surprisingly, we discover that binding of IFT-A to IFT-B shields the preferred lipid-binding interface from the ciliary membrane but orients an interconnected network of β-propeller domains with the capacity to accommodate diverse cargoes toward the ciliary membrane. This work provides a mechanistic basis for understanding IFT-train assembly and cargo interactions.
External linksCell / PubMed:36563665 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 3.5 Å
Structure data

28866

8f5o

EMDB-28866, PDB-8f5o:
Structure of Leishmania tarentolae IFT-A (state 1)
Method: EM (single particle) / Resolution: 3.5 Å

28867

8f5p

EMDB-28867, PDB-8f5p:
Structure of Leishmania tarentolae IFT-A (state 2)
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • leishmania tarentolae (eukaryote)
KeywordsPROTEIN TRANSPORT / Cilia / IFT

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