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TitleIFT-A structure reveals carriages for membrane protein transport into cilia.
Journal, issue, pagesCell, Vol. 185, Issue 26, Page 4971-4985.e16, Year 2022
Publish dateDec 22, 2022
AuthorsSophie J Hesketh / Aakash G Mukhopadhyay / Dai Nakamura / Katerina Toropova / Anthony J Roberts /
PubMed AbstractIntraflagellar transport (IFT) trains are massive molecular machines that traffic proteins between cilia and the cell body. Each IFT train is a dynamic polymer of two large complexes (IFT-A and -B) ...Intraflagellar transport (IFT) trains are massive molecular machines that traffic proteins between cilia and the cell body. Each IFT train is a dynamic polymer of two large complexes (IFT-A and -B) and motor proteins, posing a formidable challenge to mechanistic understanding. Here, we reconstituted the complete human IFT-A complex and obtained its structure using cryo-EM. Combined with AlphaFold prediction and genome-editing studies, our results illuminate how IFT-A polymerizes, interacts with IFT-B, and uses an array of β-propeller and TPR domains to create "carriages" of the IFT train that engage TULP adaptor proteins. We show that IFT-A⋅TULP carriages are essential for cilia localization of diverse membrane proteins, as well as ICK-the key kinase regulating IFT train turnaround. These data establish a structural link between IFT-A's distinct functions, provide a blueprint for IFT-A in the train, and shed light on how IFT evolved from a proto-coatomer ancestor.
External linksCell / PubMed:36462505
MethodsEM (single particle)
Resolution3.5 - 8.0 Å
Structure data

15954

8bbe

EMDB-15954, PDB-8bbe:
Structure of the IFT-A complex; IFT-A2 module
Method: EM (single particle) / Resolution: 3.5 Å

15955

8bbf

EMDB-15955, PDB-8bbf:
Structure of the IFT-A complex; IFT-A1 module
Method: EM (single particle) / Resolution: 8.0 Å

PDB-8bbg:
Structure of the IFT-A complex; anterograde IFT-A train model
Method: ELECTRON MICROSCOPY / Resolution: 3.5 Å

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / cilia / intraflagellar transport / membrane protein import / complex

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