Structural highlights
FunctionPublication Abstract from PubMedOligomeric assemblies of intraflagellar transport (IFT) particles build cilia through sequential recruitment and transport of ciliary cargo proteins within cilia. Here we present the 1.8 A resolution crystal structure of the Chlamydomonas IFT-B protein IFT80, which reveals the architecture of two N-terminal beta-propellers followed by an alpha-helical extension. The N-terminal beta-propeller tethers IFT80 to the IFT-B complex via IFT38 whereas the second beta-propeller and the C-terminal alpha-helical extension result in IFT80 homo-dimerization. Using CRISPR/Cas to create biallelic Ift80 frameshift mutations in IMCD3 mouse cells, we demonstrate that IFT80 is absolutely required for ciliogenesis. Structural mapping and rescue experiments reveal that human disease-causing missense mutations do not cluster within IFT80 and form functional IFT particles. Unlike missense mutant forms of IFT80, deletion of the C-terminal dimerization domain prevented rescue of ciliogenesis. Taken together our results may provide a first insight into higher order IFT complex formation likely required for IFT train formation. Crystal structure of intraflagellar transport protein 80 reveals a homo-dimer required for ciliogenesis.,Taschner M, Lorentzen A, Mourao A, Collins T, Freke GM, Moulding D, Basquin J, Jenkins D, Lorentzen E Elife. 2018 Apr 16;7. pii: 33067. doi: 10.7554/eLife.33067. PMID:29658880[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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