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TitleDoublet microtubule inner junction protein FAP20 recruits tubulin to the microtubule lattice.
Journal, issue, pagesStructure, Vol. 31, Issue 12, Page 1535-11544.e4, Year 2023
Publish dateDec 7, 2023
AuthorsMamata Bangera / Archita Dungdung / Sujana Prabhu / Minhajuddin Sirajuddin /
PubMed AbstractDoublet microtubules of eukaryotic cilia and flagella are made up of a complete A- and an incomplete B-tubule that are fused together. Of the two fusion points, the outer junction is made of ...Doublet microtubules of eukaryotic cilia and flagella are made up of a complete A- and an incomplete B-tubule that are fused together. Of the two fusion points, the outer junction is made of tripartite tubulin connections, while the inner junction contains non-tubulin elements. The latter includes flagellar-associated protein 20 (FAP20) and Parkin co-regulated gene protein (PACRG) that together link the A- and B-tubule at the inner junction. While structures of doublet microtubules reveal molecular details, their assembly is poorly understood. In this study, we purified recombinant FAP20 and characterized its effects on microtubule dynamics. We use in vitro reconstitution and cryo-electron microscopy to show that FAP20 recruits free tubulin to the existing microtubule lattice. Our cryo-electron microscopy reconstruction of microtubule:FAP20:tubulin complex reveals the mode of tubulin recruitment by FAP20 onto microtubules, providing insights into assembly steps of B-tubule closure during doublet microtubule formation.
External linksStructure / PubMed:37816351 / PubMed Central
MethodsEM (single particle)
Resolution11.6 Å
Structure data

EMDB-34836: Complex of GMPCPP microtubule, FAP20 and tubulin (in absence of GTP)
Method: EM (single particle) / Resolution: 11.6 Å

Source
  • Capra hircus (goat)
  • Chlamydomonas reinhardtii (plant)

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