Tetrahymena RIB72A and RIB72B are microtubule inner proteins in the ciliary doublet microtubules

Autor: Ying Zhao, Long Gui, Mark Winey, Panagiota Louka, Raphaël F.-X. Tomasi, Charles N. Baroud, Daniela Nicastro, Jacek Gaertig, Swati Suryawanshi, Pascale Dupuis-Williams, Drashti Dave, Brian A. Bayless, Daniel Stoddard
Přispěvatelé: Surrey, Thomas
Rok vydání: 2018
Předmět:
Zdroj: Molecular biology of the cell, vol 29, iss 21
Popis: Doublet and triplet microtubules are essential and highly stable core structures of centrioles, basal bodies, cilia and flagella. In contrast to dynamic cytoplasmic microtubules, their luminal surface is coated with regularly arranged Microtubule Inner Proteins (MIPs). However, the protein composition and biological function(s) of MIPs remain poorly understood. Using genetic, biochemical and imaging techniques we identifiedTetrahymenaRIB72A and RIB72B proteins as ciliary MIPs. Fluorescence imaging of tagged RIB72A and RIB72B showed that both proteins co-localize toTetrahymenacilia and basal bodies, but assemble independently. Cryo-electron tomography ofRIB72Aand/orRIB72Bknockout strains revealed major structural defects in the ciliary A-tubule involving MIP1, MIP4 and MIP6 structures. The defects of individual mutants were complementary in the double mutant. All mutants had reduced swimming speed and ciliary beat frequencies, and high-speed video imaging revealed abnormal highly curved cilia during power stroke. Our results show that RIB72A and RIB72B are crucial for the structural assembly of ciliary A-tubule MIPs and are important for proper ciliary motility.SUMMARYMicrotubule Inner Proteins (MIPs) bind to the luminal surface of highly stable microtubules. Combining cell biology and cryo-electron tomography, Stoddardet al.show that RIB72A and RIB72B are conserved MIPs in ciliary doublet microtubules and that they are important for proper ciliary motility.
Databáze: OpenAIRE