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 |
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Přispěvatelé: | Surrey, Thomas |
Rok vydání: | 2018 |
Předmět: |
Fluorescence-lifetime imaging microscopy
Axoneme Centriole 1.1 Normal biological development and functioning Green Fluorescent Proteins Protozoan Proteins Video Recording Flagellum Microtubules Medical and Health Sciences Fluorescence 03 medical and health sciences Gene Knockout Techniques 0302 clinical medicine Phagocytosis Microtubule Models Underpinning research Basal body Cilia 030304 developmental biology 0303 health sciences biology Chemistry Cilium Tetrahymena Biological Sciences biology.organism_classification Biological Cell biology Protein Subunits Cytoplasm Mutation Microtubule Proteins Generic health relevance 030217 neurology & neurosurgery Developmental Biology |
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 |
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