Three-dimensional structure of the Trypanosome flagellum suggests that the paraflagellar rod functions as a biomechanical spring. [PDF]
PLoS ONE, 2012 Flagellum motility is critical for normal human development and for transmission of pathogenic protozoa that cause tremendous human suffering worldwide.
Louise C Hughes +3 more
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Dynein light intermediate chains as pivotal determinants of dynein multifunctionality [PDF]
Journal of Cell Science, 2021 ABSTRACT In animal cells, a single cytoplasmic dynein motor mediates microtubule minus-end-directed transport, counterbalancing dozens of plus-end-directed kinesins. The remarkable ability of dynein to interact with a diverse cargo spectrum stems from its tightly regulated recruitment of cargo-specific adaptor proteins, which engage the ...
Amrita Kumari +3 more
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Cell cycle-dependent microtubule-based dynamic transport of cytoplasmic dynein in mammalian cells. [PDF]
PLoS ONE, 2009 BACKGROUND:Cytoplasmic dynein complex is a large multi-subunit microtubule (MT)-associated molecular motor involved in various cellular functions including organelle positioning, vesicle transport and cell division.
Takuya Kobayashi, Takashi Murayama
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Calaxin stabilizes the docking of outer arm dyneins onto ciliary doublet microtubule in vertebrates
eLife, 2023 Outer arm dynein (OAD) is the main force generator of ciliary beating. Although OAD loss is the most frequent cause of human primary ciliary dyskinesia, the docking mechanism of OAD onto the ciliary doublet microtubule (DMT) remains elusive in ...
Hiroshi Yamaguchi +2 more
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Identification of new genes involved in human adipogenesis and fat storage. [PDF]
PLoS ONE, 2012 Since the worldwide increase in obesity represents a growing challenge for health care systems, new approaches are needed to effectively treat obesity and its associated diseases. One prerequisite for advances in this field is the identification of genes
Jörn Söhle +7 more
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Neurodegenerative Mutation in Cytoplasmic Dynein Alters Its Organization and Dynein-Dynactin and Dynein-Kinesin Interactions [PDF]
Journal of Biological Chemistry, 2010 A single amino acid change, F580Y (Legs at odd angles (Loa), Dync1h1(Loa)), in the highly conserved and overlapping homodimerization, intermediate chain, and light intermediate chain binding domain of the cytoplasmic dynein heavy chain can cause severe motor and sensory neuron loss in mice.
Deng, Wenhan +7 more
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Inner lumen proteins stabilize doublet microtubules in cilia and flagella
Nature Communications, 2019 Microtubules in cilia are sufficiently stable to withstand the beating motion, but how they are stabilized while serving as tracks for intraflagellar transport and axonemal dyneins remains unknown.
Mikito Owa +8 more
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Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule
eLife, 2019 Dyneins are motor proteins responsible for transport in the cytoplasm and the beating of axonemes in cilia and flagella. They bind and release microtubules via a compact microtubule-binding domain (MTBD) at the end of a coiled-coil stalk.
Samuel E Lacey +3 more
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eLife, 2022 Mutations in the microtubule (MT)-binding protein doublecortin (DCX) or in the MT-based molecular motor dynein result in lissencephaly. However, a functional link between DCX and dynein has not been defined.
Xiaoqin Fu +7 more
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PLoS Genetics, 2020 Ciliary dyneins are preassembled in the cytoplasm before being transported into cilia, and a family of proteins containing the PIH1 domain, PIH proteins, are involved in the assembly process.
Ryosuke Yamamoto +7 more
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