Results 11 to 20 of about 48,169 (274)

Ciliary Dyneins and Dynein Related Ciliopathies [PDF]

Cells, 2021
Although ubiquitously present, the relevance of cilia for vertebrate development and health has long been underrated. However, the aberration or dysfunction of ciliary structures or components results in a large heterogeneous group of disorders in ...
Dinu Antony, Han G. Brunner, Miriam Schmidts   +2 more
doaj   +4 more sources

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, Garrett, Caroline, Dombert, Benjamin, Soura, Violetta, Banks, Gareth, Fisher, Elizabeth M. C., van der Brug, Marcel P., Hafezparast, Majid   +7 more
openaire   +4 more sources

Conserved Roles for the Dynein Intermediate Chain and Ndel1 in Assembly and Activation of Dynein [PDF]

Nature Communications, 2023
Cytoplasmic dynein, the primary retrograde microtubule transport motor within cells, must be activated for processive motility through the regulated assembly of a dynein-dynactin-adapter (DDA) complex. The interaction between dynein and dynactin was initially ascribed to the N-terminus of the dynein intermediate chain (IC) and a ...
Kyoko Okada, Bharat R. Iyer, Lindsay G. Lammers, Pedro A. Gutierrez, Wenzhe Li, Steven M. Markus, Richard J. McKenney   +6 more
openaire   +8 more sources

Lis1 Has Two Opposing Modes of Regulating Cytoplasmic Dynein

Cell, 2017
Regulation is central to the functional versatility of cytoplasmic dynein, a motor involved in intracellular transport, cell division, and neurodevelopment. Previous work established that Lis1, a conserved and ubiquitous regulator of dynein, binds to its
Samara Reck-Peterson, Michael A Cianfrocco   +1 more
exaly   +2 more sources

Cryo-ET and MD simulations reveal that dynein-2 is tuned for binding to the A-tubule of the ciliary doublet [PDF]

The EMBO Journal
Eukaryotic cilia and flagella are thin structures present on the surface of cells, playing vital roles in signaling and cellular motion. Cilia assembly depends on intraflagellar transport (IFT) along doublet microtubules (doublets).
Haoqiang K He, Shintaroh Kubo, Xuwei Chen, Qianru H Lv, Azusa Kage, Muneyoshi Ichikawa   +5 more
doaj   +2 more sources

Cytoplasmic dynein nomenclature [PDF]

The Journal of Cell Biology, 2005
A variety of names has been used in the literature for the subunits of cytoplasmic dynein complexes. Thus, there is a strong need for a more definitive consensus statement on nomenclature. This is especially important for mammalian cytoplasmic dyneins, many subunits of which are encoded by multiple genes.
Pfister, K. Kevin, Fisher, Elizabeth M. C., Gibbons, Ian R., Hays, Thomas S., Holzbaur, Erika L. F., McIntosh, J. Richard, Porter, Mary E., Schroer, Trina A., Vaughan, Kevin T., Witman, George B., King, Stephen M., Vallee, Richard B.   +11 more
openaire   +5 more sources

She1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain [PDF]

Nature Communications, 2017
Dynein is a microtubule motor the motility of which is affected by the microtubule-associated protein She1. Here, the authors show that She1 alters dynein stepping behavior and increases its microtubule affinity through simultaneous interactions with the
Kari H. Ecklund, Tatsuya Morisaki, Lindsay G. Lammers, Matthew G. Marzo, Timothy J. Stasevich, Steven M. Markus   +5 more
doaj   +2 more sources

NuMA recruits dynein activity to microtubule minus-ends at mitosis

eLife, 2017
To build the spindle at mitosis, motors exert spatially regulated forces on microtubules. We know that dynein pulls on mammalian spindle microtubule minus-ends, and this localized activity at ends is predicted to allow dynein to cluster microtubules into
Christina L Hueschen, Samuel J Kenny, Ke Xu, Sophie Dumont   +3 more
doaj   +2 more sources

Differential effects of the dynein-regulatory factor Lissencephaly-1 on processive dynein-dynactin motility [PDF]

Journal of Biological Chemistry, 2017
Cytoplasmic dynein is the primary minus-end–directed microtubule motor protein in animal cells, performing a wide range of motile activities, including transport of vesicular cargos, mRNAs, viruses, and proteins.
Pedro A. Gutierrez, Bryce E. Ackermann, M. Vershinin, Richard J. Mckenney   +3 more
semanticscholar   +3 more sources

Dynein Swings into Action [PDF]

Cell, 2009
Motor proteins, such as dynein, use chemical energy from ATP hydrolysis to move along the cytoskeleton. Roberts et al. (2009) now describe the arrangement of subdomains in the motor domain of dynein and propose a model for how these regions function together in force generation.
Houdusse, Anne, Carter, Andrew P.
openaire   +4 more sources