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Glycylation regulates axonemal dyneins
Science, 2021Cell Biology Physiological functions of the microtubule cytoskeleton are expected to be regulated by a variety of posttranslational tubulin modifications. For instance, tubulin glycylation is almost exclusively found in cilia and flagella, but its role in the function of these organelles remains unclear. Gadadhar et al.
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Axonemal dynein from Tetrahymena
Journal of Cell Science, 1991ABSTRACT Axonemal dynein from Tetrahymena cilia can be separated on a sucrose gradient into two fractions, at least one of which appears to be polymorphic. We have been using immuno-electron microscopy in order to try and locate the different types of dynein molecules within the axonemal structure.
E M, Crossley, S C, Hyman, C, Wells
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Current Opinion in Cell Biology, 1992
Recent advances in our understanding of the axonemal dyneins reveal them to be much more complex than previously believed. A combination of genetic, molecular genetic, ultrastructural and biochemical approaches is now aiding the elucidation of the organization and function of these important mechanochemical transducers.
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Recent advances in our understanding of the axonemal dyneins reveal them to be much more complex than previously believed. A combination of genetic, molecular genetic, ultrastructural and biochemical approaches is now aiding the elucidation of the organization and function of these important mechanochemical transducers.
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Biophysical Measurements on Axonemal Dyneins
2009In recent decades, the development of technologies such as optical trap nanometry and advanced fluorescence microscopy have provided tools for studying the dynamics of single protein molecules in vitro and in vivo with nanometer precision over timescales from milliseconds to seconds.
Hiroaki, Kojima +3 more
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Axonemal dyneins winch the cilium
Nature Structural & Molecular Biology, 2010In this issue, Ishikawa and colleagues provide direct evidence to support the 'winch' hypothesis for the dynein motor mechanism, in which the AAA domain motor unit is displaced parallel to the doublet microtubule long axis rather than undergoing a rotary motion.
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Axonemal dyneins: assembly, organization, and regulation
Current Opinion in Cell Biology, 1996Progress in the sequence determination of dynein subunits is providing new insights into the locations of functional domains in these microtubule motors. Combined structural and biochemical analyses of flagellar mutations are also yielding information on the three-dimensional organization of the dynein arms and on the different components that target ...
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Dynein heavy chain isoforms and axonemal motility
Trends in Cell Biology, 1993The translocation of dynein along microtubules is the basis for a wide variety of essential cellular movements. Dynein was first discovered in the ciliary axoneme, where it causes the directed sliding between outer doublet microtubules that underlies ciliary bending.
D J, Asai, C J, Brokaw
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1999
Abstract Axonemal dynein forms a double row of projections, the outer and inner arms, that are attached to the A tubule of each axonemal doublet and extend toward the B tubule of the adjacent doublet.10 The outer dynein arms are distributed along the length of the A tubule, with a constant spacing of 24 nm.
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Abstract Axonemal dynein forms a double row of projections, the outer and inner arms, that are attached to the A tubule of each axonemal doublet and extend toward the B tubule of the adjacent doublet.10 The outer dynein arms are distributed along the length of the A tubule, with a constant spacing of 24 nm.
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Axonemal dynein - a natural molecular motor
Nanotechnology, 1999Biological motor molecules possess many of the characteristics required to power nanomachines. They can generate force and torque, transport specific cargoes over appropriate substrates, and the character and rate of their action can be controlled.
Helen C Taylor, Michael E J Holwill
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Inherently disordered regions of axonemal dynein assembly factors
Cytoskeleton, 2023AbstractThe dynein‐driven beating of cilia is required to move individual cells and to generate fluid flow across surfaces and within cavities. These motor enzymes are highly complex and can contain upwards of 20 different protein components with a total mass approaching 2 MDa.
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