Dynein Structure and Function
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چکیده
The structure of dynein isolated from several sources follows the pattern first observed with Tetrahymena 22 S dynein, which has three globular heads attached by three flexible strands to a root-like base. Recent biochemical data indicate that there is one ATPase site on each dynein head and that all three heads interact with microtubules in an ATP-sensitive manner. Accordingly, images of dynein in situ can be interpreted in terms of a model for crossbridge action where the roots of the bouquet anchor the dynein to the A-tubule and all three heads reach out to interact with the B-tubule in an ATP-dependent reaction to produce a force for sliding.
منابع مشابه
The effect of endurance training on dynein motor protein expression in Wistar male rats sciatic nerves with diabetic neuropathy
Introduction: Most neurodegenerative diseases are associated with the disruption of axonal transport and this might also be related to diabetes-associated disorders affecting the nervous system. Cytoplasmic dynein is a very important motor driving the movement of a wide range of cargoes toward the minus ends of microtubules. The effects of endurance training on dynein motor protein expression i...
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Cytoplasmic dynein transports cargoes for a variety of crucial cellular functions. However, since dynein is essential in most eukaryotic organisms, the in-depth study of the cellular function of dynein via genetic analysis of dynein mutations has not been practical. Here, we identify and characterize 34 different dynein heavy chain mutations using a genetic screen of the ascomycete fungus Neuro...
متن کاملThe third P-loop domain in cytoplasmic dynein heavy chain is essential for dynein motor function and ATP-sensitive microtubule binding.
Sequence comparisons and structural analyses show that the dynein heavy chain motor subunit is related to the AAA family of chaperone-like ATPases. The core structure of the dynein motor unit derives from the assembly of six AAA domains into a hexameric ring. In dynein, the first four AAA domains contain consensus nucleotide triphosphate-binding motifs, or P-loops. The recent structural models ...
متن کاملThe role of dynein in microtubule-based motility.
Dyneins are high molecular weight ATPases that function as microtubule-based molecular motors. The axonemal dyneins, discovered 30 years ago, are responsible for the beating movement of cilia and sperm flagella, which they generate by producing sliding between adjacent microtubules. Cytoplasmic dynein, more recently discovered, is involved in diverse activities, including intracellular transpor...
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Intracellular active transport is driven by ATP-hydrolyzing motor proteins that move along cytoskeletal filaments. In particular, the microtubule-associated dynein motor is involved in the transport of organelles and vesicles, the maintenance of the Golgi, and mitosis. However, unlike kinesin and myosin, the mechanism by which dynein converts chemical energy into mechanical force remains largel...
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