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KMID : 0578319950050040299
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Molecules and Cells
1995 Volume.5 No. 4 p.299 ~ p.305
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The Structure and Function of Dynein heavy Chains
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David J. Asai
Lee Seung-won
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Abstract
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The translocation of dynein along microtubules is the basis for a wide variety of essential cellular movements. Organisms with cilia or flagella express many different dynein heavy chain genes, each of which corresponds to a distinct heavy chain isoform. Combinations of isoforms are precisely targeted to specific sites in the cell to perform specific tasks. Each dynein heavy chain contains a globular catalytic domain and an extended tethering domain. The catalytic domain includes the ATP-sensitive microtubule-binding site which must not only bind specifically to microtubules but also bind in an orientation so that dynein force transduction is directional with respect to the microtubule surface lattice. There are many important questions that remain unsolved. 1) How does the long dynein heavy chain fold into the compact head-tail structure? 2) What is the mechanism that underlies accurate intracellular targeting of dynein isoforms? 3) Where in the heavy chain sequence is the ATP-sensitive microtubule-binding site and what is the mechanism of force transduction?
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