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Dynactin has two antagonistic regulatory domains and exerts opposing effects on dynein motility

Takuya Kobayashi, Takuya Miyashita, Takashi Murayama, Yoko Y. Toyoshima
doi: https://doi.org/10.1101/110775
Takuya Kobayashi
Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Meguro-ku, Tokyo, Japan
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Takuya Miyashita
Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Meguro-ku, Tokyo, Japan
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Takashi Murayama
Department of Pharmacology, Juntendo University School of Medicine, Bunkyo-ku, Tokyo, Japan
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Yoko Y. Toyoshima
Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Meguro-ku, Tokyo, Japan
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  • For correspondence: cyytoyo@mail.ecc.u-tokyo.ac.jp
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Abstract

Dynactin is a dynein-regulating protein that increases the processivity of dynein movement on microtubules. Recent studies have shown that a tripartite complex of dynein–dynactin–Bicaudal D2 is essential for highly processive movement. To elucidate the regulation of dynein motility by dynactin, we focused on two isoforms (A and B) of dynactin 1 (DCTN1), the largest subunit of dynactin that contains both microtubule- and dynein-binding domains. The only difference between the primary structures of the two isoforms is that DCTN1B lacks the K-rich domain, a cluster of basic residues. We measured dynein motility by single molecule observation of recombinant dynein and dynactin. Whereas the tripartite complex containing DCTN1A exhibited highly processive movement, the complex containing DCTN1B dissociated from microtubules with no apparent processive movement. This inhibitory effect of DCTN1B was caused by reductions of the microtubule-binding affinities of both dynein and dynactin, which is attributed to the coiled-coil 1 domain of DCTN1. In DCTN1A, the K-rich domain antagonized these inhibitory effects. Therefore, dynactin has two antagonistic domains and promotes or suppresses dynein motility to accomplish correct localization and functions of dynein within a cell.

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Posted February 24, 2017.
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Dynactin has two antagonistic regulatory domains and exerts opposing effects on dynein motility
Takuya Kobayashi, Takuya Miyashita, Takashi Murayama, Yoko Y. Toyoshima
bioRxiv 110775; doi: https://doi.org/10.1101/110775
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Dynactin has two antagonistic regulatory domains and exerts opposing effects on dynein motility
Takuya Kobayashi, Takuya Miyashita, Takashi Murayama, Yoko Y. Toyoshima
bioRxiv 110775; doi: https://doi.org/10.1101/110775

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