期刊
NATURE COMMUNICATIONS
卷 5, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms6295
关键词
-
资金
- Ministry of Education, Science, Sports and Culture of Japan
- Knowledge Cluster Initiative (Stage-2) Research Foundation
- Uehara Memorial Foundation (Japan) for the Promotion of Science
- Japan Society for the Promotion of Science (JSPS) [26293066]
- Ministry of Education, Culture, Sports, Science and Technology (MEXT) [23113723]
- Strategic Research (Exploratory Research) in Osaka-City University
- Takeda Science Foundation
- NOVARTIS Foundation
- Cooperative Research Program of 'Network Joint Research Center for Materials and Devices'
- Grants-in-Aid for Scientific Research [26293066] Funding Source: KAKEN
Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. However, the regulatory mechanism underlying release of dynactin bound cargoes from dynein motor remains largely unknown. Here we report that ADP-ribosylation factor-like 3 (Arl3) and dynein light chain LC8 induce dissociation of dynactin from dynein. Immunoprecipitation and microtubule pull-down assays revealed that Arl3(Q71L) and LC8 facilitated detachment of dynactin from dynein. We also demonstrated Arl3(Q71L) or LC8-mediated dynactin release from a dynein-dynactin complex through trace experiments using quantum dot (Qdot)-conjugated proteins. Furthermore, we disclosed interactions of Arl3 and LC8 with dynactin and dynein, respectively, by live-cell imaging. Finally, knockdown (KD) of Arl3 and LC8 by siRNA induced abnormal localizations of dynein, dynactin and related organelles. Our findings uncovered the surprising functional relevance of GTP-bound Arl3 and LC8 for the unloading regulation of dynactin-bound cargo from dynein motor.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据