2013 Fiscal Year Final Research Report
Slow axonal transport driven by directional actin turnover
| Project/Area Number |
23370088
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Cell biology
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| Research Institution | Nara Institute of Science and Technology |
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Principal Investigator |
INAGAKI Naoyuki 奈良先端科学技術大学院大学, バイオサイエンス研究科, 准教授 (20223216)
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| Co-Investigator(Renkei-kenkyūsha) |
SUGIURA Tadao 奈良先端科学技術大学院大学, 情報科学研究科, 准教授 (60304010)
SAKUMURA Yuichi 愛知県立大学, 情報科学部, 准教授 (50324968)
TORIYAMA Michinori 奈良先端科学技術大学院大学, バイオサイエンス研究科, 研究員 (90457151)
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| Project Period (FY) |
2011-04-01 – 2014-03-31
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| Keywords | 脳・神経 / 発生・分化 / 神経科学 / 軸索輸送 / 細胞骨格 / 分子クラッチ / Shootin1 / アクチン線維 |
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| Research Abstract |
Although actin and associated proteins are essential for axonal extension, how they are transported along axons remains unclear. Here we show that actin filaments (F-actins) and associated proteins migrate toward the axonal growth cone by means of directional actin polymerization/depolymerization, called treadmilling. F-actins migrating along axonal shafts underwent treadmilling, with their polymerizing ends oriented toward the growth cone. F-actins were anchored to the plasma membrane through the cell adhesion molecule L1-CAM and the linker protein shootin1. Migration of F-actins depended on their polymerization and substrate anchorage, and directional counter-forces associated with F-actin migration were detected on the substrate. Actin-associated proteins co-migrated with F-actins by interacting with the filaments. Our findings reveal a new mode of intracellular transport, which supplies actin and associated proteins to the axonal leading edge, thereby promoting its protrusion.
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Research Products
(19 results)
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[Journal Article] Ceramic coating of liposomal gene carrier for minimizing toxicity to primary hippocampal neurons2013
Author(s)
Tahara, K., Moriuchi, T., Tsukui, M., Hirota, A., Maeno, T., Toriyama, M., Inagaki, N. and Kikuchi, J
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Journal Title
Chemistry Letters
Volume: 42
Pages: 1265-1267
Peer Reviewed
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