| Project/Area Number |
18570154
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | Fukuoka University (2007)
Kyushu Institute of Technology (2006) |
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Principal Investigator |
NAKAGAWA Hiroyuki (2007) Fukuoka University, Faculty of Science, Associate Professor (80274562)
宮本 茂昭 (2006) 九州工業大学, 情報工学部, 教授 (40219811)
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| Co-Investigator(Kenkyū-buntansha) |
中川 裕之 福岡大学, 理学部, 助教授 (80274562)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥3,860,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥360,000)
Fiscal Year 2007: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2006: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | actin / lasp-2 / actin bundle / fascin |
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| Research Abstract |
Actin filaments are organized into sub-compartments of meshwork and bundles in lamellipodia. Polymerization of actin molecules into filament produces a mechanical force for cell movement. Organization of these filaments is through to be regulated by actin filament binding proteins. Localization of fascin, the LIM and SH3 domain protein 1 (lasp-1), and lasp-2 to the bundles suggest their involvement in that organization; however, their contributions remain unclear. We have compared the turnover of these proteins with actin at the bundle. After photobleaching, EGFP-actin recovered inwards from the bundle tip, consistent with the retrograde flow by treadmilling. In contrast, the recovery of EGFP-fascin, -lasp-1 and -lasp-2 occurred from the anterograde direction. These results suggest that these molecules would participate in the stabilization of bundles but not in initiation.
Lasp-2 has been identified to have three domains : a LIM domain, nebulin-repeat domain and an SH3 domain in lasp-2 ; however, the region responsible for actin-binding is still unclear. We have expressed lasp-2 fragments tagged with EGFP in NG108-15 and C2C12 cells. We showed that the N-terminal fragment from the LIM domain to the first nebulin-repeat module retained actin-binding activity and a similar subcellular localization to full-length lasp-2, but the LIM domain fragment did not. Partial truncation of the LIM domain caused the loss of actin-binding activity and subcellular localization. These results suggest that lasp-2 interaction with F-actin is mediated by the cooperation of the LIM domain and first nebulin-repeat module both in vitro and in vivo.
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