2004 Fiscal Year Final Research Report Summary
Roles of WAVE in transformation of cell signals to filopodia protrusion at neuronal growth cone
| Project/Area Number |
15570136
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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 | Kyushu Institute of Technology |
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Principal Investigator |
MIYAMOTO Shigeaki Kyushu Institute of Technology, Faculty of Computer Science and Systems Engineering, Professor, 情報工学部, 教授 (40219811)
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| Co-Investigator(Kenkyū-buntansha) |
SHIGEAKI Hiroyuki Kyushu Institute of Technology, Faculty of Computer Science and Systems Engineering, Assistant Professor, 情報工学部, 助手 (80274562)
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| Project Period (FY) |
2003 – 2004
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| Keywords | growth cone / lamellipodia / filopodia / WAVE / actin / fascin / Lasp-1 / Lasp-2 |
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| Research Abstract |
Neuronal cells extend the growth cones forming lamellipodia and filopodia in the response to the external guidance factors. The reorganization of actin cytoskeleton supply the mechanical force in these process formations, and actin bundle grown in this process form a core of filopodium. We have studied the roles of WAVEs that transfer cell signals from small G-protein, Rho, to the rearrangements of actin network. By expressing WAVE isoforms tagged with fluorescent proteins in NG108 we obtained the following results.
(1)WAVE1 localized only at the leading edge of lamellipodia, and WAVE2 and WAVE3 were localized also at the tips of filopodia. Especially WAVE2 were concentrated.
(2)We identified the leucine-zipper like motif between 52th and 82th of WAVE2 at amino terminal controlled the localization at filopodium tip.
(3)The factors that bundle actin filaments are necessary to elongate the filopodia. We show that fascin takes a role to bundle actin filaments in filopodia.
(4)A novel protein family, Lasp-family(Lasp-1 and Lasp-2), bundle the actin filaments in filopodia similarly to fascin.
(5)Lasp-1,Lasp-2 and fascin interact with actin bundle by non-covalent bond, independently of retrograde flow of actins.
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