TY - GEN
T1 - Analysis of the regulation of actin cytoskeleton dynamics using dronpa, a photochromic fluorescent protein
AU - Ohashi, Kazumasa
AU - Kiuchi, Tai
AU - Nagai, Tomoaki
AU - Mizuno, Kensaku
PY - 2008
Y1 - 2008
N2 - Cofllin stimulates actin filament disassembly by severing and depolymerizing actin filaments and accelerates actin filament turnover. It is unclear whether cofilin contributes to stimulus-induced actin filament assembly by supplying actin monomers for polymerization or by creating free barbed ends through its severing activity. By measuring the time-lapse fluorescence decay of photoactivated Dronpa-actin, we have assessed the cytoplasmic actin monomer pool in living cells and provide evidence that cofllin is involved in production of more than half of the actin monomers in the cytoplasm. Actin monomers in the cytoplasm were incorporated into the tip of the lamellipodium, and incorporation depended both on cofllin activity and on the size of the cytoplasmic actin monomer pool. We therefore propose that cofllin critically contributes to stimulus-induced actin filament assembly and lamellipodium formation by supplying actin monomers abundantly to the cytoplasm.
AB - Cofllin stimulates actin filament disassembly by severing and depolymerizing actin filaments and accelerates actin filament turnover. It is unclear whether cofilin contributes to stimulus-induced actin filament assembly by supplying actin monomers for polymerization or by creating free barbed ends through its severing activity. By measuring the time-lapse fluorescence decay of photoactivated Dronpa-actin, we have assessed the cytoplasmic actin monomer pool in living cells and provide evidence that cofllin is involved in production of more than half of the actin monomers in the cytoplasm. Actin monomers in the cytoplasm were incorporated into the tip of the lamellipodium, and incorporation depended both on cofllin activity and on the size of the cytoplasmic actin monomer pool. We therefore propose that cofllin critically contributes to stimulus-induced actin filament assembly and lamellipodium formation by supplying actin monomers abundantly to the cytoplasm.
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U2 - 10.1109/MHS.2008.4752470
DO - 10.1109/MHS.2008.4752470
M3 - Conference contribution
AN - SCOPUS:62449257001
SN - 9781424429196
T3 - 2008 International Symposium on Micro-NanoMechatronics and Human Science, MHS 2008
SP - 317
EP - 322
BT - 2008 International Symposium on Micro-NanoMechatronics and Human Science, MHS 2008, with Symposium on "COE for Education and Research of Micro-Nano Mechatronics"
T2 - 2008 International Symposium on Micro-NanoMechatronics and Human Science, MHS 2008, with Symposium on "COE for Education and Research of Micro-Nano Mechatronics", Symposium on "System Cell Engineering by Multi-scale Manipulation"
Y2 - 6 November 2008 through 9 November 2008
ER -