A novel form of motility in filopodia revealed by imaging myosin-X at the single-molecule level.

A novel form of motility in filopodia revealed by imaging myosin-X at the single-molecule level.
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DOI:
10.1016/j.cub.2009.03.067
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发表时间:
2009-06-09
期刊:
Current biology : CB
影响因子:
--
通讯作者:
Cheney RE
Cheney RE
中科院分区:
其他
文献类型:
--
作者:
Kerber ML;Jacobs DT;Campagnola L;Dunn BD;Yin T;Sousa AD;Quintero OA;Cheney RE

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Although many proteins, receptors, and viruses are transported rearward along filopodia by retrograde actin flow, it is less clear how molecules move forward in filopodia. Myosin-X (Myo10) is an actin-based motor hypothesized to use its motor activity to move forward along actin filaments to the tips of filopodia. Here we use a sensitive total internal reflection fluorescence (TIRF) microscopy system to directly visualize the movements of GFP-Myo10. This reveals a novel form of motility at or near the single-molecule level in living cells wherein extremely faint particles of Myo10 move in a rapid and directed fashion towards the filopodial tip. These fast forward movements occur at ∼600 nm/s over distances of up to ∼10 μm and require Myo10 motor activity and actin filaments. As expected for imaging at the single-molecule level, the faint particles of GFP-Myo10 are diffraction-limited, have an intensity range similar to single GFP molecules, and exhibit stepwise bleaching. Faint particles of GFP-Myo5a can also move towards the filopodial tip, but at a slower characteristic velocity of ∼250 nm/s. Similar movements were not detected with GFP-Myo1a, indicating that not all myosins are capable of intrafilopodial motility. These data indicate the existence of a novel system of long-range transport based on the rapid movement of myosin molecules along filopodial actin filaments.
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影响因子: --
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