Transportation of nanoscale cargoes by myosin propelled actin filaments.
Myosin II propelled actin filaments move ten times faster than kinesin driven microtubules and are thus attractive candidates as cargo-transporting shuttles in motor driven lab-on-a-chip devices. In addition, actomyosin-based transportation of nanoparticles is useful in various fundamental studies....
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doaj-df1d70aacbce459d8e838e4c6778b9ab2020-11-25T01:14:18ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0182e5593110.1371/journal.pone.0055931Transportation of nanoscale cargoes by myosin propelled actin filaments.Malin PerssonMaria GullbergConny TolfA Michael LindbergAlf MånssonArmagan KocerMyosin II propelled actin filaments move ten times faster than kinesin driven microtubules and are thus attractive candidates as cargo-transporting shuttles in motor driven lab-on-a-chip devices. In addition, actomyosin-based transportation of nanoparticles is useful in various fundamental studies. However, it is poorly understood how actomyosin function is affected by different number of nanoscale cargoes, by cargo size, and by the mode of cargo-attachment to the actin filament. This is studied here using biotin/fluorophores, streptavidin, streptavidin-coated quantum dots, and liposomes as model cargoes attached to monomers along the actin filaments ("side-attached") or to the trailing filament end via the plus end capping protein CapZ. Long-distance transportation (>100 µm) could be seen for all cargoes independently of attachment mode but the fraction of motile filaments decreased with increasing number of side-attached cargoes, a reduction that occurred within a range of 10-50 streptavidin molecules, 1-10 quantum dots or with just 1 liposome. However, as observed by monitoring these motile filaments with the attached cargo, the velocity was little affected. This also applied for end-attached cargoes where the attachment was mediated by CapZ. The results with side-attached cargoes argue against certain models for chemomechanical energy transduction in actomyosin and give important insights of relevance for effective exploitation of actomyosin-based cargo-transportation in molecular diagnostics and other nanotechnological applications. The attachment of quantum dots via CapZ, without appreciable modulation of actomyosin function, is useful in fundamental studies as exemplified here by tracking with nanometer accuracy.http://europepmc.org/articles/PMC3578877?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Malin Persson Maria Gullberg Conny Tolf A Michael Lindberg Alf Månsson Armagan Kocer |
spellingShingle |
Malin Persson Maria Gullberg Conny Tolf A Michael Lindberg Alf Månsson Armagan Kocer Transportation of nanoscale cargoes by myosin propelled actin filaments. PLoS ONE |
author_facet |
Malin Persson Maria Gullberg Conny Tolf A Michael Lindberg Alf Månsson Armagan Kocer |
author_sort |
Malin Persson |
title |
Transportation of nanoscale cargoes by myosin propelled actin filaments. |
title_short |
Transportation of nanoscale cargoes by myosin propelled actin filaments. |
title_full |
Transportation of nanoscale cargoes by myosin propelled actin filaments. |
title_fullStr |
Transportation of nanoscale cargoes by myosin propelled actin filaments. |
title_full_unstemmed |
Transportation of nanoscale cargoes by myosin propelled actin filaments. |
title_sort |
transportation of nanoscale cargoes by myosin propelled actin filaments. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2013-01-01 |
description |
Myosin II propelled actin filaments move ten times faster than kinesin driven microtubules and are thus attractive candidates as cargo-transporting shuttles in motor driven lab-on-a-chip devices. In addition, actomyosin-based transportation of nanoparticles is useful in various fundamental studies. However, it is poorly understood how actomyosin function is affected by different number of nanoscale cargoes, by cargo size, and by the mode of cargo-attachment to the actin filament. This is studied here using biotin/fluorophores, streptavidin, streptavidin-coated quantum dots, and liposomes as model cargoes attached to monomers along the actin filaments ("side-attached") or to the trailing filament end via the plus end capping protein CapZ. Long-distance transportation (>100 µm) could be seen for all cargoes independently of attachment mode but the fraction of motile filaments decreased with increasing number of side-attached cargoes, a reduction that occurred within a range of 10-50 streptavidin molecules, 1-10 quantum dots or with just 1 liposome. However, as observed by monitoring these motile filaments with the attached cargo, the velocity was little affected. This also applied for end-attached cargoes where the attachment was mediated by CapZ. The results with side-attached cargoes argue against certain models for chemomechanical energy transduction in actomyosin and give important insights of relevance for effective exploitation of actomyosin-based cargo-transportation in molecular diagnostics and other nanotechnological applications. The attachment of quantum dots via CapZ, without appreciable modulation of actomyosin function, is useful in fundamental studies as exemplified here by tracking with nanometer accuracy. |
url |
http://europepmc.org/articles/PMC3578877?pdf=render |
work_keys_str_mv |
AT malinpersson transportationofnanoscalecargoesbymyosinpropelledactinfilaments AT mariagullberg transportationofnanoscalecargoesbymyosinpropelledactinfilaments AT connytolf transportationofnanoscalecargoesbymyosinpropelledactinfilaments AT amichaellindberg transportationofnanoscalecargoesbymyosinpropelledactinfilaments AT alfmansson transportationofnanoscalecargoesbymyosinpropelledactinfilaments AT armagankocer transportationofnanoscalecargoesbymyosinpropelledactinfilaments |
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