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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Main Authors: Malin Persson, Maria Gullberg, Conny Tolf, A Michael Lindberg, Alf Månsson, Armagan Kocer
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3578877?pdf=render
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spelling 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
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