Transportation of Nanoscale Cargoes by Myosin Propelled Actin FilamentsShow others and affiliations
2013 (English)In: PLOS ONE, E-ISSN 1932-6203, Vol. 8, no 2, article id e55931
Article in journal (Refereed) Published
Abstract [en]
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 mu m) 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.
Place, publisher, year, edition, pages
Public Library of Science , 2013. Vol. 8, no 2, article id e55931
National Category
Biophysics Biochemistry and Molecular Biology Medical Biotechnology
Identifiers
URN: urn:nbn:se:oru:diva-99362DOI: 10.1371/journal.pone.0055931ISI: 000315186000012Scopus ID: 2-s2.0-84874337312OAI: oai:DiVA.org:oru-99362DiVA, id: diva2:1663611
Funder
Carl Tryggers foundation European Commission, 228971Swedish Research Council, 621-2007-6137 621-210-5146
Note
Funding agencies:
Faculty of Natural Sciences and Engineering at Linnaeus University
Netherlands Organization for Scientific Research (NWO) 700.57.427
2022-06-022022-06-022022-06-09Bibliographically approved