Genre
Journal ArticleDate
2016-05-09Author
Pyrpassopoulos, SArpaǧ, G
Feeser, EA
Shuman, H
Tüzel, E
Ostap, EM
Subject
Actin CytoskeletonActins
Animals
Biomechanical Phenomena
Cell Membrane
Computer Simulation
Diffusion
Lipids
Mice
Models, Molecular
Myosin Type I
Optical Tweezers
Protein Transport
Permanent link to this record
http://hdl.handle.net/20.500.12613/5054
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10.1038/srep25524Abstract
Vertebrate myosin-IC (Myo1c) is a type-1 myosin that links cell membranes to the cytoskeleton via its actin-binding motor domain and its phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P 2)-binding tail domain. While it is known that Myo1c bound to PtdIns(4,5)P 2 in fluid-lipid bilayers can propel actin filaments in an unloaded motility assay, its ability to develop forces against external load on actin while bound to fluid bilayers has not been explored. Using optical tweezers, we measured the diffusion coefficient of single membrane-bound Myo1c molecules by force-relaxation experiments, and the ability of ensembles of membrane-bound Myo1c molecules to develop and sustain forces. To interpret our results, we developed a computational model that recapitulates the basic features of our experimental ensemble data and suggests that Myo1c ensembles can generate forces parallel to lipid bilayers, with larger forces achieved when the myosin works away from the plane of the membrane or when anchored to slowly diffusing regions.Citation to related work
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http://dx.doi.org/10.34944/dspace/5036