Actin structure-dependent stepping of myosin 5a and 10 during processive movement

How myosin 10, an unconventional myosin, walks processively along actin is still controversial. Here, we used single molecule fluorescence techniques, TIRF and FIONA, to study the motility and the stepping mechanism of dimerized myosin 10 heavy-meromyosin-like fragment on both single actin filaments...

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Published inPloS one Vol. 8; no. 9; p. e74936
Main Authors Bao, Jianjun, Huck, Daniel, Gunther, Laura K, Sellers, James R, Sakamoto, Takeshi
Format Journal Article
LanguageEnglish
Published United States Public Library of Science 19.09.2013
Public Library of Science (PLoS)
Subjects
Actin
Actin Cytoskeleton - chemistry
Actin Cytoskeleton - physiology
Actins - chemistry
Actins - physiology
Actins - ultrastructure
Animals
Astronomy
Biochemistry
Carrier Proteins - chemistry
Carrier Proteins - physiology
Cellular structure
Crosslinking
Filaments
Fluorescence
Microfilament Proteins - chemistry
Microfilament Proteins - physiology
Microscopy
Models, Biological
Motility
Muscle proteins
Myosin
Myosins - chemistry
Myosins - physiology
Physics
Proteins
Rabbits
Rafts
Selectivity
Studies
α-Actinin
United States > US
Detroit Michigan
Michigan
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Summary:How myosin 10, an unconventional myosin, walks processively along actin is still controversial. Here, we used single molecule fluorescence techniques, TIRF and FIONA, to study the motility and the stepping mechanism of dimerized myosin 10 heavy-meromyosin-like fragment on both single actin filaments and two-dimensional F-actin rafts cross-linked by fascin or α-actinin. As a control, we also tracked and analyzed the stepping behavior of the well characterized processive motor myosin 5a. We have shown that myosin 10 moves processively along both single actin filaments and F-actin rafts with a step size of 31 nm. Moreover, myosin 10 moves more processively on fascin-F-actin rafts than on α-actinin-F-actin rafts, whereas myosin 5a shows no such selectivity. Finally, on fascin-F-actin rafts, myosin 10 has more frequent side steps to adjacent actin filaments than myosin 5a in the F-actin rafts. Together, these results reveal further single molecule features of myosin 10 on various actin structures, which may help to understand its cellular functions.
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Competing Interests: The authors have declared that no competing interests exist.
Conceived and designed the experiments: TS. Performed the experiments: JB DH LKG TS. Analyzed the data: JB DH LKG TS. Contributed reagents/materials/analysis tools: JB DH LKG JRS TS. Wrote the manuscript: JB DH LKG JRS TS. Designed the software used in analysis: DH.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0074936