Propulsion of organelles isolated from Acanthamoeba along actin filaments by myosin-I View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1986-08

AUTHORS

Richard J. Adams, Thomas D. Pollard

ABSTRACT

Eukaryotic cells are dependent on their ability to translocate membraneous elements about the cytoplasm. In many cells long translocations of organelles are associated with microtubules1–3. In other cases, such as the rapid cytoplasmic streaming in some algae, organelles appear to be propelled along actin filaments4. It has been assumed, but not proven, that myosin produces these movements. We have tested vesicles from another eukaryotic cell for their ability to move on the exposed actin bundles of Nitella5 as an indiction that actin-based organelle movements may be a general property of cells. We found that organelles from Acanthamoeba castellanii can move along Nitella actin filaments. Here, we report two different experiments indicating that the single-headed non-polymerizable myosin isozyme myosin-I (ref. 6) is responsible for this organelle motility. First, monoclonal antibodies to myosin-I inhibit movement, but antibodies that inhibit double-headed myosin-II do not. Second, ∼20% of the myosin-I in homogenates co-migrates with motile vesicles during Percoll density-gradient ultracentrifugation. This is the first indication of a role for myosin-I within the cell and supports the suggestion of Albanesi et al.7 that myosin-I moves vesicles in this way. More... »

PAGES

754-756

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/322754a0

DOI

http://dx.doi.org/10.1038/322754a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1023150215

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/3748157


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