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Transport of cytoplasmic particles catalysed by an unconventional myosin in living Drosophila embryos

Nature volume 369, pages 560–562 (1994)Cite this article

Abstract

MYOSINS are actin-activated ATPases that are able to translocate along actin filaments using energy derived from ATP hydrolysis. Non-muscle cells contain conventional myosins, which are similar in sequence and structure to muscle myosin, and a number of unconventional myosins whose head sequences are similar but tail sequences are unrelated to conventional myosins1. The myosin superfamily currently consists of nine classes2; Drosophila 95F is an unconventional myosin3 and the original member of class VI, which includes a homologue found in pig kidney2. Some unconventional myosins have been suggested as mediators of some types of intracellular transport4,5, but there is little direct evidence for this function (but see ref. 6). We have observed transport of cytoplasmic particles in live Drosophila embryos in three dimensions using computational optical sectioning microscopy. We present here evidence that this transport is actin-based, ATP-dependent and catalysed by one such unconventional myosin, the 95F myosin. This is, to our knowledge, the first direct observation of transport catalysed by an unconventional myosin in living cells.

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Authors and Affiliations

  1. Department of Biology, Washington University, St Louis, Missouri, 63130, USA

    Valerie Mermall, James G. McNally & Kathryn G. Miller

  2. lnstitute for Biomedical Computing, Washington University, St Louis, Missouri, 63130, USA

    James G. McNally

Authors
  1. Valerie Mermall
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  2. James G. McNally
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  3. Kathryn G. Miller
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Mermall, V., McNally, J. & Miller, K. Transport of cytoplasmic particles catalysed by an unconventional myosin in living Drosophila embryos. Nature 369, 560–562 (1994). https://doi.org/10.1038/369560a0

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