Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 108, Issue 14, Pages 5566-5571Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1101415108
Keywords
unconventional myosins; cytoskeleton; trafficking
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Funding
- National Institutes of Health/National Institute of General Medical Sciences [R01-GM084947]
- National Institutes of Health [GM33289]
- Human Frontiers Science Program
- National Institutes of Health Cell and Molecular Biology [T32-GM007276]
- Stanford Graduate Fellowships
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Myosin VI is a molecular motor implicated in many processes, and it likely associates with a variety of cargoes that specify its functions. Although it is critical to Drosophila development, little is known about its cellular roles. To reveal its involvement in specific pathways, we sought to identify the binding partners of Drosophila myosin VI. We used affinity chromatography and mass spectrometry to discover interacting proteins, which we tested for direct binding. Using this approach, we found that the microtubule-associated protein Cornetto bound myosin VI, and we demonstrated a role for both in secretion of the lipidated morphogen Hedgehog. We also identified a number of other binding proteins, and further characterization of their interactions with myosin VI will advance our understanding of the roles of these complexes in cellular and developmental processes. Thus, our method has provided us the means to gain valuable insight into the multifaceted roles of a motor protein in vivo.
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