Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 109, Issue 43, Pages 17388-17393Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1208642109
Keywords
Myo10; molecular motor; filopodial growth
Categories
Funding
- Hong Kong Jockey Club
- Research Grants Council of Hong Kong [SEG_HKUST06]
- RGC of Hong Kong [SEG_HKUST06, 663808, 664009, 660709, 663610, 663811, HKUST6/CRF/10, HKUST6/CRF/09, 662710]
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Processive movements of unconventional myosins on actin filaments generally require motor dimerization. A commonly accepted myosin dimerization mechanism is via formation of a parallel coiled-coil dimer by a stretch of amino acid residues immediately carboxyl-terminal to the motor's lever-arm domain. Here, we discover that the predicted coiled-coil region of myosin X forms a highly stable, antiparallel coiled-coil dimer (anti-CC). Disruption of the anti-CC either by single-point mutations or by replacement of the anti-CC with a parallel coiled coil with a similar length compromised the filopodial induction activity of myosin X. We further show that the anti-CC and the single a-helical domain of myosin X are connected by a semirigid helical linker. The anti-CC-mediated dimerization may enable myosin X to walk on both single and bundled actin filaments.
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