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A more recent version of this article appeared on January 1, 2004
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Submitted on July 18, 2003
Revised on September 12, 2003
Accepted on September 23, 2003
1 Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520
2 Department of Molecular, Cellular and Developmental Biology and Departments of Cell Biology and Pathology, Yale University, New Haven, CT 06520
* Corresponding author. E-mail address: mark.mooseker{at}yale.edu.
Myosin-Va was identified as a microtubule binding protein by
cosedimentation analysis in the presence of microtubules. Native
myosin-Va purified from chick brain, as well as the expressed globular
tail domain of this myosin, but not head domain bound to MAP-free
microtubules. Binding of myosin-Va to microtubules was saturable and of
moderately high affinity (
1:24 Myosin-Va: tubulin; Kd:
70 nM). Myosin-Va may bind to microtubules via its tail domain since
microtuble-bound myosin-Va retained the ability to bind actin filaments
resulting in the formation of cross-linked gels of microtubules and
actin, as assessed by fluorescence and electron microscopy. In low
Ca2+, ATP addition induced dissolution of these gels, but
not release of myosin-Va from MTs. However, in 10 µM
Ca2+, ATP addition resulted in the contraction of the gels
into aster-like arrays. These results demonstrate that myosin-Va is a
microtubule binding protein that cross-links and mechanochemically
couples microtubules to actin filaments.
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