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Vol. 15, Issue 1, 151-161, January 2004
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* Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520;
Department of Cell Biology and Pathology, Yale University, New Haven, Connecticut 06520
Submitted July 18, 2003;
Revised September 12, 2003;
Accepted September 23, 2003
Monitoring Editor: Ted Salmon
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 microtubule-associated protein-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 because microtubule-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.
Abbreviations used: IF, intermediate filament; MAP, microtubule-associated protein; MT, microtubule; Myo5a, myosin-Va.
Corresponding author. E-mail address: mark.mooseker{at}yale.edu.
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