1. Department of Zoology, University of Wisconsin, Madison, Madison, Wisconsin 53706, USA
2. Program in Cellular and Molecular Biology, University of Wisconsin, Madison, Madison, Wisconsin 53706, USA
3. Department of Cell and Molecular Physiology, University of North Carolina, Chapel Hill, Chapel Hill, North Carolina 27599, USA
4. Present addresses: Department of Cell Biology, CB163, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, USA (K.L.W.); Department of Molecular Biology, Princeton University, Washington Road, Princeton, New Jersey 08544, USA (A.M.S.)

Correspondence to: William M. Bement^1,2 Email: wmbement@wisc.edu

Abstract

Proper spindle positioning and orientation are essential for asymmetric cell division and require microtubule–actin filament (F-actin) interactions in many systems^{1, 2}. Such interactions are particularly important in meiosis³, where they mediate nuclear anchoring^{4, 5, 6}, as well as meiotic spindle assembly and rotation^{7, 8}, two processes required for asymmetric cell division. Myosin-10 proteins are phosphoinositide-binding⁹, actin-based motors that contain carboxy-terminal MyTH4 and FERM domains of unknown function¹⁰. Here we show that Xenopus laevis myosin-10 (Myo10) associates with microtubules in vitro and in vivo, and is concentrated at the point where the meiotic spindle contacts the F-actin-rich cortex. Microtubule association is mediated by the MyTH4-FERM domains, which bind directly to purified microtubules. Disruption of Myo10 function disrupts nuclear anchoring, spindle assembly and spindle–F-actin association. Thus, this myosin has a novel and critically important role during meiosis in integrating the F-actin and microtubule cytoskeletons.

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