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J. Biol. Chem., Vol. 283, Issue 1, 380-387, January 4, 2008

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Filament-dependent and -independent Localization Modes of Drosophila Non-muscle Myosin II^*

From the Institute of Molecular Biology and Department of Chemistry, University of Oregon, Eugene, Oregon 97403

Myosin II assembles into force-generating filaments that drive cytokinesis and the organization of the cell cortex. Regulation of myosin II activity can occur through modulation of filament assembly and by targeting to appropriate cellular sites. Here we show, using salt-dependent solubility and a novel fluorescence resonance energy transfer assay, that assembly of the Drosophila non-muscle myosin II heavy chain, zipper, is mediated by a 90-residue region (1849–1940) of the coiled-coil tail domain. This filament assembly domain, transiently expressed in Drosophila S2 cells, does not localize to the interphase cortex or the cytokinetic cleavage furrow, whereas a 500-residue region (1350–1865) that overlaps the NH₂ terminus of the assembly domain localizes to the interphase cortex but not the cytokinetic cleavage furrow. Targeting to these two sites appears to utilize distinct localization mechanisms as the assembly domain is required for cleavage furrow recruitment of a truncated coiled-coil tail region but not targeting to the interphase cortex. These results delineate the requirements for zipper filament assembly and indicate that the ability to form filaments is necessary for targeting to the cleavage furrow but not to the interphase cortex.

Received for publication, May 14, 2007 , and in revised form, September 25, 2007.

^* This work was supported by a Damon Runyon Scholar Award and National Institutes of Health Grant GM068032. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental movies S1–S5.

¹ To whom correspondence should be addressed: Inst. of Molecular Biology, 1229 University of Oregon, Eugene, OR 97403. E-mail: prehoda{at}molbio.uoregon.edu.

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