Abstract
fusion while chelators with either a lower or higher binding constant do not (6). Therefore, the lack of a strong inhibitory effect of BAPTA on MLCK activity suggests that the binding constant for calmodulin lies outside the range of calcium fluctuations reported for BAPTA (1). The generation of sliding forces between anti-parallel actin filaments is a well-established activity of bipolar filaments of myosin-II. Therefore, the observation that actin filaments selforganized and moved in an anti-parallel fashion in these extracts fits current models of the contractile ring. These data support models in which the bundling of actin filaments involves a calcium-sensitive step. Calcium signaling through Rho G-protein pathways, which modulate the actin cytoskeleton, is the most likely mechanism by which cytosolic Ca controls actin bundle formation (7). The involvement of actin bundling activity in the formation of contractile rings has yet to be established, although these data raise such a possibility. Supported by NSF grant IBN-0131470 and MBL Shifman award to RFT.
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