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摘要: Kinesin motor proteins produce motion and force along microtubules and are essential for the organization of subcellular components (Vale, 2003). The kinesin superfamily is divided into 14 subfamilies that carry out a variety of biological functions (Miki et al., 2005). In spite of their diversity, Kinesin motors all share a conserved catalytic domain that binds to microtubule and hydrolyzes ATP (Vale and Milligan, 2000). The two studies presented here are examples of how kinesin motors can be uniquely adapted to perform their specific cellular functions. The first study focuses on the Kinesin-14 family member Ncd. Most kinesin motors, exemplified by Kinesin-1, move towards the microtubule plus end, and the structural changes that govern this directional preference have been described (Rice et al., 1999). In contrast, the structural changes underlying the minus-end-directed motility of Kinesin-14 motors are less well …