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|Title:||A coordinated molecular 'fishing' mechanism in heterodimeric kinesin||Authors:||Hou, R.
|Issue Date:||Sep-2010||Citation:||Hou, R., Wang, Z. (2010-09). A coordinated molecular 'fishing' mechanism in heterodimeric kinesin. Physical Biology 7 (3) : -. ScholarBank@NUS Repository. https://doi.org/10.1088/1478-3975/7/3/036003||Abstract:||Kar3 is a kinesin motor that facilitates chromosome segregation during cell division. Unlike many members of the kinesin superfamily, Kar3 forms a heterodimer with non-motor protein Vik1 or Cik1 in vivo. The heterodimers show ATP-driven minus-end directed motility along a microtubule (MT) lattice, and also serve as depolymerase at the MT ends. The molecular mechanisms behind this dual functionality remain mysterious. Here, a molecular mechanical model for the Kar3/Vik1 heterodimer based on structural, kinetic and motility data reveals a long-range chemomechanical transmission mechanism that resembles a familiar fishing tactic. By this molecular 'fishing', ATP-binding to Kar3 dissociates catalytically inactive Vik1 off MT to facilitate minus-end sliding of the dimer on the MT lattice. When the dimer binds the frayed ends of MT, the fishing channels ATP hydrolysis energy into MT deploymerization by a mechanochemical effect. The molecular fishing thus provides a unified mechanistic ground for Kar3's dual functionality. The fishing-promoted depolymerization differs from the depolymerase mechanisms found in homodimeric kinesins. The fishing also enables intermolecular coordination with a chemomechanical coupling feature different from the paradigmatic pattern of homodimeric motors. This study rationalizes some puzzling experimental observation, and suggests new experiments for further elucidation of the fishing mechanism. © 2010 IOP Publishing Ltd.||Source Title:||Physical Biology||URI:||http://scholarbank.nus.edu.sg/handle/10635/95614||ISSN:||14783975||DOI:||10.1088/1478-3975/7/3/036003|
|Appears in Collections:||Staff Publications|
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