Unconventional motoring: an overview of the Kin C and Kin I kinesins.
All kinesins share a conserved core motor domain implying a common mechanism for generating force from ATP hydrolysis. How is it then that kinesins exhibit such divergent activities: motility, microtubule cross-linking and microtubule depolymerization? Although conventional motile kinesins have served as the paradigm for understanding kinesin function, the unconventional kinesins exploit variations on the motile theme to perform unexpected tasks. This review summarizes the biological functions and examines the possible molecular mechanisms of Kin C and Kin I unconventional kinesins. We also discuss the possible differences between the microtubule destabilization models proposed for Kar3 and Kin I kinesins.
Ovechkina
Yulia
Y
University of Washington School of Medicine, Department of Physiology and Biophysics, Seattle, WA 98195, USA.
Wordeman
Linda
L
D000818:Animals; D002148:Calmodulin-Binding Proteins / Q000737:chemistry / Q000502:physiology*; D002453:Cell Cycle / Q000502:physiology; D017124:Conserved Sequence; D006801:Humans; D016547:Kinesins / Q000737:chemistry / Q000502:physiology*; D008954:Models, Biological; D020409:Molecular Motor Proteins / Q000502:physiology*
D002148:Calmodulin-Binding Proteins; D020409:Molecular Motor Proteins; C402502:kinesin-C protein, Strongylocentrotus purpuratus; D016547:Kinesins