bioRxiv (Cold Spring Harbor Laboratory) · 2018 · 22 citations · 30 references
Life SciencesCell BiologyMolecular BiologyCell DivisionCytoskeletonMolecular Cell BiologyCytoskeletal DynamicsCytoskeletal MechanicsCytoskeleton DynamicsMolecular MachinesMolecular MotorsMotor ProteinsDynein MotorsKinesin MotorsMicrotubule DisassemblyMicrotubule DynamicsMicrotubule InstabilityMicrotubule MechanicsMicrotubule-cytoskeleton CouplingTubulin Heterodimer Interactions
Microtubules are dynamic polymers that are used for intracellular transport and chromosome segregation during cell division. Their instability stems from the low energy of tubulin dimer interactions, which sets the growing polymer close to its disassembly conditions. Microtubules function in coordination with kinesin and dynein molecular motors, which use ATP hydrolysis to produce mechanical work and move on microtubules. This raises the possibility that the forces produced by walking motors can break dimer interactions and trigger microtubule disassembly. We tested this hypothesis by studying the interplay between microtubules and moving molecular motors in vitro. Our results show that the mechanical work of molecular motors can remove tubulin dimers from the lattice and rapidly destroy microtubules. This effect was not observed when free tubulin dimers were present in the assay. Using fluorescently labelled tubulin dimers we found that dimer removal by motors was compensated for by the insertion of free tubulin dimers into the microtubule lattice. This self-repair mechanism allows microtubules to survive the damage induced by molecular motors as they move along their tracks. Our study reveals the existence of coupling between the motion of kinesin and dynein motors and the renewal of the microtubule lattice.
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Movement of microtubules by single kinesin molecules
Jonathon Howard, A. J. Hudspeth, Ronald D. Vale · Nature · 1989 · 891 citations
Kinesin hydrolyses one ATP per 8-nm step
Mark J. Schnitzer, Steven M. Block · Nature · 1997 · 790 citations · Full text
N. J. Carter, Robert A. Cross · Nature · 2005 · 765 citations