Shock of three-state model for intracellular transport of kinesin KIF1A

  title={Shock of three-state model for intracellular transport of kinesin KIF1A},
  author={Yunxin Zhang},
Recently, a three-state model is presented to describe the intracellular traffic of unconventional (single-headed) kinesin KIF1A [Phys. Rev. Lett. 95, 118101 (2005)], in which each motor can bind strongly or weakly to its microtubule track, and each binding site of the track might be empty or occupied by one motor. As the usual two-state model, i.e. the totally asymmetric simple exclusion process (TASEP) with motor detachment and attachment, in steady state of the system, this three-state model… 
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Intracellular transport by single-headed kinesin KIF1A: effects of single-motor mechanochemistry and steric interactions.

This model generalizes a lattice-gas model which describes traffic of unconventional (single-headed) kinesins KIF1A, introducing an interaction parameter c, to account for an interesting mechanochemical process.

Direct observation of the binding state of the kinesin head to the microtubule

A single-molecule assay is reported that can directly report head binding in a walking kinesin molecule, and it is shown that only a single head is bound to the microtubule between steps at low ATP concentrations.

Direct observation of single kinesin molecules moving along microtubules

A new assay is reported in which the processive movement of individual fluorescently labelled kinesin molecules along a microtubule can be visualized directly; this observation is achieved by low-background total internal reflection fluorescence microscopy in the absence of attachment of the motor to a cargo (for example, an organelle or bead).

Intracellular transport of single-headed molecular motors KIF1A.

A model of intracellular transport by interacting molecular motors that captures explicitly not only the effects of adenosine triphosphate hydrolysis, but also the ratchet mechanism which drives individual motors is developed.

Cytoplasmic dynein functions as a gear in response to load

This work uses an optical trap to quantify motion of polystyrene beads driven along microtubules by single cytoplasmic dynein motors and proposes a model whereby the gear is downshifted through load-induced binding of ATP at secondary sites in the Dynein head.

Kinesin Walks Hand-Over-Hand

The results suggest that kinesin is bound by both heads to the microtubule while it waits for adenosine triphosphate in between steps, and strongly support a hand-over-hand mechanism, and not an inchworm mechanism.

Overlapping hand-over-hand mechanism of single molecular motility of cytoplasmic dynein.

The step size and force produced by single molecules of active cytoplasmic dynein are measured by using an optical trap and fluorescence imaging with a high temporal resolution and the velocity of dyneIn movement, 800 nm/s, is consistent with that reported in cells.