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The kinesin-related protein MCAK is a microtubule depolymerase that forms an ATP-hydrolyzing complex at microtubule ends.
This work shows that MCAK is an ATPase that catalytically depolymerizes microtubules by accelerating, 100-fold, the rate of dissociation of tubulin from microtubule ends. Expand
Processivity of the Motor Protein Kinesin Requires Two Heads
At high ATP concentration, individual single-headed kinesin molecules detached from microtubules very slowly (at a rate less than one per second), 100-fold slower than the detachment during two-headed motility, which directly supports a coordinated, hand-over-hand model in which the rapid detachment of one head in the dimer is contingent on the binding of the second head. Expand
Kinesin’s tail domain is an inhibitory regulator of the motor domain
Both ATPase and motility assays indicate that the tail does not prevent kinesin from binding to microtubules, but rather reduces the motor’s stepping rate. Expand
Kinesin's processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains.
  • W. Hancock, J. Howard
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences…
  • 9 November 1999
A heterodimeric one-headed kinesin is engineered and its biochemical properties are compared to those of the wild-type two-headed molecule and a pathway is proposed that defines the chemical and mechanical cycle for two-heads kines in the ADP.P(i) state. Expand
Bidirectional cargo transport: moving beyond tug of war
  • W. Hancock
  • Biology, Medicine
  • Nature Reviews Molecular Cell Biology
  • 1 September 2014
Three classes of bidirectional transport models — microtubule tethering, mechanical activation and steric disinhibition — are proposed, and a general mathematical modelling framework forbidirectional cargo transport is put forward to guide future experiments. Expand
Neck Linker Length Determines the Degree of Processivity in Kinesin-1 and Kinesin-2 Motors
In low-ionic-strength buffer, charge had a dominant effect on motor processivity, which resolves ongoing controversy regarding the effect of neck linker length on kinesin processivity. Expand
The Processivity of Kinesin-2 Motors Suggests Diminished Front-Head Gating
Stochastic simulations of the kinesin-1 and kines in-2 hydrolysis cycles suggest that "front-head gating," in which rearward tension prevents ATP binding to the front head when both heads are bound to the microtubule, is diminished in kinesIn-2. Expand
The Mechanochemical Cycle of Mammalian Kinesin-2 KIF3A/B under Load
The response of motor proteins to external loads underlies their ability to work in teams and determines the net speed and directionality of cargo transport, and it is concluded that the force-dependent movement of KIF3A/B differs significantly from conventional kinesin-1. Expand
Kinetics of nucleotide-dependent structural transitions in the kinesin-1 hydrolysis cycle
It is shown that kinesin utilizes a two-step powerstroke mechanism to walk at maximum velocity and defines a consensus sequence of mechanochemical transitions that can be used to understand functional diversity across the kinesIn superfamily. Expand
Kinesin processivity is gated by phosphate release
It is shown that kinesin dissociation, which characterizes the end of a processive run, is gated by phosphate release following ATP hydrolysis, and the data suggest that, during processive movement, tethered-head binding occurs subsequent to hydroolysis, rather than immediately after ATP binding, as commonly suggested. Expand