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• W3048758476 abstract "Kinesin-1 molecular motors are walking machines that step along microtubules. Their stepping action is heavily biased towards MT plus ends, but backsteps also occur, at a rate that depends on the load and the ATP concentration. Like forward steps, backsteps are typically 8nm, but larger backwards events also occur. These larger backwards events are thought to be slips rather than steps, because they are too fast to be composed of multiple, conventionally-coupled 8nm steps. Here we propose that not just these larger events, but all kinesin-1 backsteps, are slips. We find (1) that kinesin waits before forward steps for less time than before backsteps and detachments, (2) that kinesin waits for the same amount of time before backsteps and detachments, (3) that shifting kinesin from one type of MT lattice to another shifts the ratio of backsteps and detachments, without affecting forward stepping. Our findings indicate that forward kinesin steps originate from an earlier state in the mechanism than backsteps. Accordingly, we propose a revised scheme in which load-dependent ATP binding to the trailing kinesin head opens a time window devoted to ATP hydrolysis and forward stepping, whilst Pi release closes this window, creating a K.ADP.K.ADP state that can slip back along the MT, re-engage, release ADP, and retry ATP-driven forward stepping." @default.
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• W3048758476 date "2020-04-07" @default.
• W3048758476 modified "2023-09-24" @default.
• W3048758476 title "Proposed pathway for kinesin backstepping" @default.
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