A mechanochemical model of the forward/backward movement of motor protein kinesin-1.

ABSTRACT: Kinesin-1 is an ATP-driven, two-headed motor protein that transports intracellular cargoes (loads) along microtubules. The movement of kinesin-1 has generally been modeled according to its correlation with ATP cleavage (forward movement), synthesis (backward movement), or unproductive cleavage (futile consumption). Based on recent experimental observations, we formulate a mechanochemical model for this movement in which the forward/backward/futile cycle can be realized through multiple biochemical pathways. Our results show that the backward motion of kinesin-1 occurs mainly through backward sliding along the microtubule and is usually also coupled with ATP hydrolysis. We also found that with a low external load, about 80% of ATP is wasted (futile consumption) by kinesin-1. Furthermore, at

SUBMITTER: Shen B 

PROVIDER: S-EPMC9117889 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature