2026-04-03T22:04:02Zhttps://recercat.cat/oai/request

oai:recercat.cat:2445/1333202025-11-19T20:28:05Zcom_2072_1057col_2072_478822col_2072_478917

00925njm 22002777a 4500 dc Oriola Santandreu, David author Casademunt i Viader, Jaume author 2019-05-16T13:36:15Z 2019-05-16T13:36:15Z 2013-07-26 2019-05-16T13:36:15Z KIF1A is a kinesin motor protein that can work processively in a monomeric (single-headed) form by using a noise-driven ratchet mechanism. Here, we show that the combination of a passive diffusive state and finite-time kinetics of adenosine triphosphate hydrolysis provides a powerful mechanism of cooperative force generation, implying for instance that ∼ 10 monomeric KIF1As can team up to become ∼ 100 times stronger than a single one. Consequently, we propose that KIF1A could outperform conventional (double-headed) kinesin collectively and thus explain its specificity in axonal trafficking. We elucidate the cooperativity mechanism with a lattice model that includes multiparticle transitions. Proteïnes quinases Monòmers Protein kinases Monomers Cooperative force generation of KIF1A Brownian motors