2026-04-03T22:04:19Zhttps://recercat.cat/oai/requestoai:recercat.cat:2445/1333202025-11-19T20:28:05Zcom_2072_1057col_2072_478822col_2072_478917
RECERCAT
author
Oriola Santandreu, David
author
Casademunt i Viader, Jaume
2019-05-16T13:36:15Z2019-05-16T13:36:15Z2013-07-262019-05-16T13:36:15Z
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.
(c) American Physical Society, 2013 info:eu-repo/semantics/openAccess
Proteïnes quinases
Monòmers
Protein kinases
Monomers
Cooperative force generation of KIF1A Brownian motors
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion