Biased movement of monomeric kinesin-3 KLP-6 explained by a symmetric Brownian ratchet model.

ABSTRACT: Most kinesin molecular motors dimerize to move processively and efficiently along microtubules; however, some can maintain processivity even in a monomeric state. Previous studies have suggested that asymmetric potentials between the motor domain and microtubules underlie this motility. In this study, we demonstrate that the kinesin-3 family motor protein KLP-6 can move forward along microtubules as a monomer upon release of autoinhibition. This motility can be explained by a change in length between the head and tail, rather than by asymmetric potentials. Using mass photometry and single-molecule assays, we confirmed that activated full-length KLP-6 is monomeric both in solution and on microtubules. KLP-6 possesses a microtubule-binding tail domain, and its motor domain does not exhibit b

SUBMITTER: Kita T 

PROVIDER: S-EPMC11739925 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature