Regulation of kinesin-2 motility by its β-hairpin motif.

ABSTRACT: Members of the kinesin-2 family coordinate with other motors to power diverse physiological processes, but the structural mechanisms regulating kinesin-2 activity have been unknown. Distinctively, kinesin-2s canonically function as heterotrimers of two different motor subunits (for example Kif3A and Kif3B in humans) and Kap3, but the role of heterotrimerization has yet to fully emerge. Here, we combine structural, cell biological and single-molecule approaches to dissect kinesin-2 regulation as a heterodimer, heterotrimer and quaternary complex with a cargo adaptor (APC). We identify a conserved motif in the tail of kinesin-2s (the β-hairpin motif) that, in conjunction with the adjacent coiled coil, controls kinesin-2 motility by sequestering the motor domains away from their microtubule t

SUBMITTER: Webb S 

PROVIDER: S-EPMC12527917 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature