Force generation of KIF1C is impaired by pathogenic mutations.

ABSTRACT: Intracellular transport is essential for neuronal function and survival. The most effective plus-end-directed neuronal transporter is the kinesin-3 KIF1C, which transports large secretory vesicles and endosomes.^1-4 Mutations in KIF1C cause hereditary spastic paraplegia and cerebellar dysfunction in human patients.^5-8 In contrast to other kinesin-3s, KIF1C is a stable dimer and a highly processive motor in its native state.^9,10 Here, we establish a baseline for the single-molecule mechanics of Kif1C. We show that full-length KIF1C molecules can processively step against the load of an optical trap and reach average stall forces of 3.7 pN. Compared with kinesin-1, KIF1C has a higher propensity to slip backward under load, which results i

SUBMITTER: Siddiqui N 

PROVIDER: S-EPMC9631238 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature