Work

Kinesin-1 is highly flexible and adopts an open conformation in the absence of cargo

Year: 2026

Type: article

Abstract: Kinesin-1 is an essential anterograde microtubule motor protein. The core kinesin motor is a homodimer of two heavy chains; N-terminal motor domains hydrolyze ATP and walk along microtubules, while a long elongated coiled-coil stalk and an intrinsically disordered C-terminal tail region bind cargos. Kinesin autoinhibition is key to preventing futile ATP consumption and occurs, at least in part, through direct interactions between N-terminal motor domains and C-terminal inhibitory motifs. Despite significant advances in our understanding of kinesin walking, little is known about the kinesin-1 conformational landscape of the stalk and tail domains. Here, we apply solution-based biophysical analysis tools to study conformational changes in kinesin-1, with full rotational freedom, and in response to changes in ionic strength, mutations, and the presence of microtubules. This has allowed us to uncover the inherent flexibility in kinesin-1, which gives insights into autoinhibition and the regulation of intracellular transport.

Source: iScience

DOI: 10.1016/j.isci.2026.114875

Authors: Evelyn R. Smith, Emma D. Turner, Mahmoud A.S. Abdelhamid, Timothy D. Craggs, Alison E. Twelvetrees

Institution: University of Sheffield

Language: English

Topic: Microtubule and mitosis dynamics

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $3,240