Microtubule minus-end aster organization is driven by processive HSET-tubulin clusters

Stephen R. Norris, Seungyeon Jung, Prashant Singh, Claire E. Strothman, Amanda L. Erwin, Melanie D. Ohi, Marija Zanic () and Ryoma Ohi ()
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Stephen R. Norris: Vanderbilt University
Seungyeon Jung: Vanderbilt University
Prashant Singh: Vanderbilt University
Claire E. Strothman: Vanderbilt University
Amanda L. Erwin: Vanderbilt University
Melanie D. Ohi: Vanderbilt University
Marija Zanic: Vanderbilt University
Ryoma Ohi: Vanderbilt University

Nature Communications, 2018, vol. 9, issue 1, 1-14

Abstract: Abstract Higher-order structures of the microtubule (MT) cytoskeleton are comprised of two architectures: bundles and asters. Although both architectures are critical for cellular function, the molecular pathways that drive aster formation are poorly understood. Here, we study aster formation by human minus-end-directed kinesin-14 (HSET/KIFC1). We show that HSET is incapable of forming asters from preformed, nongrowing MTs, but rapidly forms MT asters in the presence of soluble (non-MT) tubulin. HSET binds soluble (non-MT) tubulin via its N-terminal tail domain to form heterogeneous HSET-tubulin clusters containing multiple motors. Cluster formation induces motor processivity and rescues the formation of asters from nongrowing MTs. We then show that excess soluble (non-MT) tubulin stimulates aster formation in HeLa cells overexpressing HSET during mitosis. We propose a model where HSET can toggle between MT bundle and aster formation in a manner governed by the availability of soluble (non-MT) tubulin.

Date: 2018
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04991-2

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DOI: 10.1038/s41467-018-04991-2

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